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MAb ID	447-52D (447/52-DII, 447-52-D, 447d, 447-52-D, 447-D, 447, 447D, 447D-52)
HXB2 Location	gp160(312-315) DNA(7158..7169)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Dr. Susan Zolla-Pazner, NYU Med Center NY, NY; Veteran Affairs Med Center NY, NY; or Cellular Products Inc, Buffalo, NY,
Epitope	GPGR	Epitope Alignment
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L P  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG3λ)
Patient
Immunogen	HIV-1 infection
Keywords	acute/early infection, ADCC, antibody binding site, antibody generation, antibody interactions, antibody lineage, antibody sequence, assay or method development, binding affinity, broad neutralizer, co-receptor, complement, computational epitope prediction, dendritic cells, dynamics, elite controllers, enhancing activity, escape, genital and mucosal immunity, glycosylation, HIV-2, kinetics, mimics, mimotopes, neutralization, optimal epitope, polyclonal antibodies, review, SIV, structure, subtype comparisons, supervised treatment interruptions (STI), Th2, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity, viral fitness and reversion

Notes

Showing 219 of 219 notes.

• 447-52d: An R5 virus isolated from chronic patient NAB01 (Patient Record# 4723) was adapted in culture to growth in the presence of target cells expressing reduced levels of CD4. Entry kinetics of the virus were altered, and these alterations resulted in extended exposure of CD4-induced neutralization-sensitive epitopes to CD4. Adapted and control viruses were assayed for their neutralization by a panel of neutralizing antibodies targeting several different regions of Env (PGT121, PGT128, 1-79, 447-52d, b6, b12, VRC01, 17b, 4E10, 2F5, Z13e1). Adapted viruses showed greater sensitivity to antibodies targeting the CD4 binding site and the V3 loop. This evolution of Env resulted in increased CD4 affinity but decreased viral fitness, a phenomenon seen also in the immune-privileged CNS, particularly in macrophages. Beauparlant2017 (neutralization, viral fitness and reversion, dynamics, kinetics)
• 447-52D: Three vaccine regimens administered in guinea pigs over 200 weeks were compared for ability to elicit NAb polyclonal sera. While tier 1 NAb responses did increase with vaccination, tier 2 NAb heterologous responses did not. The 3 regimens were C97 (monovalent, Clade C gp140), 4C (tetravalent, 4 Clade C mosaic gp140s), ABCM (tetravalent, Clades A, B, C and mosaic gp140s). Polyclonal sera generated from the 4C regimen, compared to the C97 regimen, was markedly superior at outcompeting 447-52D binding to gp140 antigens, suggesting that the 4C regimen induced the most robust V3-specific antibodies. Bricault2018 (antibody generation, vaccine-induced immune responses, polyclonal antibodies)
• 447-52D: The authors mutated two conserved tyrosine (Y) residues within the V2 loop of gp120 Y177 and Y173, individually or in combination, by replacing them with either phenylalanine (F) or alanine (A) in a clade B, tier 1B HIV-1 Env protein (BaL), and in a number of tier 2 HIV-1 Envs from different clades, namely, BG505 (clade A), JR-FL and JR-CSF (clade B), and CM244 (clade E). A consistent hierarchy of neutralization sensitivity was seen among the mutants, with a greater impact of Y177 over Y173 single mutations, of double over single mutations, and of A over F substitutions. The double-alanine mutation in mutant HIV-1 BaL, Y173A Y177A, increased sensitivity to all the weakly neutralizing MAbs tested and even rendered the virus sensitive to non-neutralizing antibodies against the CD4 binding site, such as F105, 654-30D, and b13. When tested against bNAbs instead, there was a trend to decrease neutralization sensitivity compared to WT, with the exception of N6, PGT151, 10E8, and 2G12, for which there was no change, and of 2F5 and 4E10, which were more effective against the mutant compared to the WT. Guzzo2018 (antibody binding site, binding affinity)
• 447-52D: The authors selected an optimal panel of diverse HIV-1 envelope glycoproteins to represent the antigenic diversity of HIV globally in order to be used as antigen candidates. The selection was based on genetic and geographic diversity, and experimentally and computationally evaluated humoral responses. The eligibility of the envelopes as vaccine candidates was evaluated against a panel of antibodies for breadth, affinity, binding and durability of vaccine-elicited responses. The antigen panel was capable of detecting the spectrum of V2-specific antibodies that target epitopes from the V2 strand C (V2p), the integrin binding motif in V2 (V2i), and the quaternary epitope at the apex of the trimer (V2q). Yates2018 (vaccine antigen design, vaccine-induced immune responses, binding affinity)
• 447-52D: A systems glycobiology approach was applied to reverse engineer the relationship between bNAb binding and glycan effects on Env proteins. Glycan occupancy was interrogated across every potential N-glycan site in 94 recombinant gp120 antigens. Using a Bayesian machine learning algorithm, bNAb-specific glycan footprints were identified and used to design antigens that selectively alter bNAb antigenicity. The novel synthesized antigens uccessfully bound to target bNAbs with enhanced and selective antigenicity. Yu2018 (glycosylation, vaccine antigen design)
• 447-52D: The immunologic effects of mutations in the Env cytoplasmic tail (CT) that included increased surface expression were explored using a vaccinia prime/protein boost protocol in mice. After vaccinia primes, CT- modified Envs induced up to 7-fold higher gp120-specific IgG, and after gp120 protein boosts, they elicited up to 16-fold greater Tier-1 HIV-1 neutralizing antibody titers. Envs with or without the TM1 mutations were expressed in HEK 293T cells and analyzed for the relative expression of Ab epitopes including V3 loop crown for 447-52D. Hogan2018 (vaccine antigen design)
• 447-52D: SOSIP.664 trimer was modified at V3 positions 306 and 308 by Leucine substitution to create hydrophobic interactions with the tryptophan residue at position 316 and the V1V2 domain. These modifications stabilized the resulting SOSIP.v5.2 S306L R308L trimers. In vivo, the induction of V3 non-NAbs was significantly reduced compared with the SOSIP.v5.2 trimers. With S306L plus R308L substitutions 447-52D did not bind to SOSIP.v5.2 and SOSIP.v5.2 constructs. deTaeye2018 (broad neutralizer)
• 447-52D: Three strategies were applied to perturb the structure of Env in order to make the protein more susceptible to neutralization: exposure to cold, Env-activating ligands, and a chaotropic agent. A panel of mAbs (E51, 48d, 17b, 3BNC176, 19b, 447-52D, 39F, b12, b6, PG16, PGT145, PGT126, 35O22, F240, 10E8, 7b2, 2G12) was used to test the neutralization resistance of a panel of subtype B and C pseudoviruses with and without these agents. Both cold and CD4 mimicking agents (CD4Ms) increased the sensitivity of some viruses. The chaotropic agent urea had little effect by itself, but could enhance the effects of cold or CD4Ms. Thus Env destabilizing agents can make Env more susceptible to neutralization and may hold promise as priming vaccine antigens. Johnson2017 (vaccine antigen design)
• 447-52D: Env from of a highly neutralization-resistant isolate, CH120.6, was shown to be very stable and conformationally-homogeneous. Its gp140 trimer retains many antigenic properties of the intact Env, while its monomeric gp120 exposes more epitopes. Thus trimer organization and stability are important determinants for occluding epitopes and conferring resistance to antibodies. Among a panel of 21 mAbs, CH120.6 was resistant to neutralization by all non-neutralizing and strain-specific mAbs (including 447-52D), regardless of the location of their epitopes. It was weakly neutralized by several broadly-neutralizing mAbs (VRC01, NIH45-46, 12A12, PG9, PG16, PGT128, 4E10, and 10E8), and well neutralized by only 2 (PGT145 and 10-1074). Cai2017 (neutralization)
• 447-52D: PGT145 was used to positively isolate a subtype B Env trimer immunogen, B41 SOSIP.664, that exists in two conformations, closed and partially open. bNAbs tested against the trimer were able to neutralize the B41 pseudovirus with a wide range of potencies. Among non-NAbs to CD4bs (b6, F91, F105); to CD4i (17b); to gp41_ECTO (F240); and to V3 (447-52D, 39F, CO11, 19b and 14e), none neutralized B41 (IC₅₀ >50µg/ml). Pugach2015
• 447-52D: A new trimeric immunogen, BG505 SOSIP.664 gp140, was developed that bound and activated most known neutralizing antibodies but generally did not bind antibodies lacking neuralizing activity. This highly stable immunogen mimics the Env spike of subtype A transmitted/founder (T/F) HIV-1 strain, BG505. Anti-V3 non-NAb 447-52D did not neutralize BG505.T332N, the pseudoviral equivalent of the immunogen BG505 SOSIP.664 gp140, and did not recognize or bind the immunogen either. Sanders2013 (assay or method development, neutralization, binding affinity)
• 447-52D: The study's goal was to produce modified SOSIP trimers that would reduce the exposure - and, by inference, the immunogenicity - of non-NAb epitopes such as V3. The binding of several modified SOSIP trimers was compared among 12 neutralizing (PG9, PG16, PGT145, PGT121, PGT126, 2G12, PGT135, VRC01, CH103, CD4, IgG2, PGT151, 35O22) and 3 non-neutralizing antibodies (14e, 19b, b6). The V3 non-NAbs 447-52D, 39F, 14e, and 19b bound less well to all A316W variant trimers compared to wild-type trimers. Mice and rabbits immunized with modified, stabilized SOSIP trimers developed fewer V3 Ab responses than those immunized with native trimers. deTaeye2015 (antibody binding site)
• 447D: The study compared various factors affecting the accessibility of epitopes for antibodies targeting the V2 integrin (V2i) region, versus the V3 region. CD4 treament of BaL and JRFL pseudoviruses increased their neutralization sensitivity to V3 MAbs, but not to V2i MAbs. Viruses grown in a glycosidase inhibitor were more sensitive to neutralization by V3, but not V2i, MAbs. Increasing the time of virus-MAb interaction increased virus neutralization by some V2i MAbs and all V3 MAbs. The structural dynamics of V2i and V3 epitopes has important effects in neutralization. The V3 MAbs tested were: 447, 2219, and 2557. Upadhyay2014 (glycosylation, neutralization)
• 447-52D: A computational method, MDE, predicts the presence of neutralization epitopes in the V3 loop solely from the viral sequence and the crystal structure of the antibody. For V3-specific mAbs 2219 and 447-52D, the method accurately predicted the presence of neutralization epitopes in diverse strains of HIV-1. Identification of Ab-targeted neutralization epitopes in silico enables easy prediction of the reactivity of specific mAbs across diverse variants, and facilitates rational design of immunogens. Shmelkov2014 (computational epitope prediction)
• 447-52D: This study proposes a mimotope model of the V3 crown epitope in which the PR-L and GPG sequences represent the two known epitope binding sites. Rabbit serum to these mimotopes recognized the V3 peptides and moderately decreased the fusion between HIV-1 Env- and CD4-expressing Jurkat cells. MAb 447-52D has been used as V3 epitope core recognizing Ab. The most intriguing characteristic of this mimotope model of the V3 epitope is the absence of the arginine at the position next to the GPG, which offers the flexibility of this phage-displayed linear peptide affecting the correct interaction between the epitope and the antibody tolerating substitutions of the GPG amino acids. Gazarian2013 (mimotopes)
• 447-52D: Study evaluated 4 gp140 Env protein vaccine immunogens derived from an elite neutralizer donor VC10042, an HIV+ African American male from Vanderbilt cohort. Env immunogens, VC10042.05, VC10042.05RM, VC10042.08 and VC10042.ela, elicited high titers of cross-reactive Abs recognizing V1/V2 regions. 447-52D bound to all 4 trimeric Env. Carbonetti2014 (elite controllers, vaccine-induced immune responses)
• 447-52D: This study showed that the inability of Env to elicit the production of broadly neutralizing Abs is due to the inability of diverse Env to engage the germ line B cell receptor forms of known bNAbs. 447-52D bound to all the Envs tested except the clade B REJO, the consensus A1 sequence, the clade 405c, and the clade A/E A244. The predicted germ line version of 447-52D did not exhibit any detectable binding against these Envs. Ca²⁺ influx through the 447-52D BCR was also tested as a function of binding affinity. Removal of selected N-linked glycosylaion sites on Env did not confer binding to the predicted germline 447-52D. McGuire2014 (antibody interactions, antibody lineage)
• 447-52D: Describes the mutagenesis of plasmid P5Q (a scFv antibody derived from mAb 447). Cites the original mAb 447 as first described by Buchbinder et al. 1992. Lewis1995 (binding affinity, antibody sequence)
• 447-52D: The sera of 20 HIV-1 patients were screened for ADCC in a novel assay measuring granzyme B (GrB) and T cell elimination and reported that complex sera mediated greater levels of ADCC than anti-HIV mAbs. The data suggested that total amount of IgG bound is an important determinant of robust ADCC which improves the vaccine potency. 447-52D was used as an anti-V3 Ab to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets. Smalls-Mantey2012 (ADCC, assay or method development)
• 447-52D: Somatic hypermutations are preferably found in CDR loops, which alter the Ab combining sites, but not the overall structure of the variable domain. FWR of CDR are usually resistant to and less tolerant of mutations. This study reports that most bnAbs require somatic mutations in the FWRs which provide flexibility, increasing Ab breadth and potency. To determine the consequence of FWR mutations the framework residues were reverted to the Ab's germline counterpart (FWR-GL) and binding and neutralizing properties were then evaluated. 447-52D had limited neutralizing activity recognizing the V3 loop and carried fewer somatic mutations than bnAbs. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 447-52D. Klein2013 (neutralization, structure, antibody lineage)
• 447-52D: Polyclonal B cell responses to conserved neutralization epitopes are reported. Cross-reactive plasma samples were identified and evaluated from 308 subjects tested. 447-52D was used as a control mAb in the comprehensive set of assays performed. Tomaras2011 (neutralization, polyclonal antibodies)
• 447-52D: The role of V1V2 in the resistance of HIV-1 to neutralizing Abs was studied using a panel of neutralization-sensitive and -resistant HIV-1 variants and through exchanging regions of Env between neutralization-sensitive and -resistant viruses. An increase in the length of the V1V2 loop and/or the number of potential N-linked glycosylation sites (PNGS) in that same region of Env was directly involved in the neutralization resistance. The introduction of a shorter V1V2 loop from historical seroconverters into the background of Env of HIV-1 from contemporary seroconverters resulted in significant increase in neutralization sensitivity to MAb 447-52D. vanGils2011 (glycosylation, neutralization, escape)
• 447-52D: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors. Blocking the binding of the NAb to the FcRs present on the cell surface of the DCs reduced the inhibitory activity of the IgG 447-52D. Finally, nonneutralizing inhibitory action of 447-52D Fab fragments 240D and 246D 246D, which do not exhibit neutralizing activity on PBMCs, reduced the number of HIV-1BaL-infected LCs and IDCs by 90%. Peressin2011 (genital and mucosal immunity, dendritic cells)
• 447-52D: Small sized CD4 mimetics (miniCD4s) were engineered. These miniCD4s by themselves are poorly immunogenic and do not induce anti-CD4 antibodies. Stable covalent complexes between miniCD4s and gp120 and gp140 were generated through a site-directed coupling reaction. These complexes were recognized by CD4i antibodies as well as by the HIV co-receptor CCR5 and elicited CD4i antibody responses in rabbits. A panel of MAbs of defined epitope specificities was used to analyze the antigenic integrity of the covalent complexes using capture ELISA. Binding of the cross-linked complex on 447-52D or MN 215 was increased compared with that of gp140 alone. Martin2011 (mimics, binding affinity)
• 447-52D: Signature motifs specific for neutralization epitopes present in the V3 loop crown were used to determine the presence or absence of MAb-specific epitopes in vaccine immunogens and in break-through viruses infecting vaccine and placebo recipients in the VAX003 and VAX004 Phase III clinical trials. Of the six epitopes present in the immunogens and targeted by known NAbs, only the one targeted by anti-V3 NAb 2219 exhibited a significant reduction in occurrence in vaccinated subjects from VAX003 Thailand cohort compared to the placebo group. The signature motif used for MAb 447-52D is P16, R18 in V3-loop position numbers. Shmelkov2011 (vaccine-induced immune responses)
• 447-52D: The long-term effect of broadly bNAbs on cell-free HIV particles and their capacity to irreversibly inactivate virus was studied. MPER-specific MAbs potently induced gp120 shedding upon prolonged contact with the virus, rendering neutralization irreversible. The kinetic and thermodynamic requirements of the shedding process were virtually identical to those of neutralization, identifying gp120 shedding as a key process associated with HIV neutralization by MPER bNAbs. Neutralizing and shedding capacity of 7 MPER-, CD4bs- and V3 loop-directed MAbs were assessed against 14 divergent strains. 447-52D induced potent shedding that correlated with its neutralization activity. Ruprecht2011 (neutralization, kinetics)
• 447-52D: Closely related HIV-1 B clade Envs from a pediatric subject in a late disease differed in their capacity to infect primary macrophages. E153G conferred high levels of macrophage infectivity for several heterologous R5 envelopes, while the reciprocal G153E substitution abrogated infection. Shifts in macrophage tropism were associated with dramatic shifts in sensitivity to the V3 loop MAb 447-52D and soluble CD4, as well as more modest changes in sensitivity to the CD4bs MAb, b12. Musich2011 (escape)
• 447-52D: This study analyzed the neutralization sensitivity of sequential HIV-1 primary isolates during their natural evolution in 5 subtype B and CRF02_AG HIV-1 infected drug naive individuals to 13 anti-HIV-1 MAbs (including this MAb) directed at epitopes in the V2, V3, CD4bd and carbohydrates. Patient viruses evolved to become more sensitive to neutralization by MAbs directed at epitopes at V2, V3 and CDbd, indicating that cross sectional studies are inadequate to define the neutralization spectrum of MAb neutralization with primary HIV-1 isolates. Haldar2011 (neutralization)
• 447-52D: A way to produce conformationally intact, deglycosylated soluble, cleaved recombinant Env trimers by inhibition of the synthesis of complex N-glycans during Env production, followed by treatment with glycosidases under conditions that preserve Env trimer integrity is described to facilitate crystallography and immunogenicity studies. MAb 447–52D bound more strongly to deglycosylated trimers than untreated ones. Depetris2012 (glycosylation, binding affinity)
• 447-52D: Masking signatures were developed and analyzed for 4 anti-HIV V3 loop MAbs, 2219, 3074, 2557, 447-52D. The epitopes were classified as "masked" if their signature motifs were present in a virus, but there was no detectible neutralization by the MAb of the same virus in vitro. The signature motif for MAb 2219 used in the study was R9+K10+[l,V]12+[Y,F]21. Of the 4 MAbs, 2219 neutralized the largest number of pseudoviruses containing its epitope. The 2219 neutralization epitope is unmasked in 25/68 (36.8%) of the viruses containing the 2219 epitope. Agarwal2011 (neutralization)
• 447-52D: One Env clone (4–2.J45) obtained from a recently infected Indian patient (NARI-IVC4) had exceptional neutralization sensitivity compared to other Envs obtained at the same time point from the same patient. The effect of I424M substitution in three clade B Envs (RHPA4259.7, JRFL and YU2) was tested and 2-45-fold increase was found in their sensitivities to anti-V3 MAbs including 447-52D. Ringe2011 (neutralization)
• 447-52D: Several soluble gp140 Env proteins recognized by PG9 and PG16 were identified, and the effect of Env trimerization, the requirement for specific amino acids at position 160 within the V2 loop, and the importance of proper gp120-gp41 cleavage for MAb binding to soluble gp140s were investigated along with whether and how the kinetics of PG9 and PG16 binding to soluble gp140 correlates with the neutralizing potencies of these MAbs. In some cases the affinities of PG9/PG16 binding were comparable to those of 447-52D. Lower binding affinity of gp140 ligands to PG9/PG16 than 447D was observed. 447-52D binds to an epitope within the V3 loop of gp120 and interacts very efficiently with monomeric gp120. 447-52D also bound to all clade A Env gp140s tested. The anti-SF162 neutralizing activity of 447-52D decreased when the lysine at position 160 was replaced by an asparagine. Davenport2011 (neutralization, binding affinity)
• 447-52D: The location and extent of conservation of eight protease cleavage sites on HIV-1 gp120 recognized by 3 major human proteases (cathepsins L, S and D) are described along with the effect of cathepsin cleavage on gp120 binding to CD4-IgG and NAbs. 447-52D binding was destroyed with cathepsin L-treated gp120 but preserved with cathepsin D-treated gp120. Yu2010 (binding affinity)
• 447-52D: This review discusses current understanding of Env neutralization by antibodies in relation to epitope exposure and how this insight might benefit vaccine design strategies. This MAb is in the list of current MAbs with notable cross-neutralizing activity. Pantophlet2010 (neutralization, variant cross-reactivity, review)
• 447-52D: This review outlines the general structure of the gp160 viral envelope, the dynamics of viral entry, the evolution of humoral response, the mechanisms of viral escape and the characterization of broadly neutralizing Abs. It is noted that this MAb predominantly neutralizes clade B viruses and occasionally neutralizes some viruses from non-B clades. Gonzalez2010 (neutralization, variant cross-reactivity, escape, review)
• 447-52D: The expression and characterization of different glycoforms of V3-Fc fusion protein along with its binding to HIV-neutralizing Abs 2G12 and 447-52D was examined. The binding affinity of 447-52D was high for complex type glycoform V3-Fc-CT and high-mannose type glycoforms of V3-Fc (V3-Fc-HM, V3-Fc-M9 and the two mutants:N301A and Fc-N297A) following a quick association/dissociation kinetic process but it was higher for gp120 with extremely slow dissociation process. The affinity to 447-52D was not significantly affected by removal of the N-glycans at the N297, N301 and N332 sites. Yang2010a (glycosylation, binding affinity)
• 447-D52: This paper shows that a highly neutralization-resistant virus is converted to a neutralization sensitive virus with a rare single mutation D179N in the C-terminal portion of the V2 domain for several antibodies. 447D-52, however, did not neutralize any of the mutants tested. ORourke2010 (neutralization, variant cross-reactivity)
• 447-52D: A side-by-side comparison was performed on the quality of Ab responses in humans elicited by three vaccine studies focusing on Env-specific Abs. V3 Abs with specificities similar to that of 447-52D were elicited nearly ubiquitously in all of the vaccine sera tested, where the sera were able to outcompete binding to 447-52D. Vaine2010 (antibody interactions)
• 447-52D: Structure of 447-52D bound to a peptide containing the sequence of the V3 loop was used to derive sensitive and specific signature motifs for its neutralization epitope. 447-52D epitope (¹⁶PxR¹⁸) was found conserved in 11% of circulating HIV-1 strains, and was highly restricted to subtype B strains. 447-52D neutralized 9% of subtype A pseudovirions, 47% of subtype B, 4% of subtype C, 10% of subtype D and 0% of CRF02_AG. Swetnam2010 (antibody binding site, neutralization, variant cross-reactivity, subtype comparisons, structure)
• 447-52D: Peptide ligands for CD4i epitopes on native dualtropic Envs were selected by phage display. The correct exposure of CD4i epitopes was detected by binding with MAb 447-52D, which bound both in the presence or absence of sCD4. Dervillez2010 (binding affinity)
• 447-52D: Impact of in vivo Env-CD4 interactions was studied during vaccinations of Rhesus macaques with two Env trimer variants rendered CD4 binding defective (368D/R and 423/425/431 trimers) and wild-type (WT) trimers. Ab binding profiles of the three trimer variants were assessed by binding analyses to different MAbs. V3-directed MAb 447-52D bound similarly to all three trimer variants: WT and 368D/R, and 423/425/431. Douagi2010 (binding affinity)
• 447-52D: The effect of presence and absence of V1 loop was assessed using two approaches: remove V1 loop from the soluble trimeric gp140 construct (ΔV1SF162gp140) and second, substitute the V1 loop on SF162gp140 construct with four different V1 loops from 89.6, YU2, JRFL, and HxB2 (heterologous HIV-1 viruses). Deletion or substitution of V1 loop increased resistance to neutralization by 447-52D in 3 out of 5 V1-modified gp140 constructs, although it did not affect the binding to 447-52D. D368R modification to SF162gp120 did not affect the binding to 447-52D but there was a decrease in neutralization activity by 447-52D. Ching2010 (neutralization, binding affinity)
• 447-52d: Clustering analysis was performed to find patterns of neutralization reactivity for the dataset of 103 patients sera against 20 viruses. The clustering by five MAbs (including 447-52d) against the 20 isolates was less statistically robust than that with serum titers, resulting in three clusters for both cases. The membership in an isolate cluster defined by serum titers was compared with its sensitivity to every MAb to understand the relationship of serum and MAb reactivity. Membership in two out of three clusters did not correlate with sensitivity to 447-52d. Doria-Rose2010 (neutralization)
• 447: 447 neutralizing activity was assessed against pseudoviruses expressing Envs of diverse HIV-1 subtypes from subjects with acute and chronic infection. IC50 neutralization activity was also statistically assessed based on the area under the neutralization curves (AUC). 447 was able to neutralize 6/57 viruses in U87-based assay and 12/41 viruses in TZM-based assay, including Tier 1 and Tier 2 viruses, viruses of subtypes A, B, C, AG, and viruses from both chronic and acute infections. AUC analysis revealed that 15/57 viruses in the U87-based assay, and 12/41 viruses in the TZM-based assay, were significantly neutralized by this Ab. Thus, the AUC method has the ability to detect low levels of neutralizing activity that otherwise may be missed. Hioe2010 (assay or method development, neutralization, variant cross-reactivity)
• 447-52D: A set of Env variants with deletions in V1/V2 was constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Sensitivity of the evolved ΔV1V2 viruses was evaluated to study accessibility of their neutralization epitopes. 447-52D neutralized all ΔV1V2 variants more potently than wild type virus, indicating better exposure of the 447-52D epitope when V1V2 domain is removed. Bontjer2010 (neutralization)
• 447-52D: This review discusses recent research done to improve the production, quality, and cross-reactivity of binding Abs, neutralizing Abs, monoclonal Abs with broad neutralizing activity, antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-dependent cell-mediated viral inhibition (ADCVI), and catalytic Abs. Studies focusing on several aspects of BNAb roles in vaccine development, and studies done to better understand the broad binding capacity of BNAbs are reviewed. Baum2010 (ADCC, neutralization, review)
• 447-52D: GnTI virus (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps), and the N301Q mutant virus (glycan at position 301 is removed), were both significantly more sensitive to neutralization by 447-52D compared to the parental virus. This suggests that the antennae of the complex glycans play a significant role in protecting the V3 loop from Ab binding. Binley2010 (glycosylation, neutralization)
• 447: This human Ab was compared to MAbs 2.2G, 2.3E, 2.5B derived from B-cell cultures from SHIV-infected rhesus macaques and human MAbs 2909, 830A and sCD4. 447 blocked the capture of virions by MAbs 2.2G, 2.3E, 2.5B and human MAb 2909. 447 capture of virions was partially blocked by 2909 and 830A and not blocked by sCD4. Robinson2010 (binding affinity)
• 447: Two V3-scaffold immunogen constructs were designed and expressed using 3D structures of cholera toxin B (CTB), V3 in the gp120 context, and V3 bound to 447-52D MAb. The construct (V3-CTB) presenting the complete V3 was recognized by 447-52D and by the large majority of other MAbs (18/24), indicating correctly folded and exposed MAb epitopes. V3-CTB induced V3-binding Abs and Abs displaying cross-clade neutralizing activity in immunized rabbits. Short V3-CTB construct, presenting a V3 fragment in conformation observed in complex with 447-52D, showed high affinity binding to 447-52D. Few other MAbs retained the same binding affinities for this construct as for the V3-CTB, indicating that they utilize a binding mode similar to that of 447-52D. Totrov2010 (vaccine antigen design, binding affinity, structure)
• 447-52D: A panel of 109 HIV-1 pseudoviruses was assessed for neutralization sensitivities to 447-52D MAb and patient plasma pools from genetically diverse HIV-1 positive samples. Clustering analyses revealed that the 109 viruses could be divided to 4 sub-groups, based on their neutralization sensitivity to the plasma pools: very high (Tier 1A), above-average (Tier 1B), moderate (Tier 2), and low (Tier 3) sensitivity. 3 Tier 1A, 7 Tier 1B, 3 Tier 2 and 1 Tier 3 viruses were found to be sensitive to neutralization by 447-52D. Seaman2010 (neutralization)
• 447-52D: Neutralizing sensitivity of L669S gp41 mutant virus to 447-52D increased ∼169-fold compared to the wild type virus, indicating that conformational changes in the MPER could alter the exposure of neutralization epitopes in other regions of HIV-1 Env. Shen2010 (neutralization)
• 447-52D: Neutralization potency of 447-52D was compared to that of HK20 scFv in TZM-based assay using 45 Tier 1 and Tier 2 HIV isolates. 447-52D neutralized 6/45 isolates. Sabin2010 (neutralization, variant cross-reactivity)
• 447-52D: Crystal structures of 2219, 2557, 1006-15D and 3074 MAbs in complex with V3 peptides revealed that these MAbs bind to conserved elements in four regions of the V3: the arch, the circlet, the band, and the V3 peptide main chain backbone. A mimotope that preserved the key structural elements in the circlet and band regions, but with GPG of the arch replaced by a disulfide bond, interacted with broadly reactive MAbs 2557, 1006 and 2219. It did not react with 447-52D nor 268-D, which are dependent on the Arg in the arch. Thus, mimotopes can be constructed that may focus the immune response on structurally conserved elements. Jiang2010 (antibody binding site, mimotopes, structure)
• 447-52D: B cell depletion in an HIV-1 infected patient using rituximab led to a decline in NAb titers and rising viral load. Recovery of NAb titers resulted in control of viral load, and the newly emerged virus population was examined. Strong binding competition between patient sera and 447-52D was observed. Huang2010 (antibody interactions)
• 447-52D: Binding affinity of 447-52D to a minimal peptide was 2-fold weaker than binding of this Ab to gp140 monomers and trimers. The opposite was observed for MAb 4E10. Xu2010 (binding affinity)
• 447-52D: 447-52D ability to bind different Env trimers and its neutralization breadth are reviewed. This review also summarizes data on the evolution of HIV neutralizing Abs, principles of Env immunogen design to elicit broadly neutralizing Abs, and future critical areas of research for development of an Ab-based HIV vaccine. Hoxie2010 (vaccine antigen design, review)
• 447-52D: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 447-52D neutralization activity was compared to the three new broadly neutralizing mAbs. 447-52D neutralized 88% of Tier 1 and 4% of Tier 2 viruses, the neutralization of Tier 2 viruses being inferior to that of the new mAbs HGN194 and HJ16. Corti2010 (neutralization)
• 447-52D: 433 Abs were cloned from HIV envelope-binding memory B cells from 6 patients with broadly neutralizing sera. The Abs had neutralizing activity directed against several epitopes on gp120 and the majority neutralized Tier 1 viruses. Tier-2 neutralization was observed only with mixtures of MAbs, but only at high concentrations. 447-52D was used as a control and it neutralized 5/5 Tier 1 and 2/5 Tier 2 viruses. Scheid2009 (neutralization)
• 447-52D: NAb specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. The integrity and specificity of gp120 beads in adsorption assay were validated by their ability to adsorb binding activity of 447-52D. gp120 point mutation D368R was used to screen the sera for CD4bs- Abs, and it was shown that this mutant could adsorb binding activity of 447-52D. To test for presence of coreceptor binding region MAbs in sera, gp120 I420 mutant was used. This mutant was recognized by 447-52D at equal levels as the wild type. To test sera for presence of V3 neutralizing activity, V3 peptides were used. These peptides inhibited neutralization mediated by 447-52D. In some of the broadly neutralizing sera, the gp120-directed neutralization was mapped to CD4bs. Some sera were positive for NAbs against coreceptor binding region. A subset of sera also contained NAbs directed against MPER. Li2009c (assay or method development)
• 447-52D: 447-52D sequence-independent mode of epitope recognition is reviewed in detail. The review also summarizes on how different modes of Ab binding and recognition are used to overcome viral evasion tactics and how this knowledge may be used to re-elicit responses in vivo. Kwong2009a (antibody binding site, review)
• 447-52D: The review discusses the implications of HIV-1 diversity on vaccine design and induction of neutralizing Abs, and possible novel approaches for rational vaccine design that can enhance coverage of HIV diversity. Patterns of within-clade and between-clade diversity in core epitopes of known potent neutralizing Abs is displayed. Korber2009 (review)
• 447-52D: 447-52D bound to both SF162 wild type and SF162 mutant, carrying only the monomeric form of the Env protein, virions and transfected cells. 447-52D exhibited higher binding activity to SF162 wild type compared to 2909, suggesting that 2909 epitope may not be formed on each trimer. Kimura2009 (antibody binding site, binding affinity)
• 447-D: FcγR-mediated inhibition and neutralization of HIV by 447-D and other MAbs is reviewed. The review also summarizes the role of ADCC and ADCVI Abs on HIV infection inhibition and neutralization. Forthal2009 (review)
• 447-52D: The crystal structure for VRC01 in complex with an HIV-1 gp120 core from a clade A/E recombinant strain was analyzed to understand the structural basis for its neutralization breadth and potency. The number of mutations from the germline and the number of mutated contact residues for 447-52D were smaller than those for VRC01. Zhou2010 (neutralization, structure)
• 447-52D: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 did not show binding to 447-52D. Memory B cells were selected that bound to RSC3 and full IgG mAbs were expressed. Three newly detected MAb VRC1 did not enhance neutralization by 447-52D. Addition of RSC3 had no effect on 447-52D neutralization of HXB2. Wu2010 (neutralization, binding affinity)
• 447-52d: Insertion of one or two disulfide bonds at specific residues in a V3 MN peptide sequence was used to constrain the conformations of the peptides to β-hairpin structures recognized by the 447-52d (postulated R5 V3 conformation). Insertion of two disulfide bonds increased the tendency of the peptides to form β-hairpin structures but it required replacement of residues reacting strongly with 447-52d Ab. Thus, peptides constrained by one disulfide bond are suggested to be more attractive candidates for immunogens that could elicit neutralizing Abs. Mor2009 (antibody binding site)
• 447-52d: The epitope sequence motif of 447-52d was precisely defined based on the 3D structure of the MAb complexed with V3MN peptide. Depending on how snugly V3 loop side chains are bound by the Ab, the complex can be divided into 3 subdomains. The specific epitope motif suggested by the complex structure was shown to be R315. 93% of HIV sequences with R315 in the Los Alamos HIV database fit the ag-binding site of MAb 447-52d. A set of V3 chimeric pseudoviruses, carrying either R315 or Q315, were tested for their sensitivity to neutralization by 447-52d. R315 viruses were neutralized very well while Q315 viruses were neutralized much more weakly. Thus, the sequence motif for the neutralization epitope recognized by 447-52d is R315. The neutralization-relevant epitope sequence motif of 447-52d was calculated to be present in approximately 13% of worldwide HIV isolates, predominating in subtype B isolates. Cardozo2009 (neutralization, optimal epitope)
• 447-52D: NL4.3 virus was cultured with cyclotriazadisulfonamide (CADA) and CADA-resistant virus was selected. 447-52D MAb showed enhanced binding to the CADA-resistant virus compared to wildtype. In addition, CADA-resistant virus was more susceptible to neutralization by this MAb. The mutations in CADA-resistant virus are suggested to stabilize the conformation of gp120 and reduce glycosylation. Vermeire2009 (neutralization, binding affinity)
• 447-52D: C2EB5 MAb was isolated from mice immunized with a peptide from C2 region. C2EB5 neutralization and binding affinity to virions of clades A, B, C, D and CRF01_AE was compared to that of 447-52D. Sreepian2009 (neutralization, variant cross-reactivity, binding affinity)
• 447-52D: Binding of 447-52D to gp120 was not inhibited by YZ23, an Ab derived from mice immunized with eletcrophilic analogs of gp120 (E-gp120), indicating no overlap of these MAb epitopes. Nishiyama2009
• 447-52D: V3 peptides were constrained in various ways to stabilize the β-hairpin conformation. This study showed that it is possible to constrain V3 peptides to this conformation that is recognized by 447-52D while maintaining high-affinity binding to this Ab. Peptides designed to mimic either the R5A or R5B conformation had higher affinity to 447-52D than peptides designed to mimic X4 conformation. Mester2009 (antibody binding site, kinetics, binding affinity)
• 447-52D: This Ab neutralized JRFL strain but many folds higher concentrations of the Ab were needed compared to neutralization of SF162 and SS1196 by 447-52D. 447-52D did not neutralize strain 3988.25. Hioe2009 (neutralization)
• 447-52D: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:3-15*07, IGHD:3-10, D-RF:3, IGHJ:6. There was a preferential usage of the VH5-51 gene segment for V3 Abs. The usage of the VH4 family for the V3 Abs was restricted to only one gene segment, VH4-59, and the VH3 gene family was used at a significantly lower level by these Abs. The V3 Abs preferentially used the JH3 and D2-15 gene segments. Gorny2009 (antibody sequence)
• 447-52D: An international collaboration (NeutNet) was organized to compare the performance of a wide variety of HIV-1 neutralization assays performed in different laboratories. Four neutralizing agents were evaluated: 4E10, 447-52D, sCD4 and TriMab (equal mixture of 2F5, 2G12 and 4E10). In general, there were clear differences in assay sensitivities that were dependent on both the neutralizing agent and the virus. No single assay was capable of detecting the entire spectrum of neutralizing activities. Fenyo2009 (assay or method development, neutralization)
• 447-52D: Two chimeras were constructed from a new HIV-2KR.X7 proviral scaffold where the V3 region was substituted with the V3 from HIV-1 YU2 and Ccon, generating subtype B and C HIV-2 V3 chimera. Both chimera were sensitive to neutralization by 447-52D, while the wildtype derived viruses HIV-2KR.X4 and HIV-2KR.X7 were completely resistant. A V3 linear peptide from HIV-1 JR-FL was able to absorb all 447-52D neutralizing activity and a peptide from HIV-1 YU2 removed most of the 447-52D neutralizing activity. Fc-V3 fusion proteins from subtypes B and C completely eliminated 447-52D-mediated neutralization. However, 447-52D was unable to neutralize the primary HIV-1 BORI virus while it neutralized the HIV-2-BORI V3 chimera. Competition assays showed that most of the plasmas derived from subtype B and C chronically infected individuals had neutralizing activity that was V3 specific and dependent upon residued in the V3 crown that overlap 447-52D and F425 B4e8 epitopes. Also, 55 early founder viral Env proteins from 47 subjects acutely infected with subtype B virus were tested for susceptibility to 447-52D. 51 viruses were resistant to neutralization by 447-52D, but many showed sensitivity to this Ab once conformational changes were induced with sCD4. This indicates that the V3 region in primary HIV-1 Envs is highly conserved but is shielded from Ab recognition. Davis2009 (HIV-2, neutralization, acute/early infection)
• 447-52D: Two different but genetically related viruses, CC101.19 and D1/85.16, which are resistant to small molecule CCR5 inhibitors, and two clones from their inhibitor sensitive parental strain CC1/85, were used to analyze interactions of HIV-1 with CCR5. CC101.19 had 4 substitutions in the V3 region and D1/85.16 had 3 changes in gp41. 447-52D bound detectably to gp120 of CC101.19 but this was greatly reduced compared to the binding of 447-52D to gp120 of the other three viruses. The opposite was true for 447-52D binding to the V3 peptide alone of the four viruses. 447-52D neutralized CC101.19 but did not neutralize the other three viruses. This indicates that the V3 region of CC101.19 has become unusually accessible to V3 Abs. Berro2009 (neutralization, binding affinity)
• 447-52D: This report investigated whether mannose removal alters gp120 immunogenicity in mice. Approximately 55 mannose residues were removed from gp120 by mannosidase digestion creating D-gp120 for immunization. 447-52D was able to bind to D-gp120 comparably as to the untreated gp120, indicating that the mannosidase digestion did not affect the antigenicity of gp120. Banerjee2009 (binding affinity)
• 447-52D: Reactivity and structure of 447-52D and 537-10D MAbs was compared. 447-52D was able to bind 22/24 V3 peptides from a panel of clades A, B and C, including peptides with both GPGR and GPGQ motifs, while 537-10D only reacted with peptides containing the GPGR motif. Crystal structures of the Fab fragments of 447-52D and 537-10D in complex with 23-mer peptides derived from clades A and B viruses, respectively, was determined. Although both MAbs had highly similar antigen binding sites, differences in their binding and neutralization activities were found to be due to subtile differences in their structures. The structure analyses explained the ability of 447-52D to bind to both GPGR and GPGQ motifs. Burke2009 (antibody binding site, neutralization, structure)
• 447-52D: Data is summarized on the X-ray crystal structures resolution and NMR studies of 447-52D. Sirois2007 (review, structure)
• 447-52D: This review summarizes data on possible vaccine targets for elicitation of neutralizing Abs and discusses whether it is more practical to design a clade-specific than a clade-generic HIV-1 vaccine. Development of a neutralizing Ab response in HIV-1 infected individuals is reviewed, including data that show no apparent division of different HIV-1 subtypes into clade-related neutralization groups. Also, a summary of the neutralizing activity of MAb 447-52D in different HIV-1 clades is provided. McKnight2007 (variant cross-reactivity, review)
• 447-52D: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 447-52D neutralization properties and binding to HIV-1 envelope, and current strategies to develop versions of the Env spike with functional trimer properties for elicitation of broadly neutralizing Abs, such as 447-52D, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed. Phogat2007 (review)
• 447-52D: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including 447-52D MAb, in vivo and in vitro activity of neutralizing Abs, the importance and downfalls of non-neutralizing Abs and antibodies that mediate antibody-dependent cellular cytotoxicity and the complement system, and summarizes data on areas that need future investigation on Ab-mediated immune control. Huber2007 (review)
• 447-52D: 447-52D structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit anti-V3 Abs, are reviewed in detail. Lin2007 (review, structure)
• 447/52D: This review summarizes 447-52D Ab epitope, properties and neutralization activity. Kramer2007 (review)
• 447-52D: Current insights into CTLs and NAbs, and their possible protective mechanisms against establishment of persistent HIV/SIV infection are discussed. Pre- and post-infection sterile and non-sterile protection of NAbs against viral challenge, and potential role of NAbs in antibody-mediated antigen presentation in modification of cellular immunity, are reviewed. 447-52D anti-viral activity in suppression of viral rebound in HIV-1 infected humans undergoing structured treatment interruptions is described. Yamamoto2008 (supervised treatment interruptions (STI), review)
• 447-52D: A mathematical model was developed and used to derive transmitted or founder Env sequences from individuals with acute HIV-1 subtype B infection. All but three of the transmitted or early founder Envs were resistant to neutralization by 447-52D, indicating that the coreceptor binding surfaces on transmitted/founder Envs are conformationally masked. sCD4 could trigger a conformational change in gp120 of these Envs and render the virus susceptible to neutralization by 447-52D. Keele2008 (neutralization, acute/early infection)
• 447-52D: A significantly higher level of 447-52D bound to gp120 complexed with anti-CD4bs mAbs than to gp120 alone or in complex with other non-CD4bs Abs, indicating that binding of anti-CD4bs Abs to gp120 increases exposure of specific V3 MAb epitopes. Visciano2008 (antibody binding site)
• 447D: Trimeric envelope glycoproteins with a partial deletion of the V2 loop derived from subtype B SF162 and subtype C TV1 were compared. 447D recognized both B and C trimers with similar efficiency, indicating that the epitope recognized by this Ab is exposed and preserved in the subtype C trimers. Subtype C trimer had many biophysical, biochemical, and immunological characteristics similar to subtype B trimer, except for a difference in the three binding sites for CD4, which showed cooperativity of CD4 binding in subtype C but not in subtype B. Srivastava2008 (binding affinity, subtype comparisons)
• 447-52D: In order to assess whether small molecule CCR5 inhibitor resistant viruses were more sensitive to neutralization by NAbs, two escape mutant viruses, CC101.19 and D1/85.16, were tested for their sensitivity to neutralization by 447-52D, compared to the sensitivity of CC1/85 parental isolate and the CCcon.19 control isolate. The CC101.19 escape mutant has 4 sequence changes in V3 while the D1/85.16 has no sequence changes in V3 and relies on other sequence changes for its resistance. None of the control or resistant viruses were sensitive for neutralization by 447-52D, although 447-52D bound strongly to gp120 from CC1/85 and CC101.19. These results indicate that V3-dependent and -independent changes responsible for CCR5 inhibitor resistance do not necessarily alter the exposure of V3 to some of the V3 Abs. Pugach2008 (co-receptor, neutralization, binding affinity)
• 447-52D: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 447-52D belonged to the group 2 MAbs, which are able to bind subtype B but not subtype C gp120, and are able to bind both V3 peptides. 447-52D was able to bind subtype B V3 in the subtype C Env backbone chimera, but not the reverse, indicating that 447-52D binds to a structure created by the subtype B V3 sequence that is not impacted by the gp120 backbone. For subtype B, 447-52D required an R18 residue in order to bind, but the binding was not significantly affected by the H13R change. For subtype C, Q18R mutation did not restore binding to gp120, but the R13H-Q18R double mutation did. Peptide binding was affected only by the R13H mutation, indicating that the poor binding of Q18R gp120 mutant has a structural basis. 447-52D was not able to neutralize JR-FL isolate, and somewhat neutralized SF162. A chimeric SF162 variant with a JR-FL-like V3 sequence was hypersensitive to neutralization by this Ab. Patel2008 (neutralization, binding affinity, subtype comparisons)
• 447-52D: Requirements for elicitation of CD4i Abs were examined by immunizing non-primate monkeys, rabbits, and human-CD4 transgenic (huCD4) rabbits with trimeric gp140. The trimers used for the immunizations were inoculated with PBMCs, and CD4-specific binding to live CD3+/CD4+/CD8- cells was verified by recognition of the trimers by 447-52D. Forsell2008
• 447-52D: To test whether the conformation change of Env induced by CD4 affects the breadth and potency of 447-52D neutralization, 447-52D was tested in the presence or absence of sCD4 in neutralization of a panel of 12 subtype B and 12 subtype C Env-pseudoviruses. Without sCD4, 447-52D neutralized 2 subtype B and 0 subtype C viruses. With sCD4 present, 447-52D neutralized 7 subtype B and 1 subtype C virus, indicating that neutralization resistance of some viruses to 447-52D is due to a lack of exposure of the V3 loop. Neutralization of JRFL, ADA, and YU2 isolates by 447-52D increased with increased dose of sCD4. A virus with GPGG sequence at the tip of the V3 loop did not react with 447-52D, indicating that amino acid sequence variation may account for the neutralization resistance of other viruses. The presence of b12 and F105 did not induce 447-52D mediated neutralization of JRFL virus, indicating that b12 and F105 do not induce a conformation alternation in Env that exposes V3 loop to 447-52D. Wu2008 (neutralization, variant cross-reactivity)
• 447-52D: The neutralization profile of early R5, intermediate R5X4, and late X4 viruses from a rhesus macaque infected with SHIV-SF162P3N was assessed. The parental R5 virus was resistant to neutralization by 447-52D, while both the R5X4 intermediate and the late X4 viruses were sensitive to neutralization by 447-52D. The enhanced neutralization susceptibility of the dual-tropic and the X4 viruses to 447-52D suggests adoption of an increasingly open conformation of the Env gp120 over time. Tasca2008 (co-receptor, neutralization)
• 447D: 447D neutralized 6 of the 15 subtype B isolates tested, of which 5 were resistant to neutralization by MAbs 19b, 39F, CO11, F2A3, F530, LA21 and LE311. Angle of interaction between 447D and V3 was shown by superimposing the Fab fragment of the Ab with V3. 447D was shown to interact with V3 from a nearly identical angle as MAb 58.2. Pantophlet2008 (antibody binding site, neutralization, structure)
• 447-52D: A new purification method was developed using a high affinity peptide mimicking CD4 as a ligand in affinity chromatography. This allowed the separation in one step of HIV envelope monomer from cell supernatant and capture of pre-purified trimer. Binding of 447-52D to gp120SF162 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the miniCD4 allows the separation of HIV-1 envelope with intact 447-52D epitope. gp140DF162ΔV2 was purified by the miniCD4 method to assess its ability to capture gp140 trimers. Purified gp140DF162ΔV2 was recognized by 447-52D, and the k-off value for 447-52D was reduced compared to gp120SF162 monomer, consistent with the gp140DF162ΔV2 trimeric conformation. Binding of 447-52D to gp140DF162ΔV2 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the SF162 trimer antigenicity was preserved. Martin2008 (assay or method development, kinetics, binding affinity)
• 447-52D: Variable domains of three heavy chain Abs, the VHH, were characterized. The Abs were isolated from llamas, who produce immunoglobulins devoid of light chains, immunized with HIV-1 CRF07_BC, to gp120. It was hypothesized that the small size of the VHH, in combination with their protruding CDR3 loops, and their preference for cleft recognition and binding into active sites, may allow for recognition of conserved motifs on gp120 that are occluded from conventional Abs. 447-52D provided some inhibition of binding of the three neutralizing VHH Abs to gp120, suggesting that 447-52D imposes steric hinderance to binding of the VHH Abs to gp120. Forsman2008 (antibody interactions)
• 447-52D: 24 broadly neutralizing plasmas from HIV-1 subtype B and C infected individuals were investigated using a series of mapping methods to identify viral epitopes targeted by NAbs. V3 Ab activity was measured by three assays where 447-52D was used as a control. A V3 peptide derived from the N-terminal part of the V3 loop, including the crown, potently inhibited neutralization of several HIV-1 isolates by 447-52D, indicating that V3 Abs are commonly directed to the N-terminal part of the V3 loop. Binley2008 (neutralization)
• 447: 32 human HIV-1 positive sera neutralized most viruses from clades A, B, and C. Two of the sera stood out as particularly potent and broadly reactive. Two CD4-binding site defective mutant Env proteins were generated to evaluate whether Abs to the CD4-binding site are involved in the neutralizing activity of the two sera. The integrity of the wildtype and mutant proteins was tested to their reactivity to the 447 Ab. Li2007a (binding affinity)
• 447-52D: HIV-1 env clones resistant to cyanovirin (CV-N), a carbohydrate binding agent, showed amino acid changes that resulted in deglycosylation of high-mannose type residues in the C2-C4 region of gp120. Compared to their parental virus HIV-1 IIIB, these resistant viruses were over 200 times more sensitive to 447-52D, indicating that deglycosylation in CV-N resistant viruses is likely to make the V3 loop more accessible to Abs. Hu2007 (antibody binding site, neutralization, escape)
• 447-52D: Five amino acids in the gp41 N-terminal region that promote gp140 trimerization (I535, Q543, S553, K567 and R588) were considered. Their influence on the function and antigenic properties of JR-FL Env expressed on the surfaces of pseudoviruses and Env-transfected cells was studied. Various non-neutralizing antibodies bind less strongly to the Env mutant, but neutralizing antibody binding is unaffected. 447-52D captured modestly (but not significantly) fewer mutant pseudovirions than wild type, neutralization was not tested. Dey2008 (binding affinity)
• 447D: The study explores how the V1 loop of Env influences the neutralization susceptibilities of heterologous viruses to antibodies elicited by the SF162gp140 immunogen. When the V1 loop of the heterologous isolates was replaced by the V1 loop present on the DF162go140 immunogen, these isolates became susceptible to neutralization by anti-V3 MAb 447D, indicating that the V1 loop plays an important role in the resistance of heterologous viruses to neutralization. Ching2008 (neutralization)
• 447-52D: The study determined a crystal structure of Fab 447-52D in complex with a V3 peptide NNTRKSIHLGPGRAFYATGDIIG at 2.1 A resolution. The structure revealed an extended CDR H3 loop that forms a β-sheet with the peptide, with predominantly main-chain hydrogen bonds contacts. There was high structural homology with reported structures of other Fab 447-52D complexes, indicating that the V3 loop may adopt a small set of conserved structures around the crown of the β-hairpin. Dhillon2008 (structure)
• 447-52D: 447-52D bound only to V3 peptides from the three isolates (MN, SHIVsf162p3 and clade B consensus) which contain GPGR motif. 447-52D did not recognize one B consensus peptide that did contain GPGR motif. Glycosylation of the position 154 in V1 was more important for the protection of the virus from this Ab than glycosylation of the position 195 in V2. 447-52D neutralized chimeric viruses 89.6/SF162V1, JRFL/SF162V1, YU2/SF162V1 and HxB2/SF162V1 more efficiently than their wildtype counterparts, indicating that the accessibility of the V3 loop is affected by the nature of the V1 loop. Derby2007 (neutralization, binding affinity)
• 447-52D: The epitope recognition sequence for this Ab was introduced into the corresponding region of SIVmac239 either alone or together with epitopes for Abs 2F5 and 4E10. The infectivity and replicative capacity of SIV239/447-52D and SIV239/447-52D/2F5/4E10 were, however, not detectable and too low, respectively, to be used for further analyses. Yuste2006 (SIV)
• 447-52D: The neutralizing capacity and binding of this Ab to the V3 region of gp120, as well as resistance to neutralization in different HIV-1 clades are reviewed. Pantophlet2006 (antibody binding site, neutralization, review, subtype comparisons, structure)
• 447-52D: This Ab was shown to neutralize SF162 and the neutralization sensitivity increased in the SF162 variant with a JR-FL V3 loop, SF162(JR-FL V3). In contrast, a great reduction in sensitivity to neutralization was observed in the SF162(JR-FL V1/V2) variant and was somewhat restored in the SF162(JR-FL V1/V2/V3) variant, indicating that the masking of the V1/V2 loop plays a much greater role in restricting neutralization sensitivity than the variations in V3. This Ab was shown to neutralize viruses with V3 sequences from several different subtypes (B, F, A1, CRF02_AG, H and CRF01_AE) except subtype C. This Ab failed to neutralize SF162(JR-FL V1/V2) with V3 derived from different HIV-1 clades indicating effective V1/V2-mediated masking of several HIV-1 clades. The effect on the neutralization sensitivity of the residue at the crown of the V3 loop (position 18) was shown to be great for this Ab. Krachmarov2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 447-52D: The G314E escape variant highly resistant to KD-247 was shown to be more sensitive to 447-52D than the wildtype virus. 447-52D was shown to be able to bind well to both mutant and wildtype surface-expressed Envs. Yoshimura2006 (escape, binding affinity)
• 47-52D: Binding of this Ab to three V3 peptides was compared to binding of Ab 2219 to the same peptides. 447-52D was shown to bind to V3 MN and V3 UG1033 but not to V3 UR29. Stanfield2006 (variant cross-reactivity, binding affinity)
• 447-52D: This MAb was derived from plasma from a patient with env clade B virus with the GPGR V3 motif. When cross-reactivity was tested, this Ab bound to the V3subtypeB-fusion protein containing GPGR motif but not to the V3subtypeA-fusion protein containing GPGQ motif. This Ab was also shown to be able to neutralize both clade B psSF162 (GPGR) and clade C psMW965 (GPGQ) virus, and four of subtype B and two of non-B primary isolates. Gorny2006 (neutralization, variant cross-reactivity, binding affinity, subtype comparisons)
• 447-52D: Escape variants with the V3 P313L mutation, or V2 R166K, D167N and P175L mutations, were resistant or partially resistant, respectively, to 447-52D. Binding of 447-52D to surface-expressed Env proteins with the V2 mutations was lowered compared to the binding to viruses with no mutations. Binding to surface-expressed Env proteins with the V3 mutation was comparable to the negative control values. Binding affinity of this Ab for different combinations of V2 and V3 mutants was also tested. Shibata2007 (escape, binding affinity)
• 447-52D: This Ab was used in the analysis of clade C gp140 (97CN54) antigenicity and was shown to bind with relatively high avidity to the molecule and to dissociate substantially within 420 s. It was also used as a positive control in the neutralization assay. Sheppard2007a (neutralization, variant cross-reactivity, kinetics, binding affinity)
• 447-52D: Compared to the full-length Con-S gp160, chimeric VLPs containing Con-S ΔCFI gp145 with transmembrane (TM) and cytoplasmic tail (CT) sequences derived from the mouse mammary tumor virus (MMTV), showed higher binding capacity to 447-52D. Chimeric VLPs with only CT derived from MMTV also showed higher binding capacity to 447-52D than the full-length Con-S gp160, however, not as high as the chimeric CT-TM VLPs. Wang2007a (binding affinity)
• 447-52D: The major infectivity and neutralization differences between a PBMC-derived HIV-1 W61D strain and its T-cell line adapted counterpart were conferred by the interactions of three Env amino acid substitutions, E440G, D457G and H564N. Chimeric Env-pseudotyped virus Ch5, containing all three of the mutations, was more neutralization sensitive to 447-52D than Ch2, which did not contain any of these mutations. Env-pseudotyped viruses containing D457G mutation alone, or in combination with E440G or H564N, were also more sensitive to neutralization by 447-52D than Ch2. Beddows2005a (neutralization)
• 447-52D: The structure of the 447-52D MAb and its mechanisms of the V3 loop GPGR motif recognition and binding are reviewed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed. Burton2005 (antibody binding site, review, structure)
• 447-52D: Monomeric gp120 and trimeric gp140CF proteins synthesized from an artificial group M consensus Env gene (CON6) bound well to 447-52D, indicating correct exposure of the 447-52D epitope. Gao2005a (antibody binding site)
• 447-D: This Ab was used as a control in a peptide adsorption assay. 447-D neutralized the SF162 primary isolate to 95%. When 447-D was pre-incubated with BaL or YU2 V3 loop peptides, nearly all neutralizing activity was inhibited. Grundner2005 (neutralization)
• 447-52D: The crystal and nuclear magnetic resonance structures of V3-reactive antibody-peptide complexes were examined. 447-52D completely surrounded V3, suggesting a high degree of accessibility for generating an immune response. Accessibility of V3 to this MAb is shown in a 3D figure. Huang2005 (antibody binding site, structure)
• 447-52D: A series of genetically modified Env proteins were generated and expressed in both insect and animal cells to be monitored for their antigenic characteristics. For 447-52D, five of the modified proteins expressed in insect cells, including 3G mutant (mutations in 3 glycosylation sites), dV1V2 mutant (V1V2 deletions), 3G-2G, 3G-dV2, and 3G-dV2-1G (1G being a mutation near the TM domain), showed higher binding than the wildtype. Of these, the 3G-dV2-1G mutant showed highest binding to 447-52D, indicating that glycosylation of the gp41 domain may affect exposure of the V3 loop. Expressed in animal cells, mutants dV2 and 3G-dV1V2 showed increased binding to 447-52D at relatively high Ab concentrations compared to the wildtype Env. Kang2005 (antibody binding site, binding affinity)
• 447D: Full-length gp160 clones were derived from acute and early human HIV-1 infections and used as env-pseudotyped viruses in neutralization assays for their characterization as neutralization reference agents. 2 out of 19 pseudoviruses were sensitive to neutralization by 447D, as was the SF162.LS strain. Li2005a (assay or method development, neutralization)
• 447: Pseudoviruses expressing HIV-1 envelope glycoproteins from BL01, BR07 and 89.6 strains were compared in neutralization assays to replication competent clone derived from transfection of 293T cells (IMC-293T) and to the IMC-293T derived from a single passage through PBMC (IMC-PBMC). The neutralization responses of pseudoviruses and corresponding IMC-293T to 447 were similar, while a significant decrease in viral neutralization sensitivity to 447 was observed for the BR07 and 89.6 IMC-PBMC viruses. The decrease was associated with an increase in average virion envelope glycoprotein content on the PBMC-derived virus. Louder2005 (assay or method development, neutralization)
• 447-52D: The structure of V3 HIV-1 peptides derived from IIIB and MN isolates when bound to 447-52D was determined by NMR. It was observed that the two different V3 peptides assumed same N-terminal strand conformation when bound to this Ab. V3 peptide IIIB bound to Ab 0.5β differed from the same peptide bound to 447-52D by 180 degrees N-terminal chain orientation. It is suggested that the conformation of an Ab-bound V3 peptide is dictated not only by the peptide sequence but also by an induced fit to the specific Ab. Dominant interactions of 447-52D with three conserved N-terminal residues may be responsible for the broadly neutralizing capability of this Ab. Rosen2005 (antibody binding site, co-receptor, variant cross-reactivity, structure)
• 447-52D: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed. Srivastava2005 (neutralization, variant cross-reactivity, review, subtype comparisons)
• 447-52D: gp120 alone and gp120 bound to CD4D12 (the first two domains of human CD4) or to M9 (a 27-residue CD4 analog) were used to immunize guinea pigs. Only sera from the gp120-CD4D12 immunized animals showed broadly neutralizing activity. Sera from gp120-CD4D12 and gp120 immunized animals competed equally well with 447-52D, indicating that the V3-loop was accessible in both immunogens. Varadarajan2005 (antibody binding site, vaccine antigen design)
• 447-52D: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1. McCann2005 (antibody binding site, neutralization, review, structure)
• 447-52D: MAbs were investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. Visualization of Env-Ab binding was conducted by BN-PAGE band shifts. 447-52D binding to trimer was completely dependent on sCD4, consistent with neutralization. Crooks2005 (antibody binding site, assay or method development, neutralization)
• 447-52D: This review summarizes data on 447-52D-V3 and 447-52D-V3 peptide X-ray crystallographic structures and NMRs and its neutralization capabilities. The binding mechanism of this Ab to V3 explains its ability to neutralize a wide array of viral isolates. Conformation of the V3 peptide bound to 447-52D is very similar to its conformation when bound to mouse Abs 50.1, 59.1 and 83.1. Stanfield2005 (antibody binding site, neutralization, variant cross-reactivity, review, structure)
• 447-52D: A T-cell line adapted strain (TCLA) of CRF01_AE primary isolate DA5 (PI) was more neutralization sensitive to 447-52D than the primary isolate. Mutant virus derived from the CRF01_AE PI strain, that lacked N-linked glycosylation at position 197 in the C2 region of gp120, was significantly more sensitive to neutralization by 447-52D then the PI strain. Mutants at positions 138 in V1 and 461/464 in V5 showed lower sensitivity to neutralization by 447-52D. Deglycosylated subtype B mutants at positions 197 and 234 were slightly more neutralizable by 447-52D. Teeraputon2005 (antibody binding site, neutralization, subtype comparisons)
• 447-52D: In addition to gp120-gp41 trimers, HIV-1 particles were shown to bear nonfunctional gp120-gp41 monomers and gp120-depleted gp41 stumps on their surface. 447-52D moderately neutralized wildtype virus particles. It effectively bound to nonfunctional monomers but not to gp120-gp41 trimers. Monomer binding did not correlate with neutralization, but it did correlate with virus capture. It is hypothesized that the nonfunctional monomers on the HIV-1 surface serve to divert the Ab response, helping the virus to avoid neutralization. Moore2006 (antibody binding site, neutralization)
• 447D: Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). 447D recognized SF162gp140 and ΔV2gp140 equally and failed to recognize ΔV2ΔV3gp140 and ΔV3gp140. Derby2006 (antibody binding site)
• 447-52D: 447-52D was not found to inhibit binding of gp120 to DC-SIGN. This Ab bound to Fc-gp120 construct but not to the chimeras missing the V3 loop. Binley2006 (binding affinity)
• 447-52D: 29 subtype B V3 peptides were designed and used for immunization of guinea pigs. Peptides that induced Abs that neutralized more than 3 HIV isolates were shown to bind to this Ab better than peptides unable to induce neutralization of any of the HIV-1 primary isolates. Haynes2006 (neutralization, binding affinity)
• 447-52D: Cloned Envs (clades A, B, C, D, F1, CRF01_AE, CRF02_AG, CRF06_cpx and CRF11_cpx) derived from donors either with or without broadly cross-reactive neutralizing antibodies were shown to be of comparable susceptibility to neutralization by 447-52D. Cham2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 447-52D: Guinea-pigs were immunized with 447-52D epitope inserted at three different surface V3 loop locations in the small Escherichia coli Trx protein in order to generate a competent immunogen. Only one complex was shown to successfully generate anti-V3 Abs capable of out-competing 447-52D binding to gp120 and recognizing the same epitope as this Ab. However, these 447-52D-like Abs were not able to affect neutralization of JRFL and BAL. Chakraborty2006 (neutralization, vaccine antigen design, variant cross-reactivity, binding affinity)
• 447-52D: The ability of this Ab to inhibit viral growth was increased when macrophages and immature dendritic cells (iDCs) were used as target cells instead of PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication by this Ab for macrophages and iDCs can occur by two distinct mechanisms, neutralization of infectivity involving only the Fab part of the IgG, and, an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles. Holl2006 (dendritic cells)
• 447-52D: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The neutralizing activity of 447-52D was observed to be higher in iMDDCs than in PBLs and PHA-stimulated PBMCs. A 90% reduction of HIV infection was observed without induction of MDDC maturation by this MAb. It was also demonstrated that binding of this MAb to HIV-1 was necessary for inhibition of iMDDC infection. Increased expression of FcγRI on iMDDCs increased inhibition of HIV by 447-52D, suggesting the involvement of this receptor in the HIV-inhibitory activity of this MAb. Holl2006a (neutralization, dendritic cells)
• 447-52D: The neutralization potency of this Ab against 7 HIV-1 primary isolates was compared to the neutralization potency of the anti-V3 MAb KD-247. Same Ab concentrations were needed for neutralization of the MN, N-NIID, and 92TH022 isolates, while higher concentrations of 447-52D were needed for the neutralization of the rest of the HIV-1 isolates suggesting KD-247 is more potent. Eda2006a
• 447-52D: In this study the neutralization breadth of F425 B4e8 was assessed using a panel of 40 primary HIV-1 isolates, and 447-52D was found to have a similar profile, and was used as a control to gauge the effects of the amino acid substitutions in the V3 region. As expected, replacing Arg 315 with Ala or Gln and Pro 313 with Ala reduced binding affinity of this 447-52D substantially. Ala substitutions of residues in positions 304-309 and 319-320 also unexpectedly resulted in diminished binding affinity of the Ab. Pantophlet2007 (antibody binding site, subtype comparisons)
• 447-52D: Z13e1, a high affinity variant of Fab Z13, was identified through targeted mutagenesis and affinity selection against gp41 and an MPER peptide. Z13e1 showed 100-fold improvement in binding affinity for MPER antigens over Z13. 447-52D was used as a control in this study. 447-52D was shown to clearly bind to monomers of gp120-gp41 while trimer binding was negligible, in accordance with its modest neutralization potency against HIV-1 JR-FL. Nelson2007 (vaccine antigen design)
• 447-52D: G1 and G2 recombinant gp120 proteins, consisting of 2F5 and 4E10, and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120, were tested as an immunogen to see if they could elicit MPER antibody responses. Deletion of V1/V2 from gp120, or its replacement with G1 and G2 grafts, did not greatly affect binding of 447-52D to gp120. Shortening of the N and C termini of the V3 loop enhanced the binding of 447-52D. Law2007 (vaccine antigen design)
• 447-52D: This review describes the effectiveness of the current HIV-1 immunogens in eliciting neutralizing antibody responses to different clades of HIV-1. It also summarizes different evasion and antibody escape mechanisms, as well as the most potent neutralizing MAbs and their properties. MAbs reviewed in this article are: 2G12, IgG1b12, 2F5, 4E10, A32, 447-52D and, briefly, D50. Novel immunogen design strategies are also discussed. Haynes2006a (neutralization)
• 447-52D: Viruses from early and late infection of a macaque with SHIV SF162P4 were resistant to contemporaneous serum that had broadly reactive NAbs. SF162 was highly susceptible to neutralization by anti-V3 MAbs 447D and P3E1, as well as anti-V1 MAb P3C8, while envelopes cloned from this animal at 304 days and at 643 days (time of death) post infection had developed resistance to all three of these antibodies. Kraft2007 (neutralization, escape)
• 447-52D: This Ab was used to help define the antigenic profile of envelopes used in serum depletion experiments to attempt to define the neutralizing specificities of the broadly cross-reactive neutralizing serum. Peptides containing epitopes for 447-52D did not inhibit neutralization by broadly neutralizing sera from two clade B and one clade A infected asymptomatic individuals, indicating that the V3 epitope for this MAb did not account for the broad neutralizing activity observed. 447-52D bound to JR-FL and JR-CSF gp120 monomers but not to core JR-CSF gp120 monomer. Dhillon2007 (antibody binding site, neutralization)
• 447-52D: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. V3 MAbs (447-52D, 19b, F245-B4e8 and 39F) bound to the GDMR antigen, but either did not bind or had diminished binding to mCHO. Selvarajah2005 (vaccine-induced immune responses, Th2)
• 447-52D: This study is about the V2 MAb C108g, which is type-specific and neutralizes BaL and HXB2. JR-FL is a neutralization resistant strain; modification of JRFL at V2 positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The modification in V2 also increased neutralization sensitivity to V3 MAbs 4117c, 2219, 2191, and 447-52D (447-52D was the only one of the 4 V3 MAbs that could neutralize the unmodified JRFL); but only had minor effects on neutralization by CD4BS MAb 5145A, and broadly neutralizing MAbs IgG1b12, 2G12, and 2F5. Pinter2005 (antibody binding site)
• 447-52D: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication in microglial cells. Bori-15 had increased replication in microglial cells and a robust syncytium-forming phenotype, ability to use low levels of CD4 for infection, and increased sensitivity to neutralization by sCD4 and 17b. Four amino acid changes in gp120 V1-V2 were responsible for this change. Protein functionality and integrity of soluble, monomeric gp120-molecules derived from parental HIV-1 Bori and microglial-adapted HIV-1 Bori-15 was assessed in ELISA binding assays using CD4BS MAbs F105 and IgG1b12, glycan-specific 2G12, and V3-specific 447-52D, and were unchanged. Association rates of sCD4 and 17b were not changed, but dissociation rates were 3-fold slower for sCD4 and 14-fold slower for 17b. Martin-Garcia2005 (antibody binding site)
• 447-52D: The epitope for the MAb D19 is conserved and embedded in V3. D19 is unique in that for R5 viruses, it was cryptic and did not bind without exposure to sCD4, and for X4 and R5X4 isolates it was constitutively exposed. It had an overlapping binding region with MAbs 447-52D, B4e8, and 268-D, but different reactivity patterns and fine specificity. While B4e8 and 447-52D could bind to the R5 virus BaL in the absence of sCD4, treatment with sCD4 did increase the binding of both B4e8 and 447-52D, but did not impact their ability to neutralize BaL. Lusso2005 (antibody binding site)
• 447-52D: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. Neutralization by anti-V3 B clade specific MAbs 447-52D and 4117C was fully blocked by a clade V3 loop fusion protein, but not an A clade fusion protein, while Cameroonian sera neutralization was fully blocked by both A and B clade fusion proteins. Krachmarov2005 (antibody binding site, variant cross-reactivity, subtype comparisons)
• 447-52D: Of 35 Env-specific MAbs tested, only 2F5, 4E10, IgG1b12, and two CD4BS adjacent MAbs (A32 and 1.4G) and gp41 MAbs (2.2B and KU32) had binding patterns suggesting polyspecific autoreactivity, and similar reactivities may be difficult to induce with vaccines because of elimination of such autoreactivity. 447-52D has no indication of polyspecific autoreactivity. Haynes2005 (antibody binding site)
• 447-52d: 2909 is a human anti-Env NAb that was selected by a neutralization assay and binds to the quaternary structure on the intact virion. ELISA-based competition assays and subsequent mutational analysis determined that the CD4BS and V2 and V3 loops contribute to the 2909 epitope: 2909 binding was inhibited by MAbs 447-52d (anti-V3), 830A (anti-V2), and IgG1b12 (anti-CD4BS) and sCD4. 2909 was not inhibited by MAbs 670, 1418, nor 2G12. Gorny2005
• 447-52D: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120, including 447-52D. Pantophlet2004 (vaccine antigen design)
• 447-52D: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. Neutralization outside of the B clade was very rare, and seemed to depend on the presence of a GPGR V3 tip, which is rare outside of the B clade. Binley2004 (variant cross-reactivity, subtype comparisons)
• 447-52D: Analysis of the conformation of 447-52D in complex with the V3MN18 peptide (gp12 aa 310-329, KRKRIHIGPGRAFYTTKN) was undertaken using solid state NMR. The bound peptide had a well-defined constrained structure that was in good agreement with solution NMR and crystallographic studies. Sharpe2004 (structure)
• 447-52D: A primary isolate, CC1/85, was passaged 19 times in PBMC and gradually acquired increased sensitivity to FAb b12 and sCD4 that was attributed to changes in the V1V2 loop region, in particular the loss of a potential glycosylation site. The affinity for sCD4 was unchanged in the monomer, suggesting that the structural impact of the change was manifested at the level of the trimer. The passaged virus, CCcon19, retained an R5 phenotype and its neutralization susceptibility to other Abs was essentially the same as CC1/85. 447-52D did not neutralize the primary or passaged variant. Pugach2004 (variant cross-reactivity, viral fitness and reversion)
• 447-52D: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neutralization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype. 5/6 anti-V3 MAbs, including 447-52D, had similar binding affinity to soluble SF162 and JR-FL rgp120s, although the V3 loop differs at three positions (HigpgrafyTtgE for JR-FL and TigpgrafyAtgD for SF162). Pinter2004 (variant cross-reactivity)
• 447-52D: Sera from two HIV+ people and a panel of MAbs were used to explore susceptibility to neutralization in the presence or absence of glycans within or adjacent to the V3 loop and within the C2, C4 and V5 regions of HIV-1 SF162 env gp120. The loss of the any of three glycans within or adjacent to the V3 loop (GM299 V3), C2 (GM292 C2), C3 (GM329 C3) increased neutralization susceptibility to 447-52D, but C4 (GM438 C4) or V5 (GM454 V5) removal did not make SF162 more sensitive. V3 glycans tended to shield V3 loop, CD4 and co-receptor MAb binding sites, while C4 and V5 glycans shielded V3 loop, CD4, gp41 but not co-receptor MAb binding sites. Selective removal of glycans from a vaccine candidate may enable greater access to neutralization susceptible epitopes. McCaffrey2004 (antibody binding site, vaccine antigen design)
• 447-52D: The role of serine proteases on HIV infection was explored. Trypsin decreased the binding of most Env MAb tested and diminished cell fusion of H9 cells infected with HIV-1 LAI virus (H9/IIIB) to MAGI cells. In contrast, thrombin increased the binding of MAbs to gp120 epitopes near the CD4 and CCR5 binding sites, and increased cell fusion. Binding of the V3 MAbs 694-98D and 447-52D, that both bind near the tip of the loop, was decreased by both thrombin and trypsin. Ling2004 (antibody binding site)
• 447-52D: V3 MAb neutralization is influenced by retaining the epitope, exposure on the intact virion, mobility during CD4-induced conformational change, and affinity. Anti-V3 MAbs selected using V3 peptides neutralize less effectively than V3 MAbs selected using fusion proteins or gp120, suggesting antigenic conformation is important. This MAb was selected using V3 peptides, but was an exception in that it is cross-neutralizing. 447-52D neutralized 12/13 clade B viruses. Gorny2004 (antibody binding site)
• 447-52D: This review provides summaries of Abs that bind to HIV-1 Env. There are many V3 MAbs, many neutralize some TCLA strains, and a subset can also neutralize some primary isolates. The set that can cross-neutralize primary isolates (2182, 2191, 2219, 2412, 2442, 2456) bind V3 but are conformationally sensitive, suggesting some structural conservation despite sequence variation. These MAbs have distinct epitopes relative to 447-52D, a MAb directed at the tip of the V3 loop that also can neutralize many primary isolates. Although 447-52D was selected using a peptide, it has conformational characteristics. Inter-clade cross-neutralization by anti-V3 conformation-dependent MAbs is reduced. Gorny2003 (antibody binding site, review)
• 447-52D: This paper attempts to engineer a gp120 molecule that would focus the immune response onto the IgG1b12 epitope. Adding a glycosylation sequon (P313N) to the V3 loop knocked out binding to anti-V3 MAbs loop 2, 19b and 447-52-D. Pantophlet2003b (vaccine antigen design)
• 447-52D: scFv 4KG5 reacts with a conformational epitope that is formed by the V1V2 and V3 loops and the bridging sheet (C4) region of gp120 and is influenced by carbohydrates. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120 JRFL. MAbs to the following regions diminished 4KG5 binding: V2 loop, V3 loop, V3-C4 region, CD4BS. MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected by these loops. This was one of the V3 MAbs used. Zwick2003a (antibody interactions)
• 447-52D: The Fv fragment (composed of just the light and heavy variable regions, and the smallest intact binding unit of an Ab) of 447-52 D was expressed and purified. Preliminary NMR with the peptide epitope indicates that an NMR structure determination is feasible. Kessler2003 (antibody sequence, structure)
• 447-52D: The SOS mutant envelope protein introduces a covalent disulfide bond between gp120 surface and gp41 transmembrane proteins into the R5 isolate JR-FL by adding cysteines at residues 501 and 605. Pseudovirions bearing this protein bind to CD4 and co-receptor bearing cells, but do not fuse until treatment with a reducing agent, and are arrested prior to fusion after CD4 and co-receptor engagement. 447-52D was able to neutralize the SOS protein better than the wildtype, but did not neutralize SOS well when added post-attachment, as the V3 loop is involved in co-receptor engagement. Binley2003 (vaccine antigen design)
• 447-52D: Virion capture assays are not a good predictor of neutralization, and the presentation of epitopes using this assay seems to be different from that of functional Envelope spikes on primary isolates -- F105 and b6 could efficiently block the b12-mediated capture of infectious virions in a virus capture, but did not inhibit b12 neutralization -- Ab 447-52D was able to potently neutralize 89.6 and to neutralize JR-CSF at a high concentration but poorly neutralized ADA -- b12 was potent at neutralizing the three primary virions JR-CSF, ADA, and 89.6, but anti-V3 Abs 447-52D and 19b, which did not neutralize JR-CSF and ADA, captured amounts of p24 equal to or higher than the amounts captured by the neutralizing Ab b12. Poignard2003 (antibody binding site, assay or method development, variant cross-reactivity)
• 447-52D: Review of NAbs. Ferrantelli2002
• 447-52D: Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A(CD4BS) , 4117C (plus others, V3) and 697D (and SC258, V2) were used as controls. He2002
• 447-52D: Conformation-dependent anti-V3 loop Abs may be more cross-reactive, so six new V3 MAbs were generated -- the six new MAbs all bind to the tip of the V3 loop and cross-compete with the MAb 447-52D and are conformationally sensitive -- MAbs showed cross-clade binding to native, intact virions of clades A(N=2), B(N=4), and F(N=2), limited binding to C(N=3) and D(N=3), and did not bind to CRF01(subtype E, N=2) -- the strength binding was highly correlated with percent neutralization using the ghost cell or PHA blast assay -- five well-characterized MAbs were used as controls: anti-V3 447-52D (anti-V3 MAb for competition and neutralization studies), 654 (anti-CD4BS used as a conformation-sensitive MAb control), 1331A (anti-C5 used as a linear binding site MAb control), MAb 246 (anti-gp41 MAb that bound to primary isolates of all clades) -- 447-52D bound to primary isolates from all clades except CRF01 (E), was conformationally sensitive and showed the some of the most potent neutralizing activity. Gorny2002 (variant cross-reactivity)
• 447-52D: The feasibility of determining the NMR structure of the V3(MN) peptide bound to the 447-52D Fab fragment was tested and a general strategy for obtaining NMR structures of V3 peptide-Fab fragments developed -- preliminary NMR spectra for 447-52D complexed to a 23 amino acid V3 peptide was obtained. Sharon2002 (structure)
• 447-52D: Oligomeric gp140 (o-gp140) derived from R5 primary isolate US4 was characterized for use as a vaccine reagent---antigen capture ELISA was used to compare the antigenicity of gp120 and o-gp140 using a panel of well characterized MAbs---447-D recognized the gp120 monomer much more readily than o-gp140, suggesting the V3 loop is less exposed on o-gp140 and on intact virions. Srivastava2002 (antibody binding site, vaccine antigen design)
• 447-52D: A panel of 12 MAbs was used to identify those that could neutralize the dual-tropic primary isolate HIV-1 89.6 -- six gave significant neutralization at 2 to 10 ug/ml: 2F5, 50-69, IgG1b12, 447-52D, 2G12, and 670-D six did not have neutralizing activity: 654-D, 4.8D, 450-D, 246-D, 98-6, and 1281 -- no synergy, only additive effects were seen for pairwise combinations of MAbs, and antagonism was noted between gp41 MAbs 50-69 and 98-6, as well as 98-6 and 2F5. Verrier2001 (antibody interactions, variant cross-reactivity)
• 447-52D: Abs against the V3 loop (50.1, 58.2, 59.1, 257-D, 268-D, 447-52D), CD4BS (IgG1b12, 559-64D, F105), CD4i (17b), and to gp41 (2F5, F240) each showed similar binding efficiency to Env derived from related pairs of primary and TCLA lines (primary: 168P and 320SI, and TCLA: 168C and 320SI-C3.3), but the TCLA lines were much more susceptible to neutralization suggesting that the change in TCLA lines that make them more susceptible to NAbs alters some step after binding -- the dissociation constant, Kd of 447-52D for the cell associated primary and TCLA Envs was equal, 3nM. York2001 (antibody binding site, variant cross-reactivity, binding affinity)
• 447-52D: Six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- the mutation L544P reduced binding of all MAbs against gp120 by causing conformational changes. Park2000 (antibody binding site)
• 447-52D: A panel of 47 human MAbs was tested against 26 HIV-1 group M primary isolates from clades A through H -- 19 V3 MAbs were tested, and of 494 combinations, 44% displayed some viral binding -- V3 MAbs tended to have the most cross-reactive binding to clade A, B, C, and D isolates, less to E, F, G, and H -- 447-52D showed the highest cross-reactivity, bound to 24/26 viruses tested, but achieved 90% neutralization only against MN, 50% against CA5, and no neutralization was observed for 3 other isolates tested. Nyambi2000 (subtype comparisons)
• 447-52D: Called 447D -- SF162 is a neutralization-resistant HIV-1 isolate -- N-linked glycosylation modifications in the V2 loop of the SF162 gp120 revealed that these sites prevent neutralization by CD4BS MAbs (IgG1b12 and IgGCD4), and protect against neutralization by V3 MAbs (447D and 391-95D) -- V2-region glycosylation site mutations did not alter neutralization resistance to V2 MAbs (G3.4 and G3.136) or CD4i MAbs (17b and 48d) -- V2 glycosylation site modification allows infection of macrophages, probably due to glycosylated forms requiring fewer CCR5 molecules for viral entry. Ly2000 (antibody binding site)
• 447-52D: Ab responses, because of their capacity to alter antigen uptake and processing, can influence helper T cell responses -- CD4BS MAbs or serum Ig from HIV+ individuals inhibited proliferative responses of gp120 specific T cells -- V3 MAbs 447-52-D and 268-10-D did not affect proliferation. Hioe2000
• 447-52D: To determine the antigenicity of virus killed by thermal and chemical inactivation, retention of conformation-dependent neutralization epitopes was examined, and exposure of CD4BS epitopes was found to be enhanced (MAbs IgG1b12, 205-46-9, and 205-43-1) -- binding to 2G12 and 447-52D epitopes was essentially unaltered -- the 17b CD4i epitope was also exposed. Grovit-Ferbas2000 (vaccine antigen design)
• 447-52D: Binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- V3 MAbs 447-52D, 838-D, and 1334 bound with a 7-10 fold preference for the oligomer. Gorny2000b (antibody binding site)
• 447-52D: rgp120 derived from a R5X4 subtype B virus, HIV-1 W61D, was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- TCLA strains showed enhanced 447-52D neutralization sensitivity relative to PBMC-adapted lines (32X increase between HIV-1(M2424/PBMC(p0)) and HIV-1(M2424/H9(p9)) and a >128X increase between HIV-1(W61D/PBMC) and HIV-1(W61D/SupT1) isolates) Beddows1999 (variant cross-reactivity)
• 447-52D: The presence of leukocyte function-associated molecule 1 (LFA-1) promotes virus infectivity and hinders neutralization, and anti-LFA-1 MAbs can enhance the neutralizing effect of anti-HIV V3 MAb 447-52D and anti-HIV CD4BS MAb IgG1b12 -- non-neutralizing anti-HIV CD4BS MAb 654-D did not become neutralizing in the presence of anti-LFA-1 MAbs. Hioe1999
• 447-52D: MAb peptide-reactivity pattern clustered with the immunological related MAbs: 1334, 419, 504, 447, 453 and 537 -- the core amino acids GP tended to be critical for reactivity in this group -- 447 reacted with peptides containing GPGR, but also with many lacking this sequence (GPGQ, for example), and it failed to react with 2/14 peptides containing GPGR, illustrating the importance of context. Zolla-Pazner1999a (antibody binding site, variant cross-reactivity)
• 447-52D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
• 447-52D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- 447-52D was the most potent and cross-reactive of 18 human MAbs tested and was the only MAb which bound to virions from isolates CA20 (subtype F), CA13 (subtype H), and VI526 (subtype G) Nyambi1998 (subtype comparisons)
• 447-52D: Kinetic parameters were measured, and the association rates were similar, but dissociation rate constants were quite variable for V3 MAbs, 1324E was comparable to 447-52D. Gorny1998 (kinetics)
• 447-52D: Ab from gp120 vaccinated individuals prior to infection, who subsequently became HIV infected, could not achieve 90% neutralization of the primary virus by which the individuals were ultimately infected -- these viruses were not particularly refractive to neutralization, as determined by their susceptibility to neutralization by MAbs 2G12, IgG1b12, 2F5 and 447-52D. Connor1998
• 447-52D: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope. Parren1998 (antibody binding site)
• 447-52D: Called 447-52-D -- The tip of the MN V3 loop was inserted into cold causing human rhinovirus 14 (HRV14) -- chimeras were immunoselected, and chimeric viruses were neutralized by anti-V3 loop antibodies, and 447-52D was among the Abs used -- chimeric viruses elicited potent NAbs in guinea pigs against ALA-1 and MN. Smith1998 (vaccine antigen design)
• 447-52D: Inhibits binding of Hx10 to both CD4 positive and negative HeLa cells. Mondor1998 (variant cross-reactivity)
• 447-52D: Called 447-D -- 447-D resistance took longer to acquire in virus with the M184V substituted RT, and had the form (AAC N to TAC Y) at position 5 of the V3 loop, rather than the GPGR to GPGR resistance found with wildtype RT. Inouye1998
• 447-52D: Used as a control for comparison to five V3 RF selected antibodies -- 447-52D was reactive with A, B, and C clade peptides, but not E. Gorny1997 (subtype comparisons)
• 447-52D: Abs that recognize discontinuous epitopes can identify mimotopes from a phage peptide display library -- 447-52D has an epitope involving the tip of the V3 loop, that was previously studied with this method Keller1993 -- in Keller et al., with no competition, LxGPxR was the most common six-mer, 38% of the peptides -- after competition with a gp120 IIIB ligand (QRGPGR)i, RGPxR was the most common and one peptide had the sequence QRGPGR, showing type specific mimotopes can be enriched by strain specific ligand competition protocols Boots1997. Boots1997,Keller1993 (antibody binding site, mimotopes)
• 447-52D: Called 447 -- gp120 can inhibit MIP-1alpha from binding to CCR5, but this inhibitory effect is blocked by pre-incubation of gp120 with three anti-V3 MAbs: 447, 257, 1027 -- MAb 670 which binds in the C5 region had no effect. Hill1997 (co-receptor)
• 447-52D: Neutralizes TCLA strains but not primary isolates. Parren1997 (variant cross-reactivity)
• 447-52D: Viral binding inhibition by 447-D was correlated with neutralization (all other neutralizing MAbs tested showed some correlation except 2F5) Ugolini1997 (antibody binding site)
• 447-52D: Four primary isolates showed distinct patterns of sensitivity to neutralization by polyclonal sera or plasma and MAbs -- BZ167 was the only isolate inhibited by all polyclonal sera and plasma tested, and was also neutralized by 8/17 MAbs, in particular anti-V3 loop (419-D, 447-52D, 782-D, and 838-D), anti-CD4bd (559/64-D, 654-D and 830-D and a cluster II of gp41 directed MAb (98-6) -- isolates 92HT593 and 91US056 were neutralized by V3 loop (419-D, and 447-52D)and cluster II gp41 (98-6) MAbs at higher concentrations -- US4 was neutralized by some of the polyclonal sera/plasma tested and not at all by MAbs individually or by a cocktail of ten MAbs consisting of 419-D, 447-52D, 782-D, 838-D, 559/64-D, 654-D, 450-D, 670-D, 1281-D and 98-6. Hioe1997b (variant cross-reactivity)
• 447-52D: Tested using a resting cell neutralization assay. Hioe1997 (assay or method development)
• 447-52D: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 447-52D bound monomer, oligomer, and neutralized JRFL. Fouts1997 (antibody binding site)
• 447-52D: In a multilaboratory blinded study, failed to consistently neutralize any of nine B clade primary isolates -- many of these isolates had the GPGR motif at the apex of the V3 loop. DSouza1997 (assay or method development, variant cross-reactivity)
• 447-52D: Review: called 447-52-D -- only four epitopes have been described which can stimulate a useful neutralizing response to a broad spectrum of primary isolates, represented by the binding sites of MAbs: 447-52-D, 2G12, Fab b12, and 2F5. Sattentau1996 (variant cross-reactivity, review)
• 447-52D: Neutralizes JR-FL -- strongly inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study. Trkola1996b (co-receptor, variant cross-reactivity)
• 447-52D: Called 447-52-D -- The sulfated polysaccharide curdlan sulfate (CRDS) binds to the Envelope of T-tropic viruses and neutralizes virus -- CRDS inhibits 447-52D binding. Jagodzinski1996 (antibody binding site)
• 447-52D: Neutralizing, no viral enhancing activity. Epitope provided as GPGR, but no details are given. Forthal1995 (complement, enhancing activity)
• 447-52D: Review: the V3 loop motif GPGR is not common outside subtype B isolates, MAb 19b is more cross-reactive than 447-52D. Moore1995c (variant cross-reactivity)
• 447-52D: Binding affected by identity of amino acids flanking GPGR core -- poor breadth of primary virus neutralization. Moore1995b (variant cross-reactivity)
• 447-52D: Neutralization of primary and prototype laboratory HIV-1 isolates using a resting cell assay enhances sensitivity. Zolla-Pazner1995a (assay or method development, variant cross-reactivity)
• 447-52D: Serotyping study using flow-cytometry -- bound only to GPGR V3 loop tips. Zolla-Pazner1995 (antibody binding site)
• 447-52D: Ab-mediated activation of complement on HIV+ cells is higher than Ab independent activation---what has been termed ''Ab independent'' in fact results in part from IgM in normal human serum that is HIV-cross-reactive. Saarloos1995 (complement)
• 447-52D: Called 447 -- The tip of the V3 loop was presented in a mucin backbone -- higher valency correlates with stronger affinity constant. Fontenot1995 (vaccine antigen design)
• 447-52D: Called 447d -- Formalin inactivation of virus at 0.1% formalin for 10 hours at 4 degrees was optimal for inactivation of virus while maintaining epitope integrity. Sattentau1995 (vaccine antigen design)
• 447-52D: Competition studies with human sera from seroconverting individuals showed that anti-CD4 BS antibodies can arise very early in infection, comparable or prior to anti-V3 antibodies. Moore1994d (acute/early infection)
• 447-52D: Mild oxidation of carbohydrate moieties does not alter binding. Gorny1994 (antibody binding site)
• 447-52D: GPGQ in MAL resulted in enhanced dissociation -- GPGQ in CM234 or K14T did not bind -- binding affected by identity of amino acids flanking GPGR core. VanCott1994 (antibody binding site)
• 447-52D: Neutralization synergy in combination with CD4 binding domain MAbs. Laal1994 (antibody interactions)
• 447-52D: Requires GPxR at the tip of the V3 loop, common in B clade -- neutralized primary isolates. Conley1994 (antibody binding site, variant cross-reactivity)
• 447-52D: Complement mediated virolysis of IIIB, but not in the presence of sCD4. Spear1993 (complement)
• 447-52D: Additive neutralization of MN and SF2 when combined with CD4 binding site MAb F105 -- supra-additive neutralization of RF. Cavacini1993 (antibody interactions)
• 447-52D: Peptide phage library showed that any of the residues ADGLMNQRS in the X position tolerated in peptides that react well with the antibody. Keller1993 (antibody binding site, variant cross-reactivity)
• 447-52D: Neutralizes MN and IIIB: GPGR, and binds SF2: GPGR. Gorny1993 (variant cross-reactivity)
• 447-52D: Reacts with MN, NY5, CDC4, SF2, RF, WM52, and HXB2. Karwowska1992a (variant cross-reactivity)
• 447-52D: Describes production of mAb 447-D by EBV transformation of PBMC from an HIV-infected individual, followed by fusion with a heteromyeloma. 60-fold increase in neutralization potency when combined 1:1 with human MAb 588-D. Buchbinder1992 (antibody generation, antibody interactions)
• 447-52D: Requires GPXR at the tip of the V3 loop -- neutralizes a broad array of B clade lab isolates. Gorny1992 (antibody binding site, antibody generation, variant cross-reactivity)

References

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Bricault2018 Christine A. Bricault, James M. Kovacs, Alexander Badamchi-Zadeh, Krisha McKee, Jennifer L. Shields, Bronwyn M. Gunn, George H. Neubauer, Fadi Ghantous, Julia Jennings, Lindsey Gillis, James Perry, Joseph P. Nkolola, Galit Alter, Bing Chen, Kathryn E. Stephenson, Nicole Doria-Rose, John R. Mascola, Michael S. Seaman, and Dan H. Barouch. Neutralizing Antibody Responses following Long-Term Vaccination with HIV-1 Env gp140 in Guinea Pigs. J. Virol., 92(13), 1 Jul 2018. PubMed ID: 29643249. Show all entries for this paper.

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Cai2017 Yongfei Cai, Selen Karaca-Griffin, Jia Chen, Sai Tian, Nicholas Fredette, Christine E. Linton, Sophia Rits-Volloch, Jianming Lu, Kshitij Wagh, James Theiler, Bette Korber, Michael S. Seaman, Stephen C. Harrison, Andrea Carfi, and Bing Chen. Antigenicity-Defined Conformations of an Extremely Neutralization-Resistant HIV-1 Envelope Spike. Proc. Natl. Acad. Sci. U.S.A., 114(17):4477-4482, 25 Apr 2017. PubMed ID: 28396421. Show all entries for this paper.

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Connor1998 R. I. Connor, B. T. Korber, B. S. Graham, B. H. Hahn, D. D. Ho, B. D. Walker, A. U. Neumann, S. H. Vermund, J. Mestecky, S. Jackson, E. Fenamore, Y. Cao, F. Gao, S. Kalams, K. J. Kunstman, D. McDonald, N. McWilliams, A. Trkola, J. P. Moore, and S. M. Wolinsky. Immunological and virological analyses of persons infected by human immunodeficiency virus type 1 while participating in trials of recombinant gp120 subunit vaccines. J. Virol., 72:1552-76, 1998. No gp120-vaccine induced antibodies in a human trial of gp120 MN and SF2 could neutralize the primary viruses that infected the vaccinees. The primary isolates from the infected vaccinees were shown not to be particularly refractive to neutralization by their susceptibility to a panel of neutralizing MAbs. PubMed ID: 9445059. Show all entries for this paper.

Corti2010 Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712. Show all entries for this paper.

Crooks2005 Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980. Show all entries for this paper.

Davenport2011 Thaddeus M. Davenport, Della Friend, Katharine Ellingson, Hengyu Xu, Zachary Caldwell, George Sellhorn, Zane Kraft, Roland K. Strong, and Leonidas Stamatatos. Binding Interactions between Soluble HIV Envelope Glycoproteins and Quaternary-Structure-Specific Monoclonal Antibodies PG9 and PG16. J. Virol., 85(14):7095-7107, Jul 2011. PubMed ID: 21543501. Show all entries for this paper.

Davis2009 Katie L. Davis, Frederic Bibollet-Ruche, Hui Li, Julie M. Decker, Olaf Kutsch, Lynn Morris, Aidy Salomon, Abraham Pinter, James A. Hoxie, Beatrice H. Hahn, Peter D. Kwong, and George M. Shaw. Human Immunodeficiency Virus Type 2 (HIV-2)/HIV-1 Envelope Chimeras Detect High Titers of Broadly Reactive HIV-1 V3-Specific Antibodies in Human Plasma. J. Virol., 83(3):1240-1259, Feb 2009. PubMed ID: 19019969. Show all entries for this paper.

Depetris2012 Rafael S Depetris, Jean-Philippe Julien, Reza Khayat, Jeong Hyun Lee, Robert Pejchal, Umesh Katpally, Nicolette Cocco, Milind Kachare, Evan Massi, Kathryn B. David, Albert Cupo, Andre J. Marozsan, William C. Olson, Andrew B. Ward, Ian A. Wilson, Rogier W. Sanders, and John P Moore. Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers. J. Biol. Chem., 287(29):24239-24254, 13 Jul 2012. PubMed ID: 22645128. Show all entries for this paper.

Derby2006 Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322. Show all entries for this paper.

Derby2007 Nina R. Derby, Sean Gray, Elizabeth Wayner, Dwayne Campogan, Giorgos Vlahogiannis, Zane Kraft, Susan W. Barnett, Indresh K. Srivastava, and Leonidas Stamatatos. Isolation and Characterization of Monoclonal Antibodies Elicited by Trimeric HIV-1 Env gp140 Protein Immunogens. Virology, 366(2):433-445, 30 Sep 2007. PubMed ID: 17560621. Show all entries for this paper.

Dervillez2010 Xavier Dervillez, Volker Klaukien, Ralf Dürr, Joachim Koch, Alexandra Kreutz, Thomas Haarmann, Michaela Stoll, Donghan Lee, Teresa Carlomagno, Barbara Schnierle, Kalle Möbius, Christoph Königs, Christian Griesinger, and Ursula Dietrich. Peptide Ligands Selected with CD4-Induced Epitopes on Native Dualtropic HIV-1 Envelope Proteins Mimic Extracellular Coreceptor Domains and Bind to HIV-1 gp120 Independently of Coreceptor Usage. J. Virol., 84(19):10131-10138, Oct 2010. PubMed ID: 20660187. Show all entries for this paper.

deTaeye2015 Steven W. de Taeye, Gabriel Ozorowski, Alba Torrents de la Peña, Miklos Guttman, Jean-Philippe Julien, Tom L. G. M. van den Kerkhof, Judith A. Burger, Laura K. Pritchard, Pavel Pugach, Anila Yasmeen, Jordan Crampton, Joyce Hu, Ilja Bontjer, Jonathan L. Torres, Heather Arendt, Joanne DeStefano, Wayne C. Koff, Hanneke Schuitemaker, Dirk Eggink, Ben Berkhout, Hansi Dean, Celia LaBranche, Shane Crotty, Max Crispin, David C. Montefiori, P. J. Klasse, Kelly K. Lee, John P. Moore, Ian A. Wilson, Andrew B. Ward, and Rogier W. Sanders. Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-Neutralizing Epitopes. Cell, 163(7):1702-1715, 17 Dec 2015. PubMed ID: 26687358. Show all entries for this paper.

deTaeye2018 Steven W. de Taeye, Alba Torrents de la Peña, Andrea Vecchione, Enzo Scutigliani, Kwinten Sliepen, Judith A. Burger, Patricia van der Woude, Anna Schorcht, Edith E. Schermer, Marit J. van Gils, Celia C. LaBranche, David C. Montefiori, Ian A. Wilson, John P. Moore, Andrew B. Ward, and Rogier W. Sanders. Stabilization of the gp120 V3 Loop through Hydrophobic Interactions Reduces the Immunodominant V3-Directed Non-Neutralizing Response to HIV-1 Envelope Trimers. J. Biol. Chem., 293(5):1688-1701, 2 Feb 2018. PubMed ID: 29222332. Show all entries for this paper.

Dey2008 Antu K. Dey, Kathryn B. David, Neelanjana Ray, Thomas J. Ketas, Per J. Klasse, Robert W. Doms, and John P. Moore. N-Terminal Substitutions in HIV-1 gp41 Reduce the Expression of Non-Trimeric Envelope Glycoproteins on the Virus. Virology, 372(1):187-200, 1 Mar 2008. PubMed ID: 18031785. Show all entries for this paper.

Dhillon2007 Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160. Show all entries for this paper.

Dhillon2008 Amandeep K. Dhillon, Robyn L. Stanfield, Miroslaw K. Gorny, Constance Williams, Susan Zolla-Pazner, and Ian A. Wilson. Structure Determination of an Anti-HIV-1 Fab 447-52D-Peptide Complex from an Epitaxially Twinned Data Set. Acta. Crystallogr. D Biol. Crystallogr., D64(7):792-802, Jul 2008. PubMed ID: 18566514. Show all entries for this paper.

Doria-Rose2010 Nicole A. Doria-Rose, Rachel M. Klein, Marcus G. Daniels, Sijy O'Dell, Martha Nason, Alan Lapedes, Tanmoy Bhattacharya, Stephen A. Migueles, Richard T. Wyatt, Bette T. Korber, John R. Mascola, and Mark Connors. Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables. J. Virol., 84(3):1631-1636, Feb 2010. PubMed ID: 19923174. Show all entries for this paper.

Douagi2010 Iyadh Douagi, Mattias N. E. Forsell, Christopher Sundling, Sijy O'Dell, Yu Feng, Pia Dosenovic, Yuxing Li, Robert Seder, Karin Loré, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. Influence of Novel CD4 Binding-Defective HIV-1 Envelope Glycoprotein Immunogens on Neutralizing Antibody and T-Cell Responses in Nonhuman Primates. J. Virol., 84(4):1683-1695, Feb 2010. PubMed ID: 19955308. Show all entries for this paper.

DSouza1997 M. P. D'Souza, D. Livnat, J. A. Bradac, S. H. Bridges, the AIDS Clinical Trials Group Antibody Selection Working Group, and Collaborating Investigators. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. J. Infect. Dis., 175:1056-1062, 1997. Five laboratories evaluated neutralization of nine primary B clade isolates by a coded panel of seven human MAbs to HIV-1 subtype B envelope. IgG1b12, 2G12, 2F5 showed potent and broadly cross-reactive neutralizing ability; F105, 447/52-D, 729-D, 19b did not neutralize the primary isolates. PubMed ID: 9129066. Show all entries for this paper.

Eda2006 Yasuyuki Eda, Toshio Murakami, Yasushi Ami, Tadashi Nakasone, Mari Takizawa, Kenji Someya, Masahiko Kaizu, Yasuyuki Izumi, Naoto Yoshino, Shuzo Matsushita, Hirofumi Higuchi, Hajime Matsui, Katsuaki Shinohara, Hiroaki Takeuchi, Yoshio Koyanagi, Naoki Yamamoto, and Mitsuo Honda. Anti-V3 Humanized Antibody KD-247 Effectively Suppresses Ex Vivo Generation of Human Immunodeficiency Virus Type 1 and Affords Sterile Protection of Monkeys against a Heterologous Simian/Human Immunodeficiency Virus Infection. J. Virol., 80(11):5563-5570, Jun 2006. PubMed ID: 16699037. Show all entries for this paper.

Eda2006a Yasuyuki Eda, Mari Takizawa, Toshio Murakami, Hiroaki Maeda, Kazuhiko Kimachi, Hiroshi Yonemura, Satoshi Koyanagi, Kouichi Shiosaki, Hirofumi Higuchi, Keiichi Makizumi, Toshihiro Nakashima, Kiyoshi Osatomi, Sachio Tokiyoshi, Shuzo Matsushita, Naoki Yamamoto, and Mitsuo Honda. Sequential Immunization with V3 Peptides from Primary Human Immunodeficiency Virus Type 1 Produces Cross-Neutralizing Antibodies against Primary Isolates with a Matching Narrow-Neutralization Sequence Motif. J. Virol., 80(11):5552-5562, Jun 2006. PubMed ID: 16699036. Show all entries for this paper.

Fenyo2009 Eva Maria Fenyö, Alan Heath, Stefania Dispinseri, Harvey Holmes, Paolo Lusso, Susan Zolla-Pazner, Helen Donners, Leo Heyndrickx, Jose Alcami, Vera Bongertz, Christian Jassoy, Mauro Malnati, David Montefiori, Christiane Moog, Lynn Morris, Saladin Osmanov, Victoria Polonis, Quentin Sattentau, Hanneke Schuitemaker, Ruengpung Sutthent, Terri Wrin, and Gabriella Scarlatti. International Network for Comparison of HIV Neutralization Assays: The NeutNet Report. PLoS One, 4(2):e4505, 2009. PubMed ID: 19229336. Show all entries for this paper.

Ferrantelli2002 Flavia Ferrantelli and Ruth M. Ruprecht. Neutralizing Antibodies Against HIV --- Back in the Major Leagues? Curr. Opin. Immunol., 14(4):495-502, Aug 2002. PubMed ID: 12088685. Show all entries for this paper.

Fontenot1995 J. D. Fontenot, T. C. VanCott, B. S. Parekh, C. P. Pau, J. R. George, D. L. Birx, S. Zolla-Pazner, M. K. Gorny, and J. M. Gatewood. Presentation of HIV V3 Loop Epitopes for Enhanced Antigenicity, Immunogenicity and Diagnostic Potential. AIDS, 9:1121-1129, 1995. PubMed ID: 8519447. Show all entries for this paper.

Forsell2008 Mattias N. E. Forsell, Barna Dey, Andreas Mörner, Krisha Svehla, Sijy O'dell, Carl-Magnus Högerkorp, Gerald Voss, Rigmor Thorstensson, George M. Shaw, John R. Mascola, Gunilla B. Karlsson Hedestam, and Richard T. Wyatt. B Cell Recognition of the Conserved HIV-1 Co-Receptor Binding Site Is Altered by Endogenous Primate CD4. PLoS Pathog., 4(10):e1000171, 2008. PubMed ID: 18833294. Show all entries for this paper.

Forsman2008 Anna Forsman, Els Beirnaert, Marlén M. I. Aasa-Chapman, Bart Hoorelbeke, Karolin Hijazi, Willie Koh, Vanessa Tack, Agnieszka Szynol, Charles Kelly, Áine McKnight, Theo Verrips, Hans de Haard, and Robin A Weiss. Llama Antibody Fragments with Cross-Subtype Human Immunodeficiency Virus Type 1 (HIV-1)-Neutralizing Properties and High Affinity for HIV-1 gp120. J. Virol., 82(24):12069-12081, Dec 2008. PubMed ID: 18842738. Show all entries for this paper.

Forthal1995 D. N. Forthal, G. Landucci, M. K. Gorny, S. Zolla-Pazner, and W. E. Robinson, Jr. Functional Activities of 20 Human Immunodeficiency Virus Type 1 (HIV-1)-Specific Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 11:1095-1099, 1995. A series of tests were performed on 20 human monoclonal antibodies to assess their potential therapeutic utility. Antibodies were tested for potentially harmful complement-mediated antibody enhancing activity (C-ADE), and for potentially beneficial neutralizing activity and antibody dependent cellular cytotoxicity ADCC. PubMed ID: 8554906. Show all entries for this paper.

Forthal2009 Donald N. Forthal and Christiane Moog. Fc Receptor-Mediated Antiviral Antibodies. Curr. Opin. HIV AIDS, 4(5):388-393, Sep 2009. PubMed ID: 20048702. Show all entries for this paper.

Fouts1997 T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632. Show all entries for this paper.

Gao2005a Feng Gao, Eric A. Weaver, Zhongjing Lu, Yingying Li, Hua-Xin Liao, Benjiang Ma, S Munir Alam, Richard M. Scearce, Laura L. Sutherland, Jae-Sung Yu, Julie M. Decker, George M. Shaw, David C. Montefiori, Bette T. Korber, Beatrice H. Hahn, and Barton F. Haynes. Antigenicity and Immunogenicity of a Synthetic Human Immunodeficiency Virus Type 1 Group M Consensus Envelope Glycoprotein. J. Virol., 79(2):1154-1163, Jan 2005. PubMed ID: 15613343. Show all entries for this paper.

Gazarian2013 Karlen G. Gazarian, Yadira Palacios-Rodríguez, Tatiana G. Gazarian, and Leonor Huerta. HIV-1 V3 Loop Crown Epitope-Focused Mimotope Selection by Patient Serum from Random Phage Display Libraries: Implications for the Epitope Structural Features. Mol. Immunol., 54(2):148-156, Jun 2013. PubMed ID: 23270686. Show all entries for this paper.

Gonzalez2010 Nuria Gonzalez, Amparo Alvarez, and Jose Alcami. Broadly Neutralizing Antibodies and their Significance for HIV-1 Vaccines. Curr. HIV Res., 8(8):602-612, Dec 2010. PubMed ID: 21054253. Show all entries for this paper.

Gorny1992 M. K. Gorny, A. J. Conley, S. Karwowska, A. Buchbinder, J.-Y. Xu, E. A. Emini, S. Koenig, and S. Zolla-Pazner. Neutralization of Diverse Human Immunodeficiency Virus Type 1 Variants by an Anti-V3 Human Monoclonal Antibody. J. Virol., 66:7538-7542, 1992. PubMed ID: 1433529. Show all entries for this paper.

Gorny1993 M. K. Gorny, J.-Y. Xu, S. Karwowska, A. Buchbinder, and S. Zolla-Pazner. Repertoire of Neutralizing Human Monoclonal Antibodies Specific for The V3 Domain of HIV-1 gp120. J. Immunol., 150:635-643, 1993. Characterizaton of 12 human MAbs that bind and neutralize the MN isolate with 50\% neutralization. Two of these antibodies also bound and neutralized IIIB: 447-52-D and 694/98-D; all others could not bind HXB2 peptides. All but two, 418-D and 412-D could bind to SF2 peptides. PubMed ID: 7678279. Show all entries for this paper.

Gorny1994 M. K. Gorny, J. P. Moore, A. J. Conley, S. Karwowska, J. Sodroski, C. Williams, S. Burda, L. J. Boots, and S. Zolla-Pazner. Human Anti-V2 Monoclonal Antibody That Neutralizes Primary but Not Laboratory Isolates of Human Immunodeficiency Virus Type 1. J. Virol., 68:8312-8320, 1994. Detailed characterization of the MAb 697-D. PubMed ID: 7525987. Show all entries for this paper.

Gorny1997 Miroslaw K. Gorny, Thomas C. VanCott, Catarina Hioe, Zimra R. Israel, Nelson L. Michael, Anthony J. Conley, Constance Williams, Joseph A. Kessler II, Padmasree Chigurupati, Sherri Burda, and Susan Zolla-Pazner. Human Monoclonal Antibodies to the V3 Loop of HIV-1 With Intra- and Interclade Cross-Reactivity. J. Immunol., 159:5114-5122, 1997. PubMed ID: 9366441. Show all entries for this paper.

Gorny1998 M. K. Gorny, J. R. Mascola, Z. R. Israel, T. C. VanCott, C. Williams, P. Balfe, C. Hioe, S. Brodine, S. Burda, and S. Zolla-Pazner. A Human Monoclonal Antibody Specific for the V3 Loop of HIV Type 1 Clade E Cross-Reacts with Other HIV Type 1 Clades. AIDS Res. Hum. Retroviruses, 14:213-221, 1998. PubMed ID: 9491911. Show all entries for this paper.

Gorny2000b M. K. Gorny, T. C. VanCott, C. Williams, K. Revesz, and S. Zolla-Pazner. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology, 267:220-8, 2000. PubMed ID: 10662617. Show all entries for this paper.

Gorny2002 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Sandra Cohen, Victoria R. Polonis, William J. Honnen, Samuel C. Kayman, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Human Monoclonal Antibodies Specific for Conformation-Sensitive Epitopes of V3 Neutralize Human Immunodeficiency Virus Type 1 Primary Isolates from Various Clades. J. Virol., 76(18):9035-9045, Sep 2002. PubMed ID: 12186887. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Gorny2004 Miroslaw K. Gorny, Kathy Revesz, Constance Williams, Barbara Volsky, Mark K. Louder, Christopher A. Anyangwe, Chavdar Krachmarov, Samuel C. Kayman, Abraham Pinter, Arthur Nadas, Phillipe N. Nyambi, John R. Mascola, and Susan Zolla-Pazner. The V3 Loop is Accessible on the Surface of Most Human Immunodeficiency Virus Type 1 Primary Isolates and Serves as a Neutralization Epitope. J. Virol., 78(5):2394-2404, Mar 2004. PubMed ID: 14963135. Show all entries for this paper.

Gorny2005 Miroslaw K. Gorny, Leonidas Stamatatos, Barbara Volsky, Kathy Revesz, Constance Williams, Xiao-Hong Wang, Sandra Cohen, Robert Staudinger, and Susan Zolla-Pazner. Identification of a New Quaternary Neutralizing Epitope on Human Immunodeficiency Virus Type 1 Virus Particles. J. Virol., 79(8):5232-5237, Apr 2005. PubMed ID: 15795308. Show all entries for this paper.

Gorny2006 Miroslaw K. Gorny, Constance Williams, Barbara Volsky, Kathy Revesz, Xiao-Hong Wang, Sherri Burda, Tetsuya Kimura, Frank A. J. Konings, Arthur Nádas, Christopher A. Anyangwe, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, and Susan Zolla-Pazner. Cross-Clade Neutralizing Activity of Human Anti-V3 Monoclonal Antibodies Derived from the Cells of Individuals Infected with Non-B Clades of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):6865-6872, Jul 2006. PubMed ID: 16809292. Show all entries for this paper.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.

Grovit-Ferbas2000 K. Grovit-Ferbas, J. F. Hsu, J. Ferbas, V. Gudeman, and I. S. Chen. Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1. J. Virol., 74(13):5802-9, Jul 2000. URL: http://jvi.asm.org/cgi/content/full/74/13/5802. PubMed ID: 10846059. Show all entries for this paper.

Grundner2005 Christoph Grundner, Yuxing Li, Mark Louder, John Mascola, Xinzhen Yang, Joseph Sodroski, and Richard Wyatt. Analysis of the Neutralizing Antibody Response Elicited in Rabbits by Repeated Inoculation with Trimeric HIV-1 Envelope Glycoproteins. Virology, 331(1):33-46, 5 Jan 2005. PubMed ID: 15582651. Show all entries for this paper.

Guzzo2018 Christina Guzzo, Peng Zhang, Qingbo Liu, Alice L. Kwon, Ferzan Uddin, Alexandra I. Wells, Hana Schmeisser, Raffaello Cimbro, Jinghe Huang, Nicole Doria-Rose, Stephen D. Schmidt, Michael A. Dolan, Mark Connors, John R. Mascola, and Paolo Lusso. Structural Constraints at the Trimer Apex Stabilize the HIV-1 Envelope in a Closed, Antibody-Protected Conformation. mBio, 9(6), 11 Dec 2018. PubMed ID: 30538178. Show all entries for this paper.

Haldar2011 Bijayesh Haldar, Sherri Burda, Constance Williams, Leo Heyndrickx, Guido Vanham, Miroslaw K. Gorny, and Phillipe Nyambi. Longitudinal Study of Primary HIV-1 Isolates in Drug-Naïve Individuals Reveals the Emergence of Variants Sensitive to Anti-HIV-1 Monoclonal Antibodies. PLoS One, 6(2):e17253, 2011. PubMed ID: 21383841. Show all entries for this paper.

Haynes2005 Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590. Show all entries for this paper.

Haynes2006 Barton F. Haynes, Benjiang Ma, David C. Montefiori, Terri Wrin, Christos J. Petropoulos, Laura L. Sutherland, Richard M. Scearce, Cathrine. Denton, Shi-Mao Xia, Bette T. Korber, and Hua-Xin Liao. Analysis of HIV-1 Subtype B Third Variable Region Peptide Motifs for Induction of Neutralizing Antibodies against HIV-1 Primary Isolates. Virology, 345(1):44-55, 5 Feb 2006. PubMed ID: 16242749. Show all entries for this paper.

Haynes2006a Barton F. Haynes and David C. Montefiori. Aiming to Induce Broadly Reactive Neutralizing Antibody Responses with HIV-1 Vaccine Candidates. Expert Rev. Vaccines, 5(4):579-595, Aug 2006. PubMed ID: 16989638. Show all entries for this paper.

He2002 Yuxian He, William J. Honnen, Chavdar P. Krachmarov, Michael Burkhart, Samuel C. Kayman, Jose Corvalan, and Abraham Pinter. Efficient Isolation of Novel Human Monoclonal Antibodies with Neutralizing Activity Against HIV-1 from Transgenic Mice Expressing Human Ig Loci. J. Immunol., 169(1):595-605, 1 Jul 2002. PubMed ID: 12077293. Show all entries for this paper.

Hill1997 C. M. Hill, H. Deng, D. Unutmaz, V. N. Kewalramani, L. Bastiani, M. K. Gorny, S. Zolla-Pazner, and D. R. Littman. Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor. J. Virol., 71:6296-6304, 1997. PubMed ID: 9261346. Show all entries for this paper.

Hioe1997 C. Hioe, S. Burda, P. Chigurupati, S. Xu, and S. Zolla-Pazner. Resting Cell Neutralization Assay for HIV-1 Primary Isolates. Methods: A companion to Methods in Enzymology, 12:300-305, 1997. A technique is described for detecting the activity of neutralizing polyclonal or MAbs against HIV-1 primary isolates, using unstimulated PBMC as the target cell. PubMed ID: 9245610. Show all entries for this paper.

Hioe1997b C. E. Hioe, S. Xu, P. Chigurupati, S. Burda, C. Williams, M. K. Gorny, and S. Zolla-Pazner. Neutralization of HIV-1 Primary Isolates by Polyclonal and Monoclonal Human Antibodies. Int. Immunol., 9(9):1281-1290, Sep 1997. PubMed ID: 9310831. Show all entries for this paper.

Hioe1999 C. E. Hioe, J. E. Hildreth, and S. Zolla-Pazner. Enhanced HIV Type 1 Neutralization by Human Anti-Glycoprotein 120 Monoclonal Antibodies in the Presence of Monoclonal Antibodies to Lymphocyte Function-Associated Molecule 1. AIDS Res. Hum. Retroviruses, 15:523-531, 1999. PubMed ID: 10221529. Show all entries for this paper.

Hioe2000 C. E. Hioe, G. J. Jones, A. D. Rees, S. Ratto-Kim, D. Birx, C. Munz, M. K. Gorny, M. Tuen, and S. Zolla-Pazner. Anti-CD4-Binding Domain Antibodies Complexed with HIV Type 1 Glycoprotein 120 Inhibit CD4+ T Cell-Proliferative Responses to Glycoprotein 120. AIDS Res. Hum. Retroviruses, 16:893-905, 2000. PubMed ID: 10875615. Show all entries for this paper.

Hioe2009 Catarina E. Hioe, Maria Luisa Visciano, Rajnish Kumar, Jianping Liu, Ethan A. Mack, Rachel E. Simon, David N. Levy, and Michael Tuen. The Use of Immune Complex Vaccines to Enhance Antibody Responses against Neutralizing Epitopes on HIV-1 Envelope gp120. Vaccine, 28(2):352-360, 11 Dec 2009. PubMed ID: 19879224. Show all entries for this paper.

Hioe2010 Catarina E. Hioe, Terri Wrin, Michael S. Seaman, Xuesong Yu, Blake Wood, Steve Self, Constance Williams, Miroslaw K. Gorny, and Susan Zolla-Pazner. Anti-V3 Monoclonal Antibodies Display Broad Neutralizing Activities against Multiple HIV-1 Subtypes. PLoS One, 5(4):e10254, 2010. PubMed ID: 20421997. Show all entries for this paper.

Hogan2018 Michael J. Hogan, Angela Conde-Motter, Andrea P. O. Jordan, Lifei Yang, Brad Cleveland, Wenjin Guo, Josephine Romano, Houping Ni, Norbert Pardi, Celia C. LaBranche, David C. Montefiori, Shiu-Lok Hu, James A. Hoxie, and Drew Weissman. Increased Surface Expression of HIV-1 Envelope Is Associated with Improved Antibody Response in Vaccinia Prime/Protein Boost Immunization. Virology, 514:106-117, 15 Jan 2018. PubMed ID: 29175625. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Holl2006a Vincent Holl, Maryse Peressin, Sylvie Schmidt, Thomas Decoville, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Efficient Inhibition of HIV-1 Replication in Human Immature Monocyte-Derived Dendritic Cells by Purified Anti-HIV-1 IgG without Induction of Maturation. Blood, 107(11):4466-4474, 1 Jun 2006. PubMed ID: 16469871. Show all entries for this paper.

Hoxie2010 James A. Hoxie. Toward an Antibody-Based HIV-1 Vaccine. Annu. Rev. Med., 61:135-52, 2010. PubMed ID: 19824826. Show all entries for this paper.

Hu2007 Qinxue Hu, Naheed Mahmood, and Robin J. Shattock. High-Mannose-Specific Deglycosylation of HIV-1 gp120 Induced by Resistance to Cyanovirin-N and the Impact on Antibody Neutralization. Virology, 368(1):145-154, 10 Nov 2007. PubMed ID: 17658575. Show all entries for this paper.

Huang2005 Chih-chin Huang, Min Tang, Mei-Yun Zhang, Shahzad Majeed, Elizabeth Montabana, Robyn L. Stanfield, Dimiter S. Dimitrov, Bette Korber, Joseph Sodroski, Ian A. Wilson, Richard Wyatt, and Peter D. Kwong. Structure of a V3-Containing HIV-1 gp120 Core. Science, 310(5750):1025-1028, 11 Nov 2005. PubMed ID: 16284180. Show all entries for this paper.

Huang2010 Kuan-Hsiang G. Huang, David Bonsall, Aris Katzourakis, Emma C. Thomson, Sarah J. Fidler, Janice Main, David Muir, Jonathan N. Weber, Alexander J. Frater, Rodney E. Phillips, Oliver G. Pybus, Philip J. R. Goulder, Myra O. McClure, Graham S. Cooke, and Paul Klenerman. B-Cell Depletion Reveals a Role for Antibodies in the Control of Chronic HIV-1 Infection. Nat. Commun., 1:102, 2010. PubMed ID: 20981030. Show all entries for this paper.

Huber2007 M. Huber and A. Trkola. Humoral Immunity to HIV-1: Neutralization and Beyond. J. Intern. Med., 262(1):5-25, Jul 2007. PubMed ID: 17598812. Show all entries for this paper.

Inouye1998 P. Inouye, E. Cherry, M. Hsu, S. Zolla-Pazner, and M. A. Wainberg. Neutralizing Antibodies Directed against the V3 Loop Select for Different Escape Variants in a Virus with Mutated Reverse Transcriptase (M184V) Than in Wild-Type Human Immunodeficiency Virus Type 1. AIDS Res. Hum. Retroviruses, 14:735-740, 1998. The M184V substitution in RT yields high level resistance to 3TC and low level resistance to ddI and ddC, and alters the properties of RT. Virus containing the wt form of RT grown in the presence of the MAb 447-D develops 447-D resistance in 36 days, with the GPGR to GPGK substitutions (AGA(R) to AAA(K)). 447-D resistance took longer to acquire in virus with the M184V substituted RT, and had the form CTRPN to CTRPY (AAC(N) to TAC(Y)) at position 5 of the V3 loop. PubMed ID: 9643373. Show all entries for this paper.

Jagodzinski1996 P. P. Jagodzinski, J. Wustner, D. Kmieciak, T. J. Wasik, A. Fertala, A. L. Sieron, M. Takahashi, T. Tsuji, T. Mimura, M. S. Fung, M. K. Gorny, M. Kloczewiak, Y. Kaneko, and D. Kozbor. Role of the V2, V3, and CD4-Binding Domains of GP120 in Curdlan Sulfate Neutralization Sensitivity of HIV-1 during Infection of T Lymphocytes. Virology, 226:217-227, 1996. PubMed ID: 8955041. Show all entries for this paper.

Jiang2010 Xunqing Jiang, Valicia Burke, Maxim Totrov, Constance Williams, Timothy Cardozo, Miroslaw K. Gorny, Susan Zolla-Pazner, and Xiang-Peng Kong. Conserved Structural Elements in the V3 Crown of HIV-1 gp120. Nat. Struct. Mol. Biol., 17(8):955-961, Aug 2010. PubMed ID: 20622876. Show all entries for this paper.

Johnson2017 Jacklyn Johnson, Yinjie Zhai, Hamid Salimi, Nicole Espy, Noah Eichelberger, Orlando DeLeon, Yunxia O'Malley, Joel Courter, Amos B. Smith, III, Navid Madani, Joseph Sodroski, and Hillel Haim. Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States. J. Virol., 91(15), 1 Aug 2017. PubMed ID: 28490588. Show all entries for this paper.

Kang2005 Sang-Moo Kang, Fu Shi Quan, Chunzi Huang, Lizheng Guo, Ling Ye, Chinglai Yang, and Richard W. Compans. Modified HIV Envelope Proteins with Enhanced Binding to Neutralizing Monoclonal Antibodies. Virology, 331(1):20-32, 5 Jan 2005. PubMed ID: 15582650. Show all entries for this paper.

Karwowska1992a S. Karwowska, M. K. Gorny, A. Buchbinder, and S. Zolla-Pazner. Type-specific human monoclonal antibodies cross-react with the V3-loop of various HIV-1 isolates. Vaccines 92, :171-174, 1992. Editors: F. Brown, H. S. Ginsberg and R. Lerner, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. Show all entries for this paper.

Keele2008 Brandon F. Keele, Elena E. Giorgi, Jesus F. Salazar-Gonzalez, Julie M. Decker, Kimmy T. Pham, Maria G. Salazar, Chuanxi Sun, Truman Grayson, Shuyi Wang, Hui Li, Xiping Wei, Chunlai Jiang, Jennifer L. Kirchherr, Feng Gao, Jeffery A. Anderson, Li-Hua Ping, Ronald Swanstrom, Georgia D. Tomaras, William A. Blattner, Paul A. Goepfert, J. Michael Kilby, Michael S. Saag, Eric L. Delwart, Michael P. Busch, Myron S. Cohen, David C. Montefiori, Barton F. Haynes, Brian Gaschen, Gayathri S. Athreya, Ha Y. Lee, Natasha Wood, Cathal Seoighe, Alan S. Perelson, Tanmoy Bhattacharya, Bette T. Korber, Beatrice H. Hahn, and George M. Shaw. Identification and Characterization of Transmitted and Early Founder Virus Envelopes in Primary HIV-1 Infection. Proc. Natl. Acad. Sci. U.S.A., 105(21):7552-7557, 27 May 2008. PubMed ID: 18490657. Show all entries for this paper.

Keller1993 P. M. Keller, B. A. Arnold, A. R. Shaw, R. L. Tolman, F. Van Middlesworth, S. Bondy, V. K. Rusiecki, S. Koenig, S. Zolla-Pazner, P. Conard, E. A. Emini, and A. J. Conley. Identification of HIV Vaccine Candidate Peptides by Screening Random Phage Epitope Libraries. Virology, 193:709-716, 1993. A library of 15 mers was screened for reactivity with 447-52D. 100s of 15 mers reacted, of which 70 were sequenced. All but one contained the motif GPXR. PubMed ID: 7681612. Show all entries for this paper.

Kessler2003 Naama Kessler, Anat Zvi, Min Ji, Michal Sharon, Osnat Rosen, Rina Levy, Miroslaw Gorny, Suzan Zolla-Pazner, and Jacob Anglister. Expression, Purification, and Isotope Labeling of the Fv of the Human HIV-1 Neutralizing Antibody 447-52D for NMR Studies. Protein. Expr. Purif., 29(2):291-303, Jun 2003. PubMed ID: 12767822. Show all entries for this paper.

Kimura2009 Tetsuya Kimura, Xiao-Hong Wang, Constance Williams, Susan Zolla-Pazner, and Miroslaw K. Gorny. Human Monoclonal Antibody 2909 Binds to Pseudovirions Expressing Trimers but not Monomeric HIV-1 Envelope Proteins. Hum. Antibodies, 18(1-2):35-40, 2009. PubMed ID: 19478397. Show all entries for this paper.

Klein2013 Florian Klein, Ron Diskin, Johannes F. Scheid, Christian Gaebler, Hugo Mouquet, Ivelin S. Georgiev, Marie Pancera, Tongqing Zhou, Reha-Baris Incesu, Brooks Zhongzheng Fu, Priyanthi N. P. Gnanapragasam, Thiago Y. Oliveira, Michael S. Seaman, Peter D. Kwong, Pamela J. Bjorkman, and Michel C. Nussenzweig. Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization. Cell, 153(1):126-138, 28 Mar 2013. PubMed ID: 23540694. Show all entries for this paper.

Korber2009 Bette Korber and S. Gnanakaran. The Implications of Patterns in HIV Diversity for Neutralizing Antibody Induction and Susceptibility. Curr. Opin. HIV AIDS, 4(5):408-417, Sep 2009. PubMed ID: 20048705. Show all entries for this paper.

Krachmarov2005 Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306. Show all entries for this paper.

Krachmarov2006 C. P. Krachmarov, W. J. Honnen, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and Abraham Pinter. Factors Determining the Breadth and Potency of Neutralization by V3-Specific Human Monoclonal Antibodies Derived from Subjects Infected with Clade A or Clade B Strains of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):7127-7135, Jul 2006. PubMed ID: 16809318. Show all entries for this paper.

Kraft2007 Zane Kraft, Nina R. Derby, Ruth A. McCaffrey, Rachel Niec, Wendy M. Blay, Nancy L. Haigwood, Eirini Moysi, Cheryl J. Saunders, Terri Wrin, Christos J. Petropoulos, M. Juliana McElrath, and Leonidas Stamatatos. Macaques Infected with a CCR5-Tropic Simian/Human Immunodeficiency Virus (SHIV) Develop Broadly Reactive Anti-HIV Neutralizing Antibodies. J. Virol., 81(12):6402-6411, Jun 2007. PubMed ID: 17392364. Show all entries for this paper.

Kramer2007 Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119. Show all entries for this paper.

Kwong2009a Peter D. Kwong and Ian A. Wilson. HIV-1 and Influenza Antibodies: Seeing Antigens in New Ways. Nat. Immunol., 10(6):573-578, Jun 2009. PubMed ID: 19448659. Show all entries for this paper.

Laal1994 Suman Laal, Sherri Burda, Miroslav K. Gorny, Sylwia Karwowska, Aby Buchbinder, and Susan Zolla-Pazner. Synergistic Neutralization of Human Immunodeficiency Virus Type 1 by Combinations of Human Monoclonal Antibodies. J. Virol., 68(6):4001-4008, Jun 1994. PubMed ID: 7514683. Show all entries for this paper.

Law2007 Mansun Law, Rosa M. F. Cardoso, Ian A. Wilson, and Dennis R. Burton. Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy. J. Virol., 81(8):4272-4285, Apr 2007. PubMed ID: 17267498. Show all entries for this paper.

Lewis1995 C. M. Lewis, G. F. Hollis, G. E. Mark, 3rd, J. S. Tung, and S. W. Ludmerer. Use of a Novel Mutagenesis Strategy, Optimized Residue Substitution, to Decrease the Off-Rate of an Anti-gp120 Antibody. Mol. Immunol., 32(14-15):1065-1072, Oct 1995. PubMed ID: 8544856. Show all entries for this paper.

Li2005a Ming Li, Feng Gao, John R. Mascola, Leonidas Stamatatos, Victoria R. Polonis, Marguerite Koutsoukos, Gerald Voss, Paul Goepfert, Peter Gilbert, Kelli M. Greene, Miroslawa Bilska, Denise L Kothe, Jesus F. Salazar-Gonzalez, Xiping Wei, Julie M. Decker, Beatrice H. Hahn, and David C. Montefiori. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 79(16):10108-10125, Aug 2005. PubMed ID: 16051804. Show all entries for this paper.

Li2007a Yuxing Li, Stephen A. Migueles, Brent Welcher, Krisha Svehla, Adhuna Phogat, Mark K. Louder, Xueling Wu, George M. Shaw, Mark Connors, Richard T. Wyatt, and John R. Mascola. Broad HIV-1 Neutralization Mediated by CD4-Binding Site Antibodies. Nat. Med., 13(9):1032-1034, Sep 2007. PubMed ID: 17721546. Show all entries for this paper.

Li2009c Yuxing Li, Krisha Svehla, Mark K. Louder, Diane Wycuff, Sanjay Phogat, Min Tang, Stephen A. Migueles, Xueling Wu, Adhuna Phogat, George M. Shaw, Mark Connors, James Hoxie, John R. Mascola, and Richard Wyatt. Analysis of Neutralization Specificities in Polyclonal Sera Derived from Human Immunodeficiency Virus Type 1-Infected Individuals. J Virol, 83(2):1045-1059, Jan 2009. PubMed ID: 19004942. Show all entries for this paper.

Lin2007 George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109. Show all entries for this paper.

Ling2004 Hong Ling, Peng Xiao, Osamu Usami, and Toshio Hattori. Thrombin Activates Envelope Glycoproteins of HIV Type 1 and Enhances Fusion. Microbes Infect., 6(5):414-420, Apr 2004. PubMed ID: 15109955. Show all entries for this paper.

Louder2005 Mark K. Louder, Anna Sambor, Elena Chertova, Tai Hunte, Sarah Barrett, Fallon Ojong, Eric Sanders-Buell, Susan Zolla-Pazner, Francine E. McCutchan, James D. Roser, Dana Gabuzda, Jeffrey D. Lifson, and John R. Mascola. HIV-1 Envelope Pseudotyped Viral Vectors and Infectious Molecular Clones Expressing the Same Envelope Glycoprotein Have a Similar Neutralization Phenotype, but Culture in Peripheral Blood Mononuclear Cells Is Associated with Decreased Neutralization Sensitivity. Virology, 339(2):226-238, 1 Sep 2005. PubMed ID: 16005039. Show all entries for this paper.

Lusso2005 Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935. Show all entries for this paper.

Ly2000 A. Ly and L. Stamatatos. V2 Loop Glycosylation of the Human Immunodeficiency Virus Type 1 SF162 Envelope Facilitates Interaction of this Protein with CD4 and CCR5 Receptors and Protects the Virus from Neutralization by Anti-V3 Loop and Anti-CD4 Binding Site Antibodies. J. Virol., 74:6769-6776, 2000. PubMed ID: 10888615. Show all entries for this paper.

Martin2008 Grégoire Martin, Yide Sun, Bernadette Heyd, Olivier Combes, Jeffrey B Ulmer, Anne Descours, Susan W Barnett, Indresh K Srivastava, and Loïc Martin. A Simple One-Step Method for the Preparation of HIV-1 Envelope Glycoprotein Immunogens Based on a CD4 Mimic Peptide. Virology, 381(2):241-250, 25 Nov 2008. PubMed ID: 18835005. Show all entries for this paper.

Martin2011 Grégoire Martin, Brian Burke, Robert Thaï, Antu K. Dey, Olivier Combes, Bernadette Heyd, Anthony R. Geonnotti, David C. Montefiori, Elaine Kan, Ying Lian, Yide Sun, Toufik Abache, Jeffrey B. Ulmer, Hocine Madaoui, Raphaël Guérois, Susan W. Barnett, Indresh K. Srivastava, Pascal Kessler, and Loïc Martin. Stabilization of HIV-1 Envelope in the CD4-Bound Conformation through Specific Cross-Linking of a CD4 Mimetic. J. Biol. Chem., 286(24):21706-21716, 17 Jun 2011. PubMed ID: 21487012. Show all entries for this paper.

Martin-Garcia2005 Julio Martín-García, Simon Cocklin, Irwin M. Chaiken, and Francisco González-Scarano. Interaction with CD4 and Antibodies to CD4-Induced Epitopes of the Envelope gp120 from a Microglial Cell-Adapted Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 79(11):6703-6713, Jun 2005. PubMed ID: 15890908. Show all entries for this paper.

McCaffrey2004 Ruth A McCaffrey, Cheryl Saunders, Mike Hensel, and Leonidas Stamatatos. N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of gp120 Protects Human Immunodeficiency Virus Type 1 SF162 from Neutralization by Anti-gp120 and Anti-gp41 Antibodies. J. Virol., 78(7):3279-3295, Apr 2004. PubMed ID: 15016849. Show all entries for this paper.

McCann2005 C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016. Show all entries for this paper.

McGuire2014 Andrew T. McGuire, Jolene A. Glenn, Adriana Lippy, and Leonidas Stamatatos. Diverse Recombinant HIV-1 Envs Fail to Activate B Cells Expressing the Germline B Cell Receptors of the Broadly Neutralizing Anti-HIV-1 Antibodies PG9 and 447-52D. J. Virol., 88(5):2645-2657, Mar 2014. PubMed ID: 24352455. Show all entries for this paper.

McKnight2007 Aine McKnight and Marlen M. I. Aasa-Chapman. Clade Specific Neutralising Vaccines for HIV: An Appropriate Target? Curr. HIV Res., 5(6):554-560, Nov 2007. PubMed ID: 18045111. Show all entries for this paper.

Mester2009 Brenda Mester, Revital Manor, Amit Mor, Boris Arshava, Osnat Rosen, Fa-Xiang Ding, Fred Naider, and Jacob Anglister. HIV-1 Peptide Vaccine Candidates: Selecting Constrained V3 Peptides with Highest Affinity to Antibody 447-52D. Biochemistry, 48(33):7867-7877, 25 Aug 2009. PubMed ID: 19552398. Show all entries for this paper.

Mondor1998 I. Mondor, S. Ugolini, and Q. J. Sattentau. Human Immunodeficiency Virus Type 1 Attachment to HeLa CD4 Cells Is CD4 Independent and Gp120 Dependent and Requires Cell Surface Heparans. J. Virol., 72:3623-3634, 1998. PubMed ID: 9557643. Show all entries for this paper.

Moore1994d J. P. Moore, Y. Cao, D. D. Ho, and R. A. Koup. Development of the anti-gp120 antibody response during seroconversion to human immunodeficiency virus type 1. J. Virol., 68:5142-5155, 1994. Three seroconverting individuals were studied. The earliest detectable anti-gp120 antibodies were both conformational and anti-V3 loop, and could be detected only after the peak viremia has passed. No uniform pattern of autologous neutralizing anti-CD4BS or anti-V3 MAbs was observed. PubMed ID: 8035514. Show all entries for this paper.

Moore1995b J. P. Moore, Y. Cao, L. Qing, Q. J. Sattentau, J. Pyati, R. Koduri, J. Robinson, C. F. Barbas III, D. R. Burton, and D. D. Ho. Primary Isolates of Human Immunodeficiency Virus Type I Are Relatively Resistant to Neutralization by Monoclonal Antibodies to gp120, and Their Neutralization Is Not Predicted by Studies with Monomeric gp120. J. Virol., 69:101-109, 1995. A panel of anti-gp120 MAbs and sera from HIV-1 infected individuals was tested for its ability to neutralize primary isolates. Most MAbs bound with high affinity to gp120 monomers from the various isolates, but were not effective at neutralizing. The MAb IgG1b12, which binds to a discontinuous anti-CD4 binding site epitope, was able to neutralize most of the primary isolates. PubMed ID: 7527081. Show all entries for this paper.

Moore1995c J. P. Moore and D. D. Ho. HIV-1 Neutralization: The Consequences of Adaptation to Growth on Transformed T-Cells. AIDS, 9(suppl A):S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579. Show all entries for this paper.

Moore2006 Penny L. Moore, Emma T. Crooks, Lauren Porter, Ping Zhu, Charmagne S. Cayanan, Henry Grise, Paul Corcoran, Michael B. Zwick, Michael Franti, Lynn Morris, Kenneth H. Roux, Dennis R. Burton, and James M. Binley. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1. J. Virol., 80(5):2515-2528, Mar 2006. PubMed ID: 16474158. Show all entries for this paper.

Mor2009 Amit Mor, Eugenia Segal, Brenda Mester, Boris Arshava, Osnat Rosen, Fa-Xiang Ding, Joseph Russo, Amnon Dafni, Fabian Schvartzman, Tali Scherf, Fred Naider, and Jacob Anglister. Mimicking the Structure of the V3 Epitope Bound to HIV-1 Neutralizing Antibodies. Biochemistry, 48(15):3288-3303, 21 Apr 2009. PubMed ID: 19281264. Show all entries for this paper.

Musich2011 Thomas Musich, Paul J. Peters, Maria José Duenas-Decamp, Maria Paz Gonzalez-Perez, James Robinson, Susan Zolla-Pazner, Jonathan K. Ball, Katherine Luzuriaga, and Paul R. Clapham. A Conserved Determinant in the V1 Loop of HIV-1 Modulates the V3 Loop to Prime Low CD4 Use and Macrophage Infection. J. Virol., 85(5):2397-2405, Mar 2011. PubMed ID: 21159865. Show all entries for this paper.

Nelson2007 Josh D. Nelson, Florence M. Brunel, Richard Jensen, Emma T. Crooks, Rosa M. F. Cardoso, Meng Wang, Ann Hessell, Ian A. Wilson, James M. Binley, Philip E. Dawson, Dennis R. Burton, and Michael B. Zwick. An Affinity-Enhanced Neutralizing Antibody against the Membrane-Proximal External Region of Human Immunodeficiency Virus Type 1 gp41 Recognizes an Epitope between Those of 2F5 and 4E10. J. Virol., 81(8):4033-4043, Apr 2007. PubMed ID: 17287272. Show all entries for this paper.

Nishiyama2009 Yasuhiro Nishiyama, Stephanie Planque, Yukie Mitsuda, Giovanni Nitti, Hiroaki Taguchi, Lei Jin, Jindrich Symersky, Stephane Boivin, Marcin Sienczyk, Maria Salas, Carl V. Hanson, and Sudhir Paul. Toward Effective HIV Vaccination: Induction of Binary Epitope Reactive Antibodies with Broad HIV Neutralizing Activity. J. Biol. Chem., 284(44):30627-30642, 30 Oct 2009. PubMed ID: 19726674. Show all entries for this paper.

Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of Epitopes Exposed on Intact Human Immunodeficiency Virus Type 1 (HIV-1) Virions: A New Strategy for Studying the Immunologic Relatedness of HIV-1. J. Virol., 72:9384-9391, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.

Nyambi2000 P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650. Show all entries for this paper.

ORourke2010 Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Dora P. A. J. Fonseca, Karianne Terry, Terri Wrin, Faruk Sinangil, and Phillip W. Berman. Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus. J. Virol., 84(21):11200-11209, Nov 2010. PubMed ID: 20702624. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.

Pantophlet2006 Ralph Pantophlet and Dennis R. Burton. GP120: Target for Neutralizing HIV-1 Antibodies. Annu. Rev. Immunol., 24:739-769, 2006. PubMed ID: 16551265. Show all entries for this paper.

Pantophlet2007 Ralph Pantophlet, Rowena O. Aguilar-Sino, Terri Wrin, Lisa A. Cavacini, and Dennis R. Burton. Analysis of the Neutralization Breadth of the Anti-V3 Antibody F425-B4e8 and Re-assessment of its Epitope Fine Specificity by Scanning Mutagenesis. Virology, 364(2):441-453, 1 Aug 2007. PubMed ID: 17418361. Show all entries for this paper.

Pantophlet2008 Ralph Pantophlet, Terri Wrin, Lisa A. Cavacini, James E. Robinson, and Dennis R. Burton. Neutralizing Activity of Antibodies to the V3 Loop Region of HIV-1 gp120 Relative to Their Epitope Fine Specificity. Virology, 381(2):251-260, 25 Nov 2008. PubMed ID: 18822440. Show all entries for this paper.

Pantophlet2010 Ralph Pantophlet. Antibody Epitope Exposure and Neutralization of HIV-1. Curr. Pharm. Des., 16(33):3729-3743, 2010. PubMed ID: 21128886. Show all entries for this paper.

Park2000 E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031. Show all entries for this paper.

Parren1997 P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324. Show all entries for this paper.

Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.

Patel2008 Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735. Show all entries for this paper.

Peressin2011 M. Peressin, V. Holl, S. Schmidt, T. Decoville, D. Mirisky, A. Lederle, M. Delaporte, K. Xu, A. M. Aubertin, and C. Moog. HIV-1 Replication in Langerhans and Interstitial Dendritic Cells Is Inhibited by Neutralizing and Fc-Mediated Inhibitory Antibodies. J. Virol., 85(2):1077-1085, Jan 2011. PubMed ID: 21084491. Show all entries for this paper.

Phogat2007 S. Phogat, R. T. Wyatt, and G. B. Karlsson Hedestam. Inhibition of HIV-1 Entry by Antibodies: Potential Viral and Cellular Targets. J. Intern. Med., 262(1):26-43, Jul 2007. PubMed ID: 17598813. Show all entries for this paper.

Pinter2004 Abraham Pinter, William J. Honnen, Yuxian He, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection. J. Virol., 78(10):5205-5215, May 2004. PubMed ID: 15113902. Show all entries for this paper.

Pinter2005 Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930. Show all entries for this paper.

Poignard2003 Pascal Poignard, Maxime Moulard, Edwin Golez, Veronique Vivona, Michael Franti, Sara Venturini, Meng Wang, Paul W. H. I. Parren, and Dennis R. Burton. Heterogeneity of Envelope Molecules Expressed on Primary Human Immunodeficiency Virus Type 1 Particles as Probed by the Binding of Neutralizing and Nonneutralizing Antibodies. J. Virol., 77(1):353-365, Jan 2003. PubMed ID: 12477840. Show all entries for this paper.

Pugach2004 Pavel Pugach, Shawn E. Kuhmann, Joann Taylor, Andre J. Marozsan, Amy Snyder, Thomas Ketas, Steven M. Wolinsky, Bette T. Korber, and John P. Moore. The Prolonged Culture of Human Immunodeficiency Virus Type 1 in Primary Lymphocytes Increases its Sensitivity to Neutralization by Soluble CD4. Virology, 321(1):8-22, 30 Mar 2004. PubMed ID: 15033560. Show all entries for this paper.

Pugach2008 Pavel Pugach, Thomas J. Ketas, Elizabeth Michael, and John P. Moore. Neutralizing Antibody and Anti-Retroviral Drug Sensitivities of HIV-1 Isolates Resistant to Small Molecule CCR5 Inhibitors. Virology, 377(2):401-407, 1 Aug 2008. PubMed ID: 18519143. Show all entries for this paper.

Pugach2015 Pavel Pugach, Gabriel Ozorowski, Albert Cupo, Rajesh Ringe, Anila Yasmeen, Natalia de Val, Ronald Derking, Helen J. Kim, Jacob Korzun, Michael Golabek, Kevin de Los Reyes, Thomas J. Ketas, Jean-Philippe Julien, Dennis R. Burton, Ian A. Wilson, Rogier W. Sanders, P. J. Klasse, Andrew B. Ward, and John P. Moore. A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene. J. Virol., 89(6):3380-3395, Mar 2015. PubMed ID: 25589637. Show all entries for this paper.

Ringe2011 Rajesh Ringe, Deepak Sharma, Susan Zolla-Pazner, Sanjay Phogat, Arun Risbud, Madhuri Thakar, Ramesh Paranjape, and Jayanta Bhattacharya. A Single Amino Acid Substitution in the C4 Region in gp120 Confers Enhanced Neutralization of HIV-1 by Modulating CD4 Binding Sites and V3 Loop. Virology, 418(2):123-132, 30 Sep 2011. PubMed ID: 21851958. Show all entries for this paper.

Robinson2010 James E. Robinson, Kelly Franco, Debra Holton Elliott, Mary Jane Maher, Ashley Reyna, David C. Montefiori, Susan Zolla-Pazner, Miroslaw K. Gorny, Zane Kraft, and Leonidas Stamatatos. Quaternary Epitope Specificities of Anti-HIV-1 Neutralizing Antibodies Generated in Rhesus Macaques Infected by the Simian/Human Immunodeficiency Virus SHIVSF162P4. J. Virol., 84(7):3443-3453, Apr 2010. PubMed ID: 20106929. Show all entries for this paper.

Rosen2005 Osnat Rosen, Jordan Chill, Michal Sharon, Naama Kessler, Brenda Mester, Susan Zolla-Pazner, and Jacob Anglister. Induced Fit in HIV-Neutralizing Antibody Complexes: Evidence for Alternative Conformations of the gp120 V3 Loop and the Molecular Basis for Broad Neutralization. Biochemistry, 44(19):7250-7158, 17 May 2005. PubMed ID: 15882063. Show all entries for this paper.

Ruprecht2011 Claudia R. Ruprecht, Anders Krarup, Lucy Reynell, Axel M. Mann, Oliver F. Brandenberg, Livia Berlinger, Irene A. Abela, Roland R. Regoes, Huldrych F. Günthard, Peter Rusert, and Alexandra Trkola. MPER-Specific Antibodies Induce gp120 Shedding and Irreversibly Neutralize HIV-1. J. Exp. Med., 208(3):439-454, 14 Mar 2011. PubMed ID: 21357743. Show all entries for this paper.

Saarloos1995 M. N. Saarloos, T. F. Lint, and G. T. Spear. Efficacy of HIV-Specific and `Antibody-Independent' Mechanisms for Complement Activation by HIV-Infected Cells. Clin. Exp. Immunol., 99:189-195, 1995. PubMed ID: 7851010. Show all entries for this paper.

Sabin2010 Charles Sabin, Davide Corti, Victor Buzon, Mike S. Seaman, David Lutje Hulsik, Andreas Hinz, Fabrizia Vanzetta, Gloria Agatic, Chiara Silacci, Lara Mainetti, Gabriella Scarlatti, Federica Sallusto, Robin Weiss, Antonio Lanzavecchia, and Winfried Weissenhorn. Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41. PLoS Pathog., 6(11):e1001195, 2010. PubMed ID: 21124990. Show all entries for this paper.

Sanders2013 Rogier W. Sanders, Ronald Derking, Albert Cupo, Jean-Philippe Julien, Anila Yasmeen, Natalia de Val, Helen J. Kim, Claudia Blattner, Alba Torrents de la Peña, Jacob Korzun, Michael Golabek, Kevin de los Reyes, Thomas J. Ketas, Marit J. van Gils, C. Richter King, Ian A. Wilson, Andrew B. Ward, P. J. Klasse, and John P. Moore. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but not Non-Neutralizing Antibodies. PLoS Pathog., 9(9):e1003618, Sep 2013. PubMed ID: 24068931. Show all entries for this paper.

Sattentau1995 Q. J. Sattentau, S. Zolla-Pazner, and P. Poignard. Epitope Exposure on Functional, Oligomeric HIV-1 gp41 Molecules. Virology, 206:713-717, 1995. Most gp41 epitopes are masked when associated with gp120 on the cell surface. Weak binding of anti-gp41 MAbs can be enhanced by treatment with sCD4. MAb 2F5 binds to a membrane proximal epitope which binds in the presence of gp120 without sCD4. PubMed ID: 7530400. Show all entries for this paper.

Sattentau1995b Q. J. Sattentau. Conservation of HIV-1 gp120 Neutralizing Epitopes after Formalin Inactivation. AIDS, 9:1383-1385, 1995. PubMed ID: 8605064. Show all entries for this paper.

Sattentau1996 Q. J. Sattentau. Neutralization of HIV-1 by Antibody. Curr. Opin. Immunol., 8:540-545, 1996. Review. PubMed ID: 8794008. Show all entries for this paper.

Scheid2009 Johannes F. Scheid, Hugo Mouquet, Niklas Feldhahn, Michael S. Seaman, Klara Velinzon, John Pietzsch, Rene G. Ott, Robert M. Anthony, Henry Zebroski, Arlene Hurley, Adhuna Phogat, Bimal Chakrabarti, Yuxing Li, Mark Connors, Florencia Pereyra, Bruce D. Walker, Hedda Wardemann, David Ho, Richard T. Wyatt, John R. Mascola, Jeffrey V. Ravetch, and Michel C. Nussenzweig. Broad Diversity of Neutralizing Antibodies Isolated from Memory B Cells in HIV-Infected Individuals. Nature, 458(7238):636-640, 2 Apr 2009. PubMed ID: 19287373. Show all entries for this paper.

Seaman2010 Michael S. Seaman, Holly Janes, Natalie Hawkins, Lauren E. Grandpre, Colleen Devoy, Ayush Giri, Rory T. Coffey, Linda Harris, Blake Wood, Marcus G. Daniels, Tanmoy Bhattacharya, Alan Lapedes, Victoria R Polonis, Francine E. McCutchan, Peter B. Gilbert, Steve G. Self, Bette T. Korber, David C. Montefiori, and John R. Mascola. Tiered Categorization of a Diverse Panel of HIV-1 Env Pseudoviruses for Assessment of Neutralizing Antibodies. J Virol, 84(3):1439-1452, Feb 2010. PubMed ID: 19939925. Show all entries for this paper.

Selvarajah2005 Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142. Show all entries for this paper.

Sharon2002 Michal Sharon, Matthias Görlach, Rina Levy, Yehezkiel Hayek, and Jacob Anglister. Expression, Purification, and Isotope Labeling of a gp120 V3 Peptide and Production of a Fab from a HIV-1 Neutralizing Antibody for NMR Studies. Protein Expr. Purif., 24(3):374-383, Apr 2002. PubMed ID: 11922753. Show all entries for this paper.

Sharpe2004 Simon Sharpe, Naama Kessler, Jacob A. Anglister, Wai-Ming Yau, and Robert Tycko. Solid-State NMR Yields Structural Constraints on the V3 Loop from HIV-1 Gp120 Bound to the 447-52D Antibody Fv Fragment. J. Am. Chem. Soc., 126(15):4979-4990, 21 Apr 2004. PubMed ID: 15080704. Show all entries for this paper.

Shen2010 Xiaoying Shen, S. Moses Dennison, Pinghuang Liu, Feng Gao, Frederick Jaeger, David C. Montefiori, Laurent Verkoczy, Barton F. Haynes, S. Munir Alam, and Georgia D. Tomaras. Prolonged Exposure of the HIV-1 gp41 Membrane Proximal Region with L669S Substitution. Proc. Natl. Acad. Sci. U.S.A., 107(13):5972-5977, 30 Mar 2010. PubMed ID: 20231447. Show all entries for this paper.

Sheppard2007a Neil C. Sheppard, Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins. Clin. Vaccine Immunol., 14(2):157-167, Feb 2007. PubMed ID: 17167037. Show all entries for this paper.

Shibata2007 Junji Shibata, Kazuhisa Yoshimura, Akiko Honda, Atsushi Koito, Toshio Murakami, and Shuzo Matsushita. Impact of V2 Mutations on Escape from a Potent Neutralizing Anti-V3 Monoclonal Antibody during In Vitro Selection of a Primary Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 81(8):3757-3768, Apr 2007. PubMed ID: 17251298. Show all entries for this paper.

Shmelkov2011 Evgeny Shmelkov, Arthur Nadas, James Swetnam, Susan Zolla-Pazner, and Timothy Cardozo. Indirect Detection of an Epitope-Specific Response to HIV-1 gp120 Immunization in Human Subjects. PLoS One, 6(11):e27279, 2011. PubMed ID: 22076145. Show all entries for this paper.

Shmelkov2014 Evgeny Shmelkov, Chavdar Krachmarov, Arsen V. Grigoryan, Abraham Pinter, Alexander Statnikov, and Timothy Cardozo. Computational Prediction of Neutralization Epitopes Targeted by Human Anti-V3 HIV Monoclonal Antibodies. PLoS One, 9(2):e89987, 2014. PubMed ID: 24587168. Show all entries for this paper.

Sirois2007 Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757. Show all entries for this paper.

Smalls-Mantey2012 Adjoa Smalls-Mantey, Nicole Doria-Rose, Rachel Klein, Andy Patamawenu, Stephen A. Migueles, Sung-Youl Ko, Claire W. Hallahan, Hing Wong, Bai Liu, Lijing You, Johannes Scheid, John C. Kappes, Christina Ochsenbauer, Gary J. Nabel, John R. Mascola, and Mark Connors. Antibody-Dependent Cellular Cytotoxicity against Primary HIV-Infected CD4+ T Cells Is Directly Associated with the Magnitude of Surface IgG Binding. J. Virol., 86(16):8672-8680, Aug 2012. PubMed ID: 22674985. Show all entries for this paper.

Smith1998 A. D. Smith, S. C. Geisler, A. A. Chen, D. A. Resnick, B. M. Roy, P. J. Lewi, E. Arnold, and G. F. Arnold. Human Rhinovirus Type 14: Human Immunodeficiency Virus Type 1 (HIV-1) V3 Loop Chimeras from a Combinatorial Library Induce Potent Neutralizing Antibody Responses against HIV-1. J. Virol., 72:651-659, 1998. The tip of the MN V3 loop, IGPGRAFYTTKN, was inserted into cold-causing human rhinovirus 14 (HRV14) and chimeras were immunoselected using MAbs 447-52-D, 694/98-D, NM-01, and 59.1, for good presentation of the V3 antigenic region. The selected chimeric viruses were neutralized by anti-V3 loop MAbs. The chimeric viruses elicited potent NAbs against ALA-1 and MN in guinea pigs. PubMed ID: 9420270. Show all entries for this paper.

Spear1993 G. T. Spear, D. M. Takefman, B. L. Sullivan, A. L. Landay, and S. Zolla-Pazner. Complement activation by human monoclonal antibodies to human immunodeficiency virus. J. Virol., 67:53-59, 1993. This study looked at the ability of 16 human MAbs to activate complement. MAbs directed against the V3 region could induce C3 deposition on infected cells and virolysis of free virus, but antibodies to the CD4BS and C-terminal region and two regions in gp41 could induce no complement mediated effects. Pre-treatment with sCD4 could increase complement-mediated effects of anti-gp41 MAbs, but decreased the complement-mediated effects of V3 MAbs. Anti-gp41 MAbs were able to affect IIIB but not MN virolysis, suggesting spontaneous shedding of gp120 on IIIB virions exposes gp41 epitopes. IgG isotype did not appear to have an effect on virolysis or C3 deposition. PubMed ID: 7677959. Show all entries for this paper.

Sreepian2009 Apichai Sreepian, Jongruk Permmongkol, Wannee Kantakamalakul, Sontana Siritantikorn, Nattaya Tanlieng, and Ruengpung Sutthent. HIV-1 Neutralization by Monoclonal Antibody against Conserved Region 2 and Patterns of Epitope Exposure on the Surface of Native Viruses. J. Immune Based Ther. Vaccines, 7:5, 2009. PubMed ID: 19821992. Show all entries for this paper.

Srivastava2002 Indresh K. Srivastava, Leonidas Stamatatos, Harold Legg, Elaine Kan, Anne Fong, Stephen R. Coates, Louisa Leung, Mark Wininger, John J. Donnelly, Jeffrey B. Ulmer, and Susan W. Barnett. Purification and Characterization of Oligomeric Envelope Glycoprotein from a Primary R5 Subtype B Human Immunodeficiency Virus. J. Virol., 76(6):2835-2847, Mar 2002. URL: http://jvi.asm.org/cgi/content/full/76/6/2835. PubMed ID: 11861851. Show all entries for this paper.

Srivastava2005 Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830. Show all entries for this paper.

Srivastava2008 Indresh K. Srivastava, Elaine Kan, Yide Sun, Victoria A. Sharma, Jimna Cisto, Brian Burke, Ying Lian, Susan Hilt, Zohar Biron, Karin Hartog, Leonidas Stamatatos, Ruben Diaz-Avalos, R Holland Cheng, Jeffrey B. Ulmer, and Susan W. Barnett. Comparative Evaluation of Trimeric Envelope Glycoproteins Derived from Subtype C and B HIV-1 R5 Isolates. Virology, 372(2):273-290, 15 Mar 2008. PubMed ID: 18061231. Show all entries for this paper.

Stanfield2005 Robyn L. Stanfield and Ian A. Wilson. Structural Studies of Human HIV-1 V3 Antibodies. Hum Antibodies, 14(3-4):73-80, 2005. PubMed ID: 16720977. Show all entries for this paper.

Stanfield2006 Robyn L. Stanfield, Miroslaw K. Gorny, Susan Zolla-Pazner, and Ian A. Wilson. Crystal Structures of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralizing Antibody 2219 in Complex with Three Different V3 Peptides Reveal a New Binding Mode for HIV-1 Cross-Reactivity. J. Virol., 80(12):6093-6105, Jun 2006. PubMed ID: 16731948. Show all entries for this paper.

Swetnam2010 James Swetnam, Evgeny Shmelkov, Susan Zolla-Pazner, and Timothy Cardozo. Comparative Magnitude of Cross-Strain Conservation of HIV Variable Loop Neutralization Epitopes. PLoS One, 5(12):e15994, 2010. PubMed ID: 21209919. Show all entries for this paper.

Tasca2008 Silvana Tasca, Siu-Hong Ho, and Cecilia Cheng-Mayer. R5X4 Viruses Are Evolutionary, Functional, and Antigenic Intermediates in the Pathway of a Simian-Human Immunodeficiency Virus Coreceptor Switch. J. Virol., 82(14):7089-7099, Jul 2008. PubMed ID: 18480460. Show all entries for this paper.

Teeraputon2005 Sirilak Teeraputon, Suda Louisirirojchanakul, and Prasert Auewarakul. N-Linked Glycosylation in C2 Region of HIV-1 Envelope Reduces Sensitivity to Neutralizing Antibodies. Viral Immunol., 18(2):343-353, Summer 2005. PubMed ID: 16035946. Show all entries for this paper.

Tomaras2011 Georgia D. Tomaras, James M. Binley, Elin S. Gray, Emma T. Crooks, Keiko Osawa, Penny L. Moore, Nancy Tumba, Tommy Tong, Xiaoying Shen, Nicole L. Yates, Julie Decker, Constantinos Kurt Wibmer, Feng Gao, S. Munir Alam, Philippa Easterbrook, Salim Abdool Karim, Gift Kamanga, John A. Crump, Myron Cohen, George M. Shaw, John R. Mascola, Barton F. Haynes, David C. Montefiori, and Lynn Morris. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals. J. Virol., 85(21):11502-11519, Nov 2011. PubMed ID: 21849452. Show all entries for this paper.

Totrov2010 Maxim Totrov, Xunqing Jiang, Xiang-Peng Kong, Sandra Cohen, Chavdar Krachmarov, Aidy Salomon, Constance Williams, Michael S. Seaman, Ruben Abagyan, Timothy Cardozo, Miroslaw K. Gorny, Shixia Wang, Shan Lu, Abraham Pinter, and Susan Zolla-Pazner. Structure-Guided Design and Immunological Characterization of Immunogens Presenting the HIV-1 gp120 V3 Loop on a CTB Scaffold. Virology, 405(2):513-523, 30 Sep 2010. PubMed ID: 20663531. Show all entries for this paper.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Ugolini1997 S. Ugolini, I. Mondor, P. W. H. I Parren, D. R. Burton, S. A. Tilley, P. J. Klasse, and Q. J. Sattentau. Inhibition of Virus Attachment to CD4+ Target Cells Is a Major Mechanism of T Cell Line-Adapted HIV-1 Neutralization. J. Exp. Med., 186:1287-1298, 1997. PubMed ID: 9334368. Show all entries for this paper.

Upadhyay2014 Chitra Upadhyay, Luzia M. Mayr, Jing Zhang, Rajnish Kumar, Miroslaw K. Gorny, Arthur Nádas, Susan Zolla-Pazner, and Catarina E. Hioe. Distinct Mechanisms Regulate Exposure of Neutralizing Epitopes in the V2 and V3 Loops of HIV-1 Envelope. J. Virol., 88(21):12853-12865, Nov 2014. PubMed ID: 25165106. Show all entries for this paper.

Vaine2010 Michael Vaine, Shixia Wang, Qin Liu, James Arthos, David Montefiori, Paul Goepfert, M. Juliana McElrath, and Shan Lu. Profiles of Human Serum Antibody Responses Elicited by Three Leading HIV Vaccines Focusing on the Induction of Env-Specific Antibodies. PLoS One, 5(11):e13916, 2010. PubMed ID: 21085486. Show all entries for this paper.

VanCott1994 T. C. VanCott, F. R. Bethke, V. R. Polonis, M. K. Gorny, S. Zolla-Pazner, R. R. Redfield, and D. L. Birx. Dissociation Rate of Antibody-gp120 Binding Interactions Is Predictive of V3-Mediated Neutralization of HIV-1. J. Immunol., 153:449-459, 1994. Using surface plasmon resonance it was found that the rate of the dissociation of the MAb-gp120 complex, but not the association rate, correlated with MAbs ability to neutralize homologous virus (measured by 50\% inhibition of p24 production). Association constants were similar for all MAbs tested, varying less than 4-fold. Dissociation rate constants were quite variable, with 100-fold differences observed. PubMed ID: 7515931. Show all entries for this paper.

vanGils2011 Marit J. van Gils, Evelien M. Bunnik, Brigitte D. Boeser-Nunnink, Judith A. Burger, Marijke Terlouw-Klein, Naomi Verwer, and Hanneke Schuitemaker. Longer V1V2 Region with Increased Number of Potential N-Linked Glycosylation Sites in the HIV-1 Envelope Glycoprotein Protects against HIV-Specific Neutralizing Antibodies. J. Virol., 85(14):6986-6995, Jul 2011. PubMed ID: 21593147. Show all entries for this paper.

Varadarajan2005 Raghavan Varadarajan, Deepak Sharma, Kausik Chakraborty, Mayuri Patel, Michael Citron, Prem Sinha, Ramkishor Yadav, Umar Rashid, Sarah Kennedy, Debra Eckert, Romas Geleziunas, David Bramhill, William Schleif, Xiaoping Liang, and John Shiver. Characterization of gp120 and Its Single-Chain Derivatives, gp120-CD4D12 and gp120-M9: Implications for Targeting the CD4i Epitope in Human Immunodeficiency Virus Vaccine Design. J. Virol., 79(3):1713-1723, Feb 2005. PubMed ID: 15650196. Show all entries for this paper.

Vermeire2009 Kurt Vermeire, Kristel Van Laethem, Wouter Janssens, Thomas W. Bell, and Dominique Schols. Human Immunodeficiency Virus Type 1 Escape from Cyclotriazadisulfonamide-Induced CD4-Targeted Entry Inhibition Is Associated with Increased Neutralizing Antibody Susceptibility. J. Virol., 83(18):9577-9583, Sep 2009. PubMed ID: 19570853. Show all entries for this paper.

Verrier2001 F. Verrier, A. Nadas, M. K. Gorny, and S. Zolla-Pazner. Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. J. Virol., 75(19):9177--86, Oct 2001. URL: http://jvi.asm.org/cgi/content/full/75/19/9177. PubMed ID: 11533181. Show all entries for this paper.

Visciano2008 Maria Luisa Visciano, Michael Tuen, Miroslaw K. Gorny, and Catarina E. Hioe. In Vivo Alteration of Humoral Responses to HIV-1 Envelope Glycoprotein gp120 by Antibodies to the CD4-Binding Site of gp120. Virology, 372(2):409-420, 15 Mar 2008. PubMed ID: 18054978. Show all entries for this paper.

Wang2007a Bao-Zhong Wang, Weimin Liu, Sang-Moo Kang, Munir Alam, Chunzi Huang, Ling Ye, Yuliang Sun, Yingying Li, Denise L. Kothe, Peter Pushko, Terje Dokland, Barton F. Haynes, Gale Smith, Beatrice H. Hahn, and Richard W. Compans. Incorporation of High Levels of Chimeric Human Immunodeficiency Virus Envelope Glycoproteins into Virus-Like Particles. J. Virol., 81(20):10869-10878, Oct 2007. PubMed ID: 17670815. Show all entries for this paper.

Wu2008 Xueling Wu, Anna Sambor, Martha C. Nason, Zhi-Yong Yang, Lan Wu, Susan Zolla-Pazner, Gary J. Nabel, and John R. Mascola. Soluble CD4 Broadens Neutralization of V3-Directed Monoclonal Antibodies and Guinea Pig Vaccine Sera against HIV-1 Subtype B and C Reference Viruses. Virology, 380(2):285-295, 25 Oct 2008. PubMed ID: 18804254. Show all entries for this paper.

Wu2010 Xueling Wu, Zhi-Yong Yang, Yuxing Li, Carl-Magnus Hogerkorp, William R. Schief, Michael S. Seaman, Tongqing Zhou, Stephen D. Schmidt, Lan Wu, Ling Xu, Nancy S. Longo, Krisha McKee, Sijy O'Dell, Mark K. Louder, Diane L. Wycuff, Yu Feng, Martha Nason, Nicole Doria-Rose, Mark Connors, Peter D. Kwong, Mario Roederer, Richard T. Wyatt, Gary J. Nabel, and John R. Mascola. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1. Science, 329(5993):856-861, 13 Aug 2010. PubMed ID: 20616233. Show all entries for this paper.

Xu2010 Hengyu Xu, Likai Song, Mikyung Kim, Margaret A. Holmes, Zane Kraft, George Sellhorn, Ellis L. Reinherz, Leonidas Stamatatos, and Roland K. Strong. Interactions between Lipids and Human Anti-HIV Antibody 4E10 Can Be Reduced without Ablating Neutralizing Activity. J. Virol., 84(2):1076-1088, Jan 2010. PubMed ID: 19906921. Show all entries for this paper.

Yamamoto2008 Hiroyuki Yamamoto and Tetsuro Matano. Anti-HIV Adaptive Immunity: Determinants for Viral Persistence. Rev. Med. Virol., 18(5):293-303, Sep-Oct 2008. PubMed ID: 18416450. Show all entries for this paper.

Yang2010a Qiang Yang, Cishan Li, Yadong Wei, Wei Huang, and Lai-Xi Wang. Expression, Glycoform Characterization, and Antibody-Binding of HIV-1 V3 Glycopeptide Domain Fused with Human IgG1-Fc. Bioconjug. Chem., 21(5):875-883, 19 May 2010. PubMed ID: 20369886. Show all entries for this paper.

Yates2018 Nicole L. Yates, Allan C. deCamp, Bette T. Korber, Hua-Xin Liao, Carmela Irene, Abraham Pinter, James Peacock, Linda J. Harris, Sheetal Sawant, Peter Hraber, Xiaoying Shen, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayapan, Phillip W. Berman, Merlin L. Robb, Giuseppe Pantaleo, Susan Zolla-Pazner, Barton F. Haynes, S. Munir Alam, David C. Montefiori, and Georgia D. Tomaras. HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees. J. Virol., 92(8), 15 Apr 2018. PubMed ID: 29386288. Show all entries for this paper.

York2001 J. York, K. E. Follis, M. Trahey, P. N. Nyambi, S. Zolla-Pazner, and J. H. Nunberg. Antibody binding and neutralization of primary and T-cell line-adapted isolates of human immunodeficiency virus type 1. J. Virol., 75(6):2741--52, Mar 2001. URL: http://jvi.asm.org/cgi/content/full/75/6/2741. PubMed ID: 11222697. Show all entries for this paper.

Yoshimura2006 Kazuhisa Yoshimura, Junji Shibata, Tetsuya Kimura, Akiko Honda, Yosuke Maeda, Atsushi Koito, Toshio Murakami, Hiroaki Mitsuya, and Shuzo Matsushita. Resistance Profile of a Neutralizing Anti-HIV Monoclonal Antibody, KD-247, that Shows Favourable Synergism with Anti-CCR5 Inhibitors. AIDS, 20(16):2065-2073, 24 Oct 2006. PubMed ID: 17053352. Show all entries for this paper.

Yu2010 Bin Yu, Dora P. A. J. Fonseca, Sara M. O'Rourke, and Phillip W. Berman. Protease Cleavage Sites in HIV-1 gp120 Recognized by Antigen Processing Enzymes Are Conserved and Located at Receptor Binding Sites. J. Virol., 84(3):1513-1526, Feb 2010. PubMed ID: 19939935. Show all entries for this paper.

Yu2018 Wen-Han Yu, Peng Zhao, Monia Draghi, Claudia Arevalo, Christina B. Karsten, Todd J. Suscovich, Bronwyn Gunn, Hendrik Streeck, Abraham L. Brass, Michael Tiemeyer, Michael Seaman, John R. Mascola, Lance Wells, Douglas A. Lauffenburger, and Galit Alter. Exploiting Glycan Topography for Computational Design of Env Glycoprotein Antigenicity. PLoS Comput. Biol., 14(4):e1006093, Apr 2018. PubMed ID: 29677181. Show all entries for this paper.

Yuste2006 Eloisa Yuste, Hannah B. Sanford, Jill Carmody, Jacqueline Bixby, Susan Little, Michael B. Zwick, Tom Greenough, Dennis R. Burton, Douglas D. Richman, Ronald C. Desrosiers, and Welkin E. Johnson. Simian Immunodeficiency Virus Engrafted with Human Immunodeficiency Virus Type 1 (HIV-1)-Specific Epitopes: Replication, Neutralization, and Survey of HIV-1-Positive Plasma. J. Virol., 80(6):3030-3041, Mar 2006. PubMed ID: 16501112. Show all entries for this paper.

Zhou2010 Tongqing Zhou, Ivelin Georgiev, Xueling Wu, Zhi-Yong Yang, Kaifan Dai, Andrés Finzi, Young Do Kwon, Johannes F. Scheid, Wei Shi, Ling Xu, Yongping Yang, Jiang Zhu, Michel C. Nussenzweig, Joseph Sodroski, Lawrence Shapiro, Gary J. Nabel, John R. Mascola, and Peter D. Kwong. Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01. Science, 329(5993):811-817, 13 Aug 2010. PubMed ID: 20616231. Show all entries for this paper.

Zolla-Pazner1995 S. Zolla-Pazner, J. O'Leary, S. Burda, M. K. Gorny, M. Kim, J. Mascola, and F. McCutchan. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J. Virol., 69:3807-3815, 1995. A set of 13 human MAbs to a variety of epitopes were tested against a panel of primary isolates of HIV-1, representing different genetic clades. The V3 loop tended to be B clade restricted, and a single gp120 C-terminus binding antibody was clade specific. Two other gp120 C-terminus binding antibodies were group specific. PubMed ID: 7745728. Show all entries for this paper.

Zolla-Pazner1995a S. Zolla-Pazner and S. Sharpe. A Resting Cell Assay for Improved Detection of Antibody-Mediated Neutralization of HIV Type 1 Primary Isolates. AIDS Res. Hum. Retroviruses, 11:1449-1458, 1995. PubMed ID: 8679288. Show all entries for this paper.

Zolla-Pazner1999a S. Zolla-Pazner, M. K. Gorny, P. N. Nyambi, T. C. VanCott, and A. Nadas. Immunotyping of Human Immunodeficiency Virus Type 1 (HIV): An Approach to Immunologic Classification of HIV. J. Virol., 73:4042-4051, 1999. 21 human anti-V3 MAbs were studied with respect to cross-clade reactivity and immunological relationship to other human anti-V3 MAbs. Broad cross-reactivities were observed, and V3 peptides were grouped into immunotypes that contained peptides from several clades. PubMed ID: 10196300. Show all entries for this paper.

Zolla-Pazner1999b S. Zolla-Pazner, M. K. Gorny, and P. N. Nyambi. The implications of antigenic diversity for vaccine development. Immunol. Lett., 66:159-64, 1999. PubMed ID: 10203049. Show all entries for this paper.

Zwick2003a Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015. Show all entries for this paper.

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Displaying record number 1370

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MAb ID	2G12 (c2G12)
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Research Contact	Herman Katinger, Inst. Appl. Microbiol. or Polymun Scientific Inc., Vienna, Austria,
Epitope	(Discontinuous epitope)
Subtype	AD
Ab Type	gp120 carbohydrates at glycosylation residues in C2, C3, C4, and V4, gp120 V3 // V3 glycan (V3g)
Neutralizing	L P  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG1κ)
Patient
Immunogen	HIV-1 infection
Keywords	acute/early infection, ADCC, anti-idiotype, antibody binding site, antibody gene transfer, antibody generation, antibody interactions, antibody lineage, antibody polyreactivity, antibody sequence, assay or method development, autoantibody or autoimmunity, autologous responses, binding affinity, brain/CSF, broad neutralizer, cell-line isolated antibody, co-receptor, complement, computational epitope prediction, dendritic cells, drug resistance, dynamics, early treatment, elite controllers, enhancing activity, escape, genital and mucosal immunity, glycosylation, HAART, ART, immunoprophylaxis, immunotherapy, isotype switch, kinetics, memory cells, mimics, mimotopes, mother-to-infant transmission, neutralization, NK cells, polyclonal antibodies, rate of progression, responses in children, review, SIV, structure, subtype comparisons, supervised treatment interruptions (STI), therapeutic vaccine, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity, viral fitness and reversion

Notes

Showing 535 of 535 notes.

• 2G12: Analyses of all PDB HIV1-Env trimer (prefusion, closed) structures fulfilling certain parameters of resolution were performed to classify them on the basis of (a) antibody class which was informed by parental B cells as well as structural recognition, and (b) Env residues defining recognized HIV epitopes. Structural features of the 206 HIV epitope and bNAb paratopes were correlated with functional properties of the breadth and potency of neutralization against a 208-strain panel. bNAbs with >25% breadth of neutralization belonged to 20 classes of antibody with a large number of protruding loops and somatic hypermutation (SHM). HIV epitopes recognized placed the bNAbs into 6 categories (viz. V1V2, Glycan-V3, CD4-binding site, Silent face center, Fusion peptide and Subunit Interface). The epitopes contained high numbers of independent sequence segments and glycosylated surface area. 2G12-Env formed a distinct group within the Glycan-V3 category, Class 2G12 due to its unique V_H domain structure. Data for 2G12 complexed to BG505 DS-SOSIP trimer and VRC03 as a cryo-EM electron-density map was solved and deposited as EMD-8981. 2G12 epitope residues on Env were defined as residue 411 and glycans N295, N332, N339, and N392 from the cryo-EM reconstruction. Chuang2019 (antibody binding site, antibody interactions, neutralization, binding affinity, antibody sequence, structure, antibody lineage, broad neutralizer)
• 2G12: Rabbits were immunized with a DNA vaccine encoding JR-CSF gp120. Five sera with potent autologous neutralizing activity were selected and compared with a human neutralizing plasma (Z23) and monoclonal antibodies targeting various regions of gp120 (VRC01, b12, b6, F425, 2F5, 2G12, and X5). The rabbit sera contained different neutralizing activities dependent on C3 and V5, C3 and V4, or V4 regions of the glycan-rich outer domain of gp120. All sera showed enhanced neutralizing activity toward an Env variant that lacked a glycosylation site in V4. The JR-CSF gp120 epitopes recognized by the sera were distinct from those of the mAbs. The activity of one serum required specific glycans that are also important for 2G12 neutralization, and this serum blocked the binding of 2G12 to gp120. The findings show that different fine specificities can achieve potent neutralization of HIV-1, yet this strong activity does not result in improved breadth. Narayan2013 (neutralization, polyclonal antibodies)
• 2G12: The study compared well-characterized nAbs (2G12, b12, VRC01, 10E8, 17b) with 4 mAbs derived from a Japanese patient (4E9C, 49G2, 916B2, 917B11), in their neutralization and ADCC activity against viruses of subtypes B and CRF01. CRF01 viruses were less susceptible to neutralization by 2G12 and b12, while VRC01 was highly effective in neutralizing CRF01 viruses. 49G2 showed better neutralization breadth against CRF01 than against B viruses. CRF01_AE viruses from Japan also showed a slightly higher susceptibility to anti-CD4i Ab 4E9C than the subtype B viruses, and to CRF01_AE viruses from Vietnam. Neutralization breadth of other anti-CD4i Abs 17b, 916B2 and 917B11 was low against both subtype B and CRF01_AE viruses. Anti-CD4bs Ab 49G2, which neutralized only 22% of the viruses, showed the broadest coverage of Fc-mediated signaling activity against the same panel of Env clones among the Abs tested. The CRF01_AE viruses from Japan were more susceptible to 49G2-mediated neutralization than the CRF01_AE viruses from Vietnam, but Fc-mediated signaling activity of 49G2was broader and stronger in the CRF01_AE viruses from Vietnam than the CRF01_AE viruses from Japan. Thida2019 (ADCC, neutralization, subtype comparisons)
• 2G12: The Chinese HIV Reference Laboratory produced 124 pseudoviruses from patients with subype B, BC, and CRF01 infections. These viruses were assigned to tiers based on their neutralization by a panel of patient sera. Their neutralization sensitivities were also measured against a panel of well-characterized mAbs (2F5, b12, 2G12, 4E10, 10E8, VRC01, VRC-CH31, CH01, PG9, PG16, PGT121, PGT126). Nie2020 (assay or method development, neutralization)
• 2G12: Novel Env pseudoviruses were derived from 22 patients in China infected with subtype CRF01_AE viruses. Neutralization IC50 was determined for 11 bNAbs: VRC01, NIH45-46G54W, 3BNC117, PG9, PG16, 2G12, PGT121, 10-1074, 2F5, 4E10, and 10E8. The CRF01_AE pseudoviruses exhibited different susceptibility to these bNAbs. Overall, 4E10, 10E8, and 3BNC117 neutralized all 22 env-pseudotyped viruses, followed by NIH45-46G54W and VRC01, which neutralized more than 90% of the viruses. 2F5, PG9, and PG16 showed only moderate breadth, while the other three bNAbs neutralized none of these pseudoviruses. Specifically, 10E8, NIH45-46G54Wand 3BNC117 showed the highest efficiency, combining neutralization potency and breadth. Mutations at position 160, 169, 171 were associated with resistance to PG9 and PG16, while loss of a potential glycan at position 332 conferred insensitivity to V3-glycan-targeting bNAbs. These results may help in choosing bNAbs that can be used preferentially for prophylactic or therapeutic approaches in China. Wang2018a (assay or method development, neutralization, subtype comparisons)
• 2G12: Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized. Cross-linking/mass spectrometry to evaluate the conformations of functional membrane Env and sgp140 SOSIP.664 has been reported. Differences were detected in the gp120 trimer association domain and C terminus and in the gp41 HR1 region which can guide the improvement of Env glycoprotein preparations and potentially increasing their effectiveness as a vaccine. 2G12 broadly neutralized HIV-1AD8 full-length and cytoplasmic tail-deleted Envs. Castillo-Menendez2019 (vaccine antigen design, structure)
• 2G12: The authors mutated two conserved tyrosine (Y) residues within the V2 loop of gp120 Y177 and Y173, individually or in combination, by replacing them with either phenylalanine (F) or alanine (A) in a clade B, tier 1B HIV-1 Env protein (BaL), and in a number of tier 2 HIV-1 Envs from different clades, namely, BG505 (clade A), JR-FL and JR-CSF (clade B), and CM244 (clade E). A consistent hierarchy of neutralization sensitivity was seen among the mutants, with a greater impact of Y177 over Y173 single mutations, of double over single mutations, and of A over F substitutions. The double-alanine mutation in mutant HIV-1 BaL, Y173A Y177A, increased sensitivity to all the weakly neutralizing MAbs tested and even rendered the virus sensitive to non-neutralizing antibodies against the CD4 binding site, such as F105, 654-30D, and b13. When tested against bNAbs instead, there was a trend to decrease neutralization sensitivity compared to WT, with the exception of N6, PGT151, 10E8, and 2G12, for which there was no change, and of 2F5 and 4E10, which were more effective against the mutant compared to the WT. Guzzo2018 (antibody binding site, binding affinity)
• 2G12: Without SOSIP changes, cleaved Env trimers disintegrate into their gp120 and gp41-ectodomain (gp41_ECTO) components. This study demonstrates that the gp41_ECTO component is the primary source of this Env metastability and that replacing wild-type gp41_ECTO with BG505 gp41_ECTO of the uncleaved prefusion-optimized design is a general and effective strategy for trimer stabilization. A panel of 11 bNAbs, including the N332 supersite recognized by PGT121, PGT128, PGT135, and 2G12, was used to assess conserved neutralizing epitopes on the trimer surface, and the main result was that the substitution was found to significantly improve trimer binding to bNAbs VRC01, PGT151, and 35O22, with P values (paired t test) of 0.0229, 0.0269, and 0.0407, respectively. He2018 (antibody interactions, glycosylation, vaccine antigen design)
• 2G12: To reduce local V2 flexibility and improve the binding of V2-dependent bNAbs and germline precursor bNAbs, the authors designed BG505 SOSIP.664 trimer variants whose V1 and V2 domains were stabilized by introducing disulfide bonds either within the V2 loop or between the V1 and V2 loops. The resulting SOSIP trimer variants — E153C/K178C, E153C/K178C/G152E and I184C/E190C — have improved reactivity with V2 bNAbs and their inferred germline precursors and are more sensitive to neutralization by V2 bNAbs. Compared with BG505 SOSIP.664, the E153C/R178C V1-V2 disulfide mutant bound the VRC01, PGT151, and 2G12 slightly less well and the G152E compensatory mutation improved VRC01, PGT151, and 2G12 binding. However, sensitivity to antibodies 2G12 and PGT151 was not affected for either mutant virus E153C/K178C/G152E and I184C/E190C. deTaeye2019 (antibody interactions, variant cross-reactivity, binding affinity, structure, broad neutralizer)
• 2G12: This study looks at the role of somatic mutations within antibody variable and framework regions (FWR) in bNAbs and how these mutations alter thermostability and neutralization as the Ab lineage reaches maturation. The emergence and selection of different mutations in the complementarity-determining and framework regions are necessary to maintain a balance between antibody function and stability. The study shows that all major classes of bnAbs (DH2070, CH103, CH235 etc.) have lower thermostability than their corresponding inferred UCA antibodies. Henderson2019 (neutralization, antibody lineage, broad neutralizer)
• 2G12: Two HIV-1-infected individuals, VC10014 and VC20013, were monitored from early infection until well after they had developed broadly neutralizing activity. The bNAb activity developed about 1 year after infection and mapped to a single epitope in both subjects. Isolates from each subject, taken at five different time points, were tested against monoclonal bNAbs: VRC01, B12, 2G12, PG9, PG16, 4E10, and 2F5. In subject VC10014, the bNAb activity developed around 1 year postinfection and targeted an epitope that overlaps the CD4-BS and is similar to (but distinct from) bNAb HJ16. In the case of VC20013, the bNAb activity targeted a novel epitope in the MPER that is critically dependent on residue 677 (mutation K677N). Sather2014 (neutralization, broad neutralizer)
• 2G12: This study demonstrated that bNAb signatures can be utilized to engineer HIV-1 Env vaccine immunogens eliciting Ab responses with greater neutralization breadth. Data from four large virus panels were used to comprehensively map viral signatures associated with bNAb sensitivity, hypervariable region characteristics, and clade effects. The bNAb signatures defined for the V2 epitope region were then employed to inform immunogen design in a proof-of-concept exploration of signature-based epitope targeted (SET) vaccines. V2 bNAb signature-guided mutations were introduced into Env 459C to create a trivalent vaccine which resulted in increased breadth of NAb responses compared with Env 459C alone. Bricault2019 (antibody binding site, vaccine antigen design, computational epitope prediction, broad neutralizer)
• 2G12: The influence of a V2 State 2/3-stabilizing Env mutation, L193A, on ADCC responses mediated by sera from HIV-1-infected individuals was evaluated. Conformations spontaneously sampled by the Env trimer at the surface of infected cells had a significant impact on ADCC. 2G12 was used as a conformation-independent antibody. Prevost2018 (ADCC)
• 2G12: Polyreactive properties of natural and artificially engineered HIV-1 bNAbs were studied, with almost 60% of the tested HIV-1 bNAbs (including this one) exhibiting low to high polyreactivity in different immunoassays. A previously unappreciated polyreactive binding for PGT121, PGT128, NIH45-46W, m2, and m7 was reported. Binding affinity, thermodynamic, and molecular dynamics analyses revealed that the co-emergence of enhanced neutralizing capacities and polyreactivity was due to an intrinsic conformational flexibility of the antigen-binding sites of bNAbs, allowing a better accommodation of divergent HIV-1 Env variants. Prigent2018 (antibody polyreactivity)
• 2G12: A systems glycobiology approach was applied to reverse engineer the relationship between bNAb binding and glycan effects on Env proteins. Glycan occupancy was interrogated across every potential N-glycan site in 94 recombinant gp120 antigens. Using a Bayesian machine learning algorithm, bNAb-specific glycan footprints were identified and used to design antigens that selectively alter bNAb antigenicity. The novel synthesized antigens uccessfully bound to target bNAbs with enhanced and selective antigenicity. Yu2018 (glycosylation, vaccine antigen design)
• 2G12: A panel of bnAbs were studied to assess ongoing adaptation of the HIV-1 species to the humoral immunity of the human population. Resistance to neutralization is increasing over time, but concerns only the external glycoprotein gp120, not the MPER, suggesting a high selective pressure on gp120. Almost all the identified major neutralization epitopes of gp120 are affected by this antigenic drift, suggesting that gp120 as a whole has progressively evolved in less than 3 decades. Bouvin-Pley2014 (neutralization)
• 2G12: The first cryo-EM structure of a cross-linked vaccine antigen was solved. The 4.2 Å structure of HIV-1 BG505 SOSIP soluble recombinant Env in complex with a bNAb PGV04 Fab fragment revealed how cross-linking affects key properties of the trimer. SOSIP and GLA-SOSIP trimers were compared for antigenicity by ELISA, using a large panel of mAbs previously determined to react with BG505 Env. Non-NAbs globally lost reactivity (7-fold median loss of binding), likely because of covalent stabilization of the cross-linked ‘closed’ form of the GLA-SOSIP trimer that binds non-NAbs weakly or not at all. V3-specific non-NAbs showed 2.1–3.3-fold reduced binding. Three autologous rabbit monoclonal NAbs to the N241/N289 ‘glycan-hole’ surface, showed a median ˜1.5-fold reduction in binding. V3 non-NAb 4025 showed residual binding to the GLA-SOSIP trimer. By contrast, bNAbs like 2G12 broadly retained reactivity significantly better than non-NAbs, with exception of PGT145 (3.3-5.3 fold loss of binding in ELISA and SPR). Schiffner2018 (vaccine antigen design, binding affinity, structure)
• 2G12: This study describes the generation of CHO cell lines stably expressing the following vaccine Env Ags: CRF01_AE A244 Env gp120 protein (A244.AE) and 6240 Env gp120 protein (6240.B). The antigenic profiles of the molecules were assessed with a panel of well-characterized mAbs recognizing critical epitopes and glycosylation analysis confirming previously identified sites and revealing unknown sites at non-consensus motifs. A244.AE gp120 showed low level of binding to 2G12 in ELISA EC50 and Surface Plasmon Resonance (SPR) assays. 6240.B gp120 exhibited binding to 2G12. Wen2018 (glycosylation, vaccine antigen design)
• 2G12: Assays of poly- and autoreactivity demonstrated that broadly neutralizing NAbs are significantly more poly- and autoreactive than non-neutralizing NAbs. 2G12 is neither autoreactive nor polyreactive. Liu2015a (autoantibody or autoimmunity, antibody polyreactivity)
• 2G12: A panel of 14 pseudoviruses of subtype CRF01_AE was developed to assess the neutralization of several neutralizing antibodies (b12, PG9, PG16, 4E10, 10E8, 2F5, PGT121, PGT126, 2G12). Neutralization was assessed in both TZM-bl and A3R5 cell-based assays. Most viruses were more susceptible to mAb-neutralization in A3R5 than in the TZM-bl cell-based assay. The increased neutralization sensitivity observed in the A3R5 assay was not linked to the year of virus transmission or to the stages of infection, but chronic viruses from the years 1990-92 were more sensitive to neutralization than the more current viruses, in both assays. Chenine2018 (assay or method development, neutralization, subtype comparisons)
• 2G12: The immunologic effects of mutations in the Env cytoplasmic tail (CT) that included increased surface expression were explored using a vaccinia prime/protein boost protocol in mice. After vaccinia primes, CT- modified Envs induced up to 7-fold higher gp120-specific IgG, and after gp120 protein boosts, they elicited up to 16-fold greater Tier-1 HIV-1 neutralizing antibody titers. Hogan2018 (vaccine antigen design)
• 2G12: SOSIP.664 trimer was modified at V3 positions 306 and 308 by Leucine substitution to create hydrophobic interactions with the tryptophan residue at position 316 and the V1V2 domain. These modifications stabilized the resulting SOSIP.v5.2 S306L R308L trimers. In vivo, the induction of V3 non-NAbs was significantly reduced compared with the SOSIP.v5.2 trimers. S306L plus R308L paired substitutions had no effect on the trimer reactivity of 2G12. deTaeye2018 (broad neutralizer)
• 2G12: Repetitive immunization of macaques over 3 years with an Env expressing V3-high mannose glycan, CON-S gp140CFI, elicited plasma antibodies neturalizing HIV-1 expressing high mannose glycans only. NAb DH501 was isolated and found to possess a structure where 3 V_H chain CDRs formed a cavity into which the HIV-1 Env V3-glycan could insert. Rhesus DH501 possessed characteristics of V3-glycan bNAb precursors but its binding to M.CON-S gp140CFI was blocked 70% by 2G12. Saunders2017 (vaccine-induced immune responses, structure)
• 2G12: Nanodiscs (discoidal lipid bilayer particles of 10-17 nm surrounded by membrane scaffold protein) were used to incorporate Env complexes for the purpose of vaccine platform generation. The Env-NDs (Env-NDs) were characterized for antigenicity and stability by non-NAbs and NAbs. Most NAb epitopes in gp41 MPER and in the gp120:gp41 interface were well exposed while non-NAb cell surface epitopes were generally masked. Anti-gp120 glycan NAb 2G12, had a Kd of 10.16 nM and bound the Env-ND well. Witt2017 (vaccine antigen design, binding affinity)
• 2G12: The DS-SOSIP.4mut is a soluble, closed pre-fusion-state HIV-1 Env trimer that has improved stability and immunogenicity. It has 4 specific alterations at M154, M300, M302 and L320. 2G12 recognizes this trimer antigenically. Chuang2017 (antibody interactions)
• 2G12: Three strategies were applied to perturb the structure of Env in order to make the protein more susceptible to neutralization: exposure to cold, Env-activating ligands, and a chaotropic agent. A panel of mAbs (E51, 48d, 17b, 3BNC176, 19b, 447-52D, 39F, b12, b6, PG16, PGT145, PGT126, 35O22, F240, 10E8, 7b2, 2G12) was used to test the neutralization resistance of a panel of subtype B and C pseudoviruses with and without these agents. Both cold and CD4 mimicking agents (CD4Ms) increased the sensitivity of some viruses. The chaotropic agent urea had little effect by itself, but could enhance the effects of cold or CD4Ms. Thus Env destabilizing agents can make Env more susceptible to neutralization and may hold promise as priming vaccine antigens. Johnson2017 (vaccine antigen design)
• 2G12: Man₉-V3, a synthetic minimal immunogen designed to reflect the HIV-1 native Env V3-glycan bNAb epitope, binds memory B cells and V3-glycan bNAbs as well as germline bNAbs. Man₉-V3 was used to isolate a bNAb from an HIV-1+ subject and also induce V3-glycan-targeting antibodies in rhesus macaques. Using the crystal structure of PGT128-gp120 Env OD (outer domain), Man₉-V3 glycopeptide was synthesized based on Clade B JRFL with deletion of residues 305-320, retention of P321 and stabilization of disulfide bridge C296-C331. High mannose-glycans presented on Man₉-V3 were appropriately spaced for binding to 2G12. Alam2017 (antibody binding site)
• 2G12: Env from of a highly neutralization-resistant isolate, CH120.6, was shown to be very stable and conformationally-homogeneous. Its gp140 trimer retains many antigenic properties of the intact Env, while its monomeric gp120 exposes more epitopes. Thus trimer organization and stability are important determinants for occluding epitopes and conferring resistance to antibodies. Among a panel of 21 mAbs, CH120.6 was resistant to neutralization by all non-neutralizing and strain-specific mAbs, regardless of the location of their epitopes. It was weakly neutralized by several broadly-neutralizing mAbs (VRC01, NIH45-46, 12A12, PG9, PG16, PGT128, 4E10, and 10E8), and well neutralized by only 2 (PGT145 and 10-1074). Cai2017 (neutralization)
• 2G12: Mice twice-primed with DNA plasmids encoding HIV-1 gp120 and gag and given a double boost with HIV-1 virus-like particles (VLPs) i.e. DDVV immunization, elicited Env-specific antibody responses as well as Env- and Gag-specific CTL responses. In vivo electroporation (EP) was used to increase breadth and potency of response. Human anti-gp120 2G12 was used to prove that the VLP spike included the broad neutralization epitope recognized by it. Huang2017a (therapeutic vaccine, variant cross-reactivity)
• 2G12: A panel of mAbs (2G12, VRC01, HJ16, 2F5, 4E10, 35O22, PG9, PGT121, PGT126, 10-1074) was tested to compare their efficacy in cell-free versus cell-cell transmission. Almost all bNAbs (with the exception of anti-CD4 mAb Leu3a) blocked cell-free infection with greater potency than cell-cell infection, and showed greater potency in neutralization of cell-free viruses. The lower effectiveness on neutralization was particularly pronounced for transmitted/founder viruses, and less pronounced for chronic and lab-adapted viruses. The study highlights that the ability of an antibody to inhibit cell-cell transmission may be an important consideration in the development of Abs for prophylaxis. Li2017 (immunoprophylaxis, neutralization)
• 2G12: Compared to patient-derived mAbs, vaccine-elicited mAbs are often less able to neutralize the virus, due to a less-effective angle of approach to the Env spike. This study engineered an immunogen consisting of the gp120 core in complex with a CD4bs mAb, 17b. Rabbits immunized with this antigen displayed earlier affinity maturation and better virus neutralization compared to those immunized with the gp120 core alone. VRC01 and 2G12 bound to the the 17b-gp120 complex more avidly than to the gp120 core alone. Chen2016b (antibody binding site, vaccine antigen design, vaccine-induced immune responses, structure)
• 2G12: The amino acid at gp120 position 375 is embedded in the Phe43 cavity, which affects susceptibility to ADCC. Most M-group strains of HIV-1 have serine at position 375, but CRF01 typically has histidine, which is a bulky residue. MAbs 2G12 and 10E8 were not affected by changes in residue 375, while recognition by CD4i mAbs 17b and A32 was increased by mutations of residue 375 to histidine or tryptophan. Participants in the AIDSVAX vaccine trial were infected by CRF01, and a significant part of the efficacy of this vaccine rested on ADCC responses. The ADCC response of MAbs derived from AIDSVAX participants (CH29, CH38, CH40, CH51, CH52, CH54, CH77, CH80, CH81, CH89, CH91, CH94) was dependent on the presence of 375H and greatly decreased by the presence of 375S. Prevost2017 (ADCC, vaccine-induced immune responses)
• 2G12: This review focuses on the potential role of HIV-1-specific NAbs in preventing HIV-1 infection. Several NAbs have provided protection from infection in SHIV challenge studies in primates: b12, VRC01, VRC07-523LS, 3BNC117, PG9, PGT121, PGT126, 10-1074, 2G12, 4E10, 2F5, 10E8. Pegu2017 (immunoprophylaxis, review)
• 2G12: Prevalence, breadth, and potency of NAb responses in 98 CRF07_BC-infected individuals using a multi-subtype panel of 30 tier 2-3 Env-pseudotyped viruses were identified and the neutralization pattern of CRF07_BC-infected people was compared with that of subtype B'-infected individuals in China. 18% of 98 plasma samples neutralized >80% of viruses, and 53% neutralized >50%, suggesting the presence of broadly NAbs. CRF07_BC-infected individuals generated higher but less broad neutralization titers against intra-subtype viruses than subtype B'-infected individuals with longer infection length, indicating the transition from narrow autologous to broad heterologous neutralization over time. Neutralization activity of the top six plasmas from each cohort was attributable to the IgG fraction, and half of them developed CD4 binding site antibody reactivity. VRC01 and 2G12 were used as controls. Hu2017 (broad neutralizer)
• 2G12: This study investigated Ab binding abilities of saccharide ligands and the effects of the inner water molecules of ligand–Ab complexes. 2G12 complexes with saccharide ligands were studied by modeling to estimate how inner water molecules of the protein affect the dynamics of the complexes as well as the ligand–Ab interaction. This indicates that D -fructose’s strong affinity to the Ab was partly due to the good retentiveness of solvent water molecules of the ligand and its stability of the ligand’s conformation and relative position in the active site. Ueno-Noto2016 (antibody binding site, antibody interactions)
• 2G12: The results confirm that Nef and Vpu protect HIV-1-infected cells from ADCC, but also show that not all classes of antibody can mediate ADCC. Anti-cluster-A antibodies are able to mediate potent ADCC responses, whereas anti-coreceptor binding site antibodies are not. Position 69 in gp120 is important for antibody-mediated cellular toxicity by anti-cluster-A antibodies. The angle of approach of a given class of antibodies could impact its capacity to mediate ADCC. MAb 2G12 was used as a CD4-independent outer-domain-recognizing antibody to show that more Env is present on the cell surface in cells infected with Vpu-deleted HIV. Ding2015 (ADCC)
• 2G12: The ability of neutralizing and nonneutralizing mAbs to block infection in models of mucosal transmission was tested. Neutralization potency did not fully predict activity in mucosal tissue. CD4bs-specific bNAbs, in particular VRC01, blocked HIV-1 infection across all cellular and tissue models. MPER (2F5) and outer domain glycan (2G12) bNAbs were also efficient in preventing infection of mucosal tissues, while bNAbs targeting V1-V2 glycans (PG9 and PG16) were more variable. Non-nAbs alone and in combinations, were poorly protective against mucosal infection. The protection provided by specific bNAbs demonstrates their potential over that of nonneutralizing antibodies for preventing mucosal entry. 2G12 was selected to represent mAbs of the outer domain glycan class. Cheeseman2017 (genital and mucosal immunity, immunoprophylaxis)
• 2G12: This study investigated the ability of native, membrane-expressed JR-FL Env trimers to elicit NAbs. Rabbits were immunized with virus-like particles (VLPs) expressing trimers (trimer VLP sera) and DNA expressing native Env trimer, followed by a protein boost (DNA trimer sera). N197 glycan- and residue 230- removal conferred sensitivity to Trimer VLP sera and DNA trimer sera respectively, showing for the first time that strain-specific holes in the "glycan fence" can allow the development of tier 2 NAbs to native spikes. All 3 sera neutralized via quaternary epitopes and exploited natural gaps in the glycan defenses of the second conserved region of JR-FL gp120. Fig S7 showed that gp120 monomer and gp140F trimer both interfered with mAb 2G12 neutralization, but 2G12 was unable to inhibit CD4bs NAb binding. Crooks2015 (glycosylation, neutralization)
• 2G12: Nedd8 activation enzyme inhibitor, MLN4924, partially blocks Vpu activity through CD4 downregulation. Host antiviral factor BST2, however, is not inhibited and so reversal of Vpu activity is partial, exposing CD4-induced eptiopes that recruit ADCC-mediated host defense. Ab 2G12 which recognizes a CD4-independent epitope was used to show that even under best conditions, MLN4924 only minimally increases the binding of 2G12 to Env. Tokarev2015 (ADCC)
• 2G12: New antibodies were isolated from 3 patients: Donor 14 (PDGM11, PGDM12, PGDM13, PGDM14), Donor 82 (PGDM21), and Donor 26 (PGDM31). These bnAbs bound both the GDIR peptide (Env 324-327) and the high-mannose patch glycans, enabling broad reactivity. N332 glycan was absolutely required for neutralization, while N301 glycan modestly affected neutralization. Removing N156 and N301 glycans together while retaining N332 glycan abrogated neutralization for PGDM12 and PGDM21. Neutralization by PGDM11-14 bnAbs depended on R327A and H330A substitutions and neutralization by PGDM21 depended on D325A and H330A substitutions. G324A mutation resulted in slight loss of neutralization for both antibody families. In comparison, 2G12 and PGT135 did not show any dependence on residues in the 324GDIR327 region for neutralization activity, although PGT135 did show dependence on H330. Sok2016 (antibody binding site, glycosylation)
• 2G12: Env residue N197 on the BG505-SOSIP trimer was mutated to test the effect of its glycosylation on the binding kinetics of CD4BS and other mAbs. Removal of the glycan had little effect on the overall structure of the molecule. Its removal resulted in increased binding of CD4 and CD4BS antibodies (VRC01, VRC03, V3-3074), but little effect on bNAbs targeting other epitopes (PG9, PG16, PGT145, 17b, A32, 2G12, PGT121, PGT126). Two CD4BS-binding antibodies tested (b12, F105) had insufficient breadth to bind the BG505-SOSIP trimer. Removal of the N197 glycan may allow for the development of better SOSIP immunogens, particularly to elicit CD4BS-specific Abs. Liang2016 (glycosylation, vaccine antigen design)
• 2G12: This study produced Env SOSIP trimers for clades A (strain BG505), B (strain JR-FL), and G (strain X1193). Based on simulations, the MAb-trimer structures of all MAbs tested needed to accommodate at least one glycan, including both antibodies known to require specific glycans (PG9, PGT121, PGT135, 8ANC195, 35O22) and those that bind the CD4-binding site (b12, CH103, HJ16, VRC01, VRC13). A subset of monoclonal antibodies bound to glycan arrays assayed on glass slides (VRC26.09, PGT121, 2G12, PGT128, VRC13, PGT151, 35O22), while most of the antibodies did not have affinity for oligosaccharide in the context of a glycan array (PG9, PGT145, PGDM1400, PGT135, b12, CH103, HJ16, VRC16, VRC01, VRC-PG04, VRC-CH31, VRC-PG20, 3BNC60, 12A12, VRC18b, VRC23, VRC27, 1B2530, 8ANC131, 8ANC134, 8ANC195). Stewart-Jones2016 (antibody binding site, glycosylation, structure)
• 2G12: This study assessed the ADCC activity of antibodies of varied binding types, including CD4bs (b6, b12, VRC01, PGV04, 3BNC117), V2 (PG9, PG16), V3 (PGT126, PGT121, 10-1074), oligomannose (2G12), MPER (2F5, 4E10, 10E8), CD4i (17b, X5), C1/C5 (A32, C11), cluster I (240D, F240), and cluster II (98-6, 126-7). ADCC activity was correlated with binding to Env on the surfaces of virus-infected cells. ADCC was correlated with neutralization, but not always for lab-adapted viruses such as HIV-1 NLA-3. vonBredow2016 (ADCC)
• 2G12: This review summarizes representative anti-HIV MAbs of the first generation (2G12, b12, 2F5, 4E10) and second generation (PG9, PG16, PGT145, VRC26.09, PGDM1400, PGT121, PGT124, PGT128, PGT135, 10-1074, VRC01, 3BNC117, CH103, PGT151, 35O22, 8ANC195, 10E8). Structures, epitopes, VDJ usage, CDR usage, and degree of somatic hypermutation are compared among these antibodies. The use of SOSIP trimers as immunogens to elicit B-cell responses is discussed. Burton2016 (review, structure)
• 2G12: Two stable homogenous gp140 Env trimer spikes, Clade A 92UG037.8 Env and Clade C C97ZA012 Env, were identified. 293T cells stably transfected with either presented fully functional surface timers, 50% of which were uncleaved. A panel of neutralizing and non-neutralizing Abs were tested for binding to the trimers. Glycan Ab 2G12 bound cell surface gp160 weakly and strongly bound it without its C-terminal (gp160ΔCT), whether in the presence of sCD4 or not. It was unable to neutralize the 92UG037.8 HIV-1 isolate. Chen2015 (neutralization, binding affinity)
• 2G12: PGT145 was used to positively isolate a subtype B Env trimer immunogen, B41 SOSIP.664-D7324, that exists in two conformations, closed and partially open. bNAbs tested against the trimer were able to neutralize the B41 pseudovirus with a wide range of potencies. All tested non-NAbs did not neutralize B41 (IC₅₀ >50µg/ml). OD glycan bNAb, 2G12, neutralized and bound B41 pseudovirus and trimer. Pugach2015
• 2G12: A comprehensive antigenic map of the cleaved trimer BG505 SOSIP.664 was made by bNAb cross-competition. Epitope clusters at the CD4bs, quaternary V1/V2 glycan, N332-oligomannose patch and new gp120-gp41 interface and their interactions were delineated. Epitope overlap, proximal steric inhibition, allosteric inhibition or reorientation of glycans were seen in Ab cross-competition. Thus bNAb binding to trimers can affect surfaces beyond their epitopes. 2G12 non-reciprocally out-competed PGT135 and PGT136, all N332-outer domain (OD) glycan oligomannose patch bNAbs. Derking2015 (antibody interactions, neutralization, binding affinity, structure)
• 2G12: Two clade C recombinant Env glycoprotein trimers, DU422 and ZM197M, with native-like structural and antigenic properties involving epitopes for all known classes of bNAbs, were produced and characterized. These Clade C trimers (10-15% of which are in a partially open form) were more like B41 Clade B trimers which have 50-75% trimers in the partially open configuration than like B505 Clade B trimers, almost 100% in the closed, prefusion state. The Clade C trimers are reactive with bNAb 2G12, which was used to purify antigenically high quality, native-like trimers. OD-glycan binding 2G12 however, was not able to neutralize the equivalent pseudotyped viruses for either trimer. Julien2015 (assay or method development, structure)
• 2G12: Env trimer BG505 SOSIP.664 as well as the clade B trimer B41 SOSIP.664 were stabilized using a bifunctional aldehyde (glutaraldehye, GLA) or a heterobifunctional cross-linker, EDC/NHS with modest effects on antigenicity and barely any on biochemistry or structural morphology. ELISA, DSC and SPR were used to test recognition of the trimers by bNAbs, which was preserved and by weakly NAbs or non-NAbs, which was reduced. Cross-linking partially preserves quaternary morphology so that affinity chromatography by positive selection using quaternary epitope-specific bNAabs, and negative selection using non-NAbs, enriched antigenic characteristics of the trimers. Mannose patch-specific gp120-binding bNAb, 2G12, was conformationally insensitive to mild denaturation during ELISA and bound timers. Schiffner2016 (assay or method development, binding affinity, structure)
• 2G12: The native-like, engineered trimer BG505 SOSIP.664 induced potent NAbs against conformational epitopes of neutralization-resistant Tier-2 viruses in rabbits and macaques, but induced cross-reactive NAbs against linear V3 epitopes of neutralization-sensitive Tier-1 viruses. A different trimer, B41 SOSIP.664 also induced strong autologous Tier-2 NAb responses in rabbits. Sera from only 2/20 BG505 SOSIP.664-D7324 trimer-immunized rabbits were capable of inhibiting N332 glycan-dependent 2G12 binding to outer domain glycans. Sanders2015 (antibody generation, neutralization, binding affinity, polyclonal antibodies)
• 2G12: A new trimeric immunogen, BG505 SOSIP.664 gp140, was developed that bound and activated most known neutralizing antibodies but generally did not bind antibodies lacking neuralizing activity. This highly stable immunogen mimics the Env spike of subtype A transmitted/founder (T/F) HIV-1 strain, BG505. Anti-OD glycan bNAb 2G12 neutralized BG505.T332N, the pseudoviral equivalent of the immunogen BG505 SOSIP.664 gp140, and was shown to recognize and bind the immunogen too. Sanders2013 (assay or method development, neutralization, binding affinity)
• 2G12: This review discusses the application of bNAbs for HIV treatment and eradication, focusing on bnAbs that target key epitopes, specifically: 2G12, 2F5, 4E10, VRC01, 3BNC117, PGT121, VRC26.08, VRC26.09, PGDM1400, and 10-1074. Antibodies 2G12, 2F5, and 4E10 were among the first bnAbs available for clinical testing, and a cocktail of these 3 Abs was assessed in human trials. Stephenson2016 (immunotherapy, review)
• 2G12: This study described a natural interaction between Abs and mucin protein, especially, MUC16 that is enhanced in chronic HIV infection. Agalactosylated (G0) Abs demonstrated the highest binding to MUC16. Binding of Abs to epithelial cells was diminished following MUC16 knockdown, and the MUC16 N-linked glycans were critical for binding.These point to a novel opportunity to enrich Abs at mucosal sites by targeting Abs to MUC16 through changes in Fc glycosylation, potentially blocking viral movement. In 2G12 differential G0 content was linked to MUC16 binding supporting a role for G0 glycosylation in preferential MUC16 binding, independent of antigen specificity (Fig: S4). Gunn2016 (antibody interactions, glycosylation)
• 2G12: A mathematical model was developed to predict the Ab concentration at which antibody escape variants outcompete their ancestors, and this concentration was termed the mutant selection window (MSW). The MSW was determined experimentally for 12 pairings of diverse HIV strains against 7 bnAbs (b12, 2G12, PG9, PG16, PGT121, PGT128, 2F5). The neutralization of 2G12 was assayed against JRFL-N332S (resistant strain) and JRFL (sensitive strain). Magnus2016 (neutralization, escape)
• 2G12: The study detailed binding kinetics of the interaction between BG505 SOSIP.664 trimer or its variants (gp120 monomer; first study of disulfide-stabilized variant gp120-gp41_ECTO protomer) and several mAbs, both neutralizing (VRC01, PGV04, PG9, PG16, PGT121, PGT122, PGT123, PGT145, PGT151, 2G12) and non-neutralizing (b6, b12, 14e, 19b, F240). Glycan-binding 2G12 bound similarly to monomer and trimer and marginally better to protomer. Yasmeen2014 (antibody binding site, assay or method development)
• 2G12: 2G12 was expressed in transgenic rice endosperm to evaluate the potential of rice seeds as a vehicle for inexpensive microbicide production. Although the heavy chain was predominantly aglycosylated, the heavy and light chains assembled into functional antibodies with more potent HIV-neutralizing activity than other plant-derived forms of 2G12 bearing typical high-mannose or plant complex-type glycans. Assembled antibody accumulated predominantly in protein storage vacuoles but also induced the formation of novel, spherical storage compartments surrounded by ribosomes indicating that they originated from the endoplasmic reticulum. Vamvaka2016
• 2G12: Neutralization breadth in 157 antiretroviral-naive individuals infected for less than 1 year post-infection was studied and compared to a cohort of 170 untreated chronic patients. A range of neutralizing activities was observed with a panel of six recombinant viruses from five different subtypes. Some sera were broadly reactive, predominantly targeting envelope epitopes within the V2 glycan-dependent region. The Env neutralization breadth was positively associated with time post infection. 2G12 has been used as a control in detection of glycan-dependent HIV-1 neutralizing sera. Sanchez-Merino2016 (neutralization, acute/early infection)
• 2G12: Ten mAbs were isolated from a vertically-infected infant BF520 at 15 months of age. Ab BF520.1 neutralized pseudoviruses from clades A, B and C with a breadth of 58%, putting it in the same range as second-generation bNAbs derived from adults, but its potency was lower. BF520.1 was shown to target the base of the V3 loop at the N332 supersite. Outer domain glycan-binding, first generation mAb, 2G12 when compared had a geometric mean of IC₅₀=2.43 µg/ml for 2/12 viruses it neutralized at a potency of 17%. The infant-derived antibodies had a lower rate of somatic hypermutation (SHM) and no indels compared to adult-derived anti-V3 mAbs. This study shows that bnAbs can develop without SHM or prolonged affinity maturation. Simonich2016 (neutralization, structure)
• 2G12: The neutralization of 14 bnAbs was assayed against a global panel of 12 or 17 Env pseudoviruses. From IC₅₀, IC₈₀, IC₉₀, and IC₉₉ values, the slope of the dose-response curve was calculated. Each class of Ab had a fairly consistent slope. Neutralization breadth was strongly correlated with slope. An IIP (Instantaneous Inhibitory Potential) value was calculated, based on both the slope and IC50, and this value may be predictive of clinical efficacy. 2G12, a high mannose (HM) cluster bnAb belonged to a group with slopes ˜1. Webb2015 (neutralization)
• 2G12: The study's goal was to produce modified SOSIP trimers that would reduce the exposure - and, by inference, the immunogenicity - of non-NAb epitopes such as V3. The binding of several modified SOSIP trimers was compared among 12 neutralizing (PG9, PG16, PGT145, PGT121, PGT126, 2G12, PGT135, VRC01, CH103, CD4, IgG2, PGT151, 35O22) and 3 non-neutralizing antibodies (14e, 19b, b6). The V3 non-NAbs 447-52D, 39F, 14e, and 19b bound less well to all A316W variant trimers compared to wild-type trimers. Mice and rabbits immunized with modified, stabilized SOSIP trimers developed fewer V3 Ab responses than those immunized with native trimers. deTaeye2015 (antibody binding site)
• 2G12: HIV-1 strains were isolated from 60 patients infected with CRFs 01_AE, 07_BC, and 08_BC. Eight CRF01 strains that produced high-titer Env pseudoviruses were studied further. All were sensitive to neutralization by VRC01, PG9, PG16, and NIH45-46, but insensitive to 2G12. Of the 8 strains, 7 lacked glycans at Env 295 or 332, or both, suggesting that these glycosylation sites play a role in 2G12 binding and neutralization. Chen2016 (neutralization, subtype comparisons)
• 2G12: A large cross-sectional study of sera from 205 ART-naive patients infected with different HIV clades was tested against a panel of 219 cross-clade Env-pseudotyped viruses. Their neutralization was compared to the neutralization of 10 human bNAbs (10E8, 4E10, VRC01, PG9, PGT145, PGT128, 2F5, CH01, b12, 2G12) tested with a panel of 119 Env-pseudotyped viruses. Results from b12 and 2G12 suggested that these bnAbs may not be as broadly neutralizing as previously thought. 2G12 neutralized 20% of the 199 viruses tested, whereas a previous study had estimated this value at 41%. Hraber2014 (neutralization)
• 2G12: A flow-cytometry-based assay allowed non-radioactive measurement of ADCC-mediated elimination of HIV-1 gp120 envelope glycoprotein (Env)-coated target cells. This assay relies on staining target and effector cells with different dyes, which allows precise gating and permits the calculation of the number of surviving target cells by normalization to flow-cytometry particles. Richard2014 (ADCC, anti-idiotype, assay or method development)
• 2G12: This study describes a new level of complexity in antibody recognition of the mixed glycan-protein epitopes of the N332 region of HIV gp120. A combination of three antibody families that target the high-mannose patch can lead to 99% neutralization coverage of a large panel of viruses containing the N332/334 glycan site and up to 66% coverage for viruses that lack the N332/334 glycan site. PGT121, PGT128 and PGT135 families were studied. 2G12 was used as control since its binding is N332-dependent but it is less potent and broad in neutralization, recognizes glycans solely, and has a unique domain-exchanged structure. Sok2014a (antibody interactions, glycosylation)
• 2G12: Incomplete neutralization may decrease the ability of bnAbs to protect against HIV exposure. In order to determine the extent of non-sigmoidal slopes that plateau at <100% neutralization, a panel of 24 bnMAbs targeting different regions on Env was tested in a quantitative pseudovirus neutralization assay on a panel of 278 viral clones. All bNAbs had some viruses that they neutralized with a plateau <100%, but those targeting the V2 apex and MPER did so more often. All bnMAbs assayed had some viruses for which they had incomplete neutralization and non-sigmoidal neutralization curves. bNAbs were grouped into 3 groups based on their neutralization curves: group 1 antibodies neutralized more than 90% of susceptible viruses to >95% (PGT121-123, PGT125-128, PGT136, PGV04); group 2 was less effective, resulting in neutralization of 60-84% of susceptible viruses to >95% (b12, PGT130-131, PGT135, PGT137, PGT141-143, PGT145, 2G12, PG9); group 3 neutralized only 36-60% of susceptible viruses to >95% (PG16, PGT144, 2F5, 4E10). Among the panel tested, antibodies b12, 2G12, PGT136, and PGT137 had relatively few viruses neutralized with an IC50 <1 ug/ml. McCoy2015 (neutralization)
• 2G12: The neutralization abilities of Abs were enhanced by bioconjugation with aplaviroc, a small-molecule inhibitor of virus entry into host cells. Diazonium hexafluorophosphate was used. The conjugated Abs blocked HIV-1 entry through two mechanisms: by binding to the virus itself and by blocking the CCR5 receptor on host cells. Chemical modification did not significantly alter the potency and the pharmacokinetics. Improvements in potency over the parent Ab was ∼3-fold for 2G12-aplaviroc against the JR-FL isolate. Gavrilyuk2013 (neutralization)
• 2G12: Galactosyl ceramide (Galcer), a glycosphingolipid, is a receptor for the HIV-1 Env glycoprotein. This study has mimicked this interaction by using an artificial membrane containing synthetic Galcer and recombinant HIV-1 Env proteins to identify antibodies that would block the HIV-1 Env-Galcer interaction. HIV-1 ALVAC/AIDSVAX vaccinee-derived MAbs specific for the gp120 C1 region blocked Galcer binding of a transmitted/founder HIV-1 Env gp140. The antibody-dependent cellular cytotoxicity-mediating CH38 IgG and its natural IgA isotype were the most potent blocking antibodies.2G12 did not block Env-Galcer binding. Dennison2014 (ADCC, antibody binding site, antibody interactions, glycosylation)
• 2G12: This review surveyed the Vectored Immuno Prophylaxis (VIP) strategy, which involves passive immunization by viral vector-mediated delivery of genes encoding bnAbs for in vivo expression. Recently published studies in humanized mice and macaques were discussed as well as the pros and cons of VIP towards clinical applications to control HIV endemics. A single injection of AAV8 vector achieved peak Ab production in serum at week 6 and offered moderate protection. 2G12 (˜250 μg/mL) yielded partial protection. Yang2014 (immunoprophylaxis, review, antibody gene transfer)
• 2G12: The ability of bNAbs to inhibit the HIV cell entry was tested for b12, VRC01,VRC03, PG9, PG16, PGT121, 2F5, 10E8, 2G12. Among them, PGT121, VRC01, and VRC03 potently inhibited HIV entry into CD4+ T cells of infected individuals whose viremia was suppressed by ART. Chun2014 (immunotherapy)
• 2G12: Pairwise combinations of 6 NAbs (4E10, 2F5, 2G12, b12, PG9, PG16) were tested for neutralization of pseudoviruses and transmitted/founder viruses. Each of the NAbs tested targets a different region of gp120 or gp41. Some pairwise combinations enhanced neutralization synergistically, suggesting that combinations of NAbs may enhance clinical effectiveness. Miglietta2014 (neutralization)
• 2G12: The study compared various factors affecting the accessibility of epitopes for antibodies targeting the V2 integrin (V2i) region, versus the V3 region. CD4 treament of BaL and JRFL pseudoviruses increased their neutralization sensitivity to V3 MAbs, but not to V2i MAbs. Viruses grown in a glycosidase inhibitor were more sensitive to neutralization by V3, but not V2i, MAbs. Increasing the time of virus-MAb interaction increased virus neutralization by some V2i MAbs and all V3 MAbs. The structural dynamics of V2i and V3 epitopes has important effects in neutralization. Some experiments also included CD4BS antibodies b12, 2G12 and NIH45-46. Upadhyay2014
• 2G12: Dimeric 2G12 is much more potent than the monomeric form. This study compared monomeric and dimeric 2G12 by examination of crystal structures and electron microscopy. The greater potency and breadth of the dimeric form were attributed to intermolecular domain exchange, flexibility, and the avidity effects of bivalent binding. Wu2013 (structure)
• 2G12: Cross-group neutralization of HIV-1 isolates from groups M, N, O, and P was tested with diverse patient sera and bNAbs PG9, PG16, 4E10, b12, 2F5, 2G12, VRC01, VRC03, and HJ16. The primary isolates displayed a wide spectrum of sensitivity to neutralization by the human sera, with some cross-group neutralization clearly observed. Among the bNAbs, only PG9 and PG16 showed any cross-group neutralization. The group N prototype strain YBF30 was highly sensitive to neutralization by PG9, and the interaction between their key residues was confirmed by molecular modeling. The conservation of the PG9/PG16 epitope within groups M and N suggests its relevance as a vaccine immunogen. Braibant2013 (neutralization, variant cross-reactivity)
• 2G12: The binding affinity of 2G12 for sugar molecules associated with glycans was tested through computer modeling. Affinity for D-fructose was greater than for D-mannose. Koyama2014 (binding affinity)
• 2G12: The structure of 2G12 in association with Env trimer from HIV strain BG505-SOSIP was characterized. The 2G12 epitope overlaps with several other bNAbs that target the N332 supersite of vulnerability. Glycans N295, N392, and N339 are centrally located within the footprint of the antibody, while N448 and N386 are on the periphery. 2G12 may block membrane fusion by inducing steric hindrance upon primary receptor binding, thus abrogating Env's interaction with coreceptors. Murin2014 (structure)
• 2G12: 2G12 was one of 10 MAbs used to study chronic vs. consensus vs. transmitted/founder (T/F) gp41 Envs for immunogenicity. Consensus Envs were the most potent eliciters of response but could only neutralize tier 1 and some tier 2 viruses. T/F Envs elicited the greatest breadth of NAb response; and chronic Envs elicited the lowest level and narrowest response. This Glycan binding Nab bound well at <10 nM to 3/5 chronic Envs, 4/6 Consensus Envs and 4/7 T/F Envs. Liao2013c (antibody interactions, binding affinity)
• 2G12: The infectious virion (iVirions) capture index (IVCI) of different Abs have been determined. bnAbs captured higher proportions of iVirions compared to total virus particles (rVirions) indicating the capacity, breadth and selectively of bnAbs to capture iVirions. IVCI was additive with a mixture of Abs, providing proof of concept for vaccine-induced effect of improved capacity. bnAb 2G12 showed significantly high IVCI >1.0, but did not capture HIV subtype B T/F CH040, subtype C CH185.C, or subtype A/E AE.92TH023. Liu2014 (binding affinity)
• 2G12: Study evaluated 4 gp140 Env protein vaccine immunogens derived from an elite neutralizer donor VC10042, an HIV+ African American male from Vanderbilt cohort. Env immunogens, VC10042.05, VC10042.05RM, VC10042.08 and VC10042.ela, elicited high titers of cross-reactive Abs recognizing V1/V2 regions. All the Env protein except VC10042.ela bound to 2G12, but none of the parental Env were neutralized by 2G12. Carbonetti2014 (elite controllers, vaccine-induced immune responses)
• 2G12: The effect of low pH and HIV-1 Abs which increased the transcytosis of the virus by 20 fold, has been reported. This enhanced transcytosis was due to the Fc neonatal receptor (FcRn), which facilitates HIV-1's own transmission by usurping Ab responses directed against itself. Both infectious and noninfectious viruses were transcytosed by 2G12. Gupta2013
• 2G12: This study examined how the conserved gp120-gp41 association site adapts to glycan changes that are linked to neutralization sensitivity, using a DSR mutant virus, K601D. K601D has a defective gp120-association, and was sequentially passaged in peripheral blood mononuclear cells to select for suppressor mutations. Mutations 136 and/or glycan 142 increased the sensitivity of T138N and ΔN. Drummer2013 (antibody interactions, glycosylation)
• 2G12: Clade A Env sequence, BG505, was identified to bind to bNAbs representative of most of the known NAb classes. This sequence is the best natural sequence match (73%) to the MRCA sequence from 19 Env sequences derived from PG9 and PG16 MAbs' donor. A point mutation at position L111A of BG505 enabled more efficient production of a stable gp120 monomer, preserving the major neutralization epitopes. The antisera produced by this adjuvanted formulation of gp120 competed with bnAbs from 3 classes of non-overlapping epitopes. 2G12 bound to BG505L111A monomer, but failed to neutralize BG505 pseudovirus. Hoffenberg2013 (antibody interactions)
• 2G12: The neutralization profile of 1F7, a human CD4bs mAb, is reported and compared to other bnNAbs. 1F7 exhibited extreme potency against primary HIV-1, but limited breadth across clades. 2G12 neutralized 33% of a cross-clade panel of 157 HIV-1 isolates (Fig. S1) while 1F7 neutralized only 20% of the isolates. Gach2013 (neutralization)
• 2G12: This study reported the Ab binding titers and neutralization of 51 patients with chronic HIV-1 infection on supressive ART for 3 yrs. A high titer of Ab against gp120, gp41, and MPER was found. Patient sera were evaluated for binding against recombinant gp120_JR-FL mutants lacking either the V1/V2 loop or the V3 loop. Significantly higher end point binding titers and HIV1_JR-FL neutralization were noticed in patients with >10 compared to <10 yrs of detectable HIV RNA. 2G12 was used as a CD4b Ab control. Gach2014 (neutralization, HAART, ART)
• 2G12: This study reports the development of a new cell-line (A3R5)-based highly sensitive Ab detection assay. This T-lymphoblastoid cell-line stably expreses CCR5 and recognizes CCR5-tropic circulating strains of HIV-1. A3R5 cells showed greater neutralization potency compared to the current cell-line of choice TZM-bl. 2G12 was used as a reference Ab in neutralization assay comparing A3R5 and TZM-bl. McLinden2013 (assay or method development)
• 2G12: The crystal structure of PGT135 with gp120, CD4 and Fab 17b was analyzed to study how PGT135 recognizes its Asn332 glycan-dependent epitope. The combined structural studies of PGT 135, PGT 128 and 2G12 show this Asn332-dependent epitope is highly accessible and much more extensive than initially appreciated, allowing for multiple binding modes and varied angles of approach, thus representing a supersite of vulnerability for antibody neutralization. Kong2013 (structure)
• 2G12: This is a review of identified bNAbs, including the ontogeny of B cells that give rise to these antibodies. Breadth and magnitude of neutralization, unique features and similar bNAbs are listed. 2G12 is a V3-glycan Ab, with breadth 18%, IC₅₀ 4.85 μg per ml, and its unique feature is glycan-only recognition. Kwong2013 (review)
• 2G12: A32 and 2G12 MAbs were used to trigger ADCC activity and to show that HIV Nef and Vpu protect HIV-infected CD4+ T cells from ADCC through down-modulation of CD4 and BST2. Pham2014 (ADCC)
• 2G12: A highly conserved mechanism of exposure of ADCC epitopes on Env is reported, showing that binding of Env and CD4 within the same HIV-1 infected cell effectively exposes these epitopes. The mechanism might explain the evolutionary advantage of downregulation of cell surface CD4v by the Vpu and Nef proteins. 2G12 was used in CD4 coexpression and competitive binding assay. Results showed a strong correlation of deletion of vpu gene and 2G12 binding. Veillette2014 (ADCC)
• 2G12: The ability of MAb A32 to recognize HIV-1 Env expressed on the surface of infected CD4(+) T cells as well as its ability to mediate antibody-dependent cellular cytotoxicity (ADCC) activity was investigated. This study demonstrates that the epitope defined by MAb A32 is a major target on gp120 for plasma ADCC activity. 2G12 was used as a control and A32 showed >3 fold higher ADCC activity than 2G12. Ferrari2011a (ADCC)
• 2G12: Env pseudo-typed viruses generated from 7 transmitting and 4 non-transmitting mothers and their children were studied to identify phenotypes that associate with the risk of mother to child transmission. There were no differences in neutralization with 2F5, 2G12, 4E10 and b12, but transmitting mothers had higher autologous NAb responses against gp120/gp41, suggesting that strong autologous neutralization activity can associate with risk of transmission and be in fact detrimental. Baan2013 (neutralization, mother-to-infant transmission)
• 2G12: A statistical model selection method was used to identify a global panel of 12 reference Env clones among 219 Env-pseudotyped viruses that represent the spectrum of neutralizing activity seen with sera from 205 chronically HIV-1-infected individuals. This small final panel was also highly sensitive for detection of many of the known bNAbs, including this one. The small panel of 12 Env clones should facilitate assessments of vacine-elicited NAbs. Decamp2014 (assay or method development)
• 2G12: A panel of NAbs and non-neutralizing Abs (NoNAbs) displaying the highest Fc γR-mediated inhibitory activity and significant ADCC were selected and formulated in a microbicidal gel and tested for their antiviral activity against SHIVSF162P3 vaginal challenge in non-human primates. Combination of 2G12, 2F5 and 4E10 fully prevented vaginal transmission. Two NoNAbs 246-D and 4B3 had no impact on viral acquisition, but reduced plasma viral load. Moog2014 (ADCC, SIV)
• 2G12: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 2G12 is discussed as the C2, C3, C4 and V4 glycation sites-targeting neutralizing anti-gp120 mAb exhibiting ADCC activity and having a discontinuous epitope. Pollara2013 (ADCC, review)
• 2G12: "Neutralization fingerprints" for 30 neutralizing antibodies were determined using a panel of 34 diverse HIV-1 strains. 10 antibody clusters were defined: VRC01-like, PG9-like, PGT128-like, 2F5-like, 10E8-like and separate clusters for b12, CD4, 2G12, HJ16, 8ANC195. This mAb belongs to 10E8-like cluster. Georgiev2013 (neutralization)
• 2G12: This paper reported the nature of junk Env glycan that undermine the development of Ab responses against gp120/gp41 trimers and evaluated enzyme digestion as a way to remove aberrant Env to produce "trimer VLPs". 2G12 with its high-mannose glycan profile showed binding to gp160ER, considered as VLP-contaminant. Crooks2011 (glycosylation)
• 2G12: This study described a potential novel conformational epitope that is present in a subtype C infected subject during early infection. This epitope was recognized by three different B cell receptors and elicited both glycan dependent and independent MAbs. This also showed the power of a single strategically placed amino acid change in viral escape. 2G12 was discussed as a BnAb directed against glycan in describing the role of "glycan shield" in viral escape. Lynch2011a (glycosylation, escape, cell-line isolated antibody)
• 2G12: The role of NK cells and NK cell receptor polymorphisms in the assessment of HIV-1 neutralization is reported. 2G12 was used in viral inhibition assay as a control to compare NK cells participation and activity. Brown2012 (neutralization, NK cells)
• 2G12: This study describes an ˜11 Angstrom cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and gp41 subunits form a cage like structure with an interior void surrounding the trimer axis which restricts Ab access. 2G12 was used in ELISA to asses the recognition of the purified Env glycoproteins and recognized a high-mannose glycan array on the gp120 outer domain. Mao2012 (structure)
• 2G12: The sera of 20 HIV-1 patients were screened for ADCC in a novel assay measuring granzyme B (GrB) and T cell elimination and reported that complex sera mediated greater levels of ADCC than anti-HIV mAbs. The data suggested that total amount of IgG bound is an important determinant of robust ADCC which improves the vaccine potency. 2G12 was used as an anti-gp120 to study effects of Ab specificity and affinity on ADCC against HIV-1 infected targets. Smalls-Mantey2012 (ADCC, assay or method development)
• 2G12: Isolation of VRC06 and VRC06b MAbs from a slow progressor donor 45 is reported. This is the same donor from whom bnMAbs VRC01, VRC03 and NIH 45-46 were isolated and the new MAbs are clonal variants of VRC03. 2G12 was used as a glycan specific Ab and as a negative control to compare binding specificity of VRC06. Li2012
• 2G12: Immunogenicity of gp120 immunogens from two pairs of clade B and two pairs of clade C mother-to-child transmitted HIV-1 variants was studied in rabbits. While high level Env-specific antibody responses were elicited by all immunogens, their abilities to NAb responses differed and neutralization-resistant variants elicited broader NAb. Each of the six Env antigens resistant to 2G12 lacked at least one of the four Potential N-Linked Glycosylation sites (PNGS) important for 2G12 binding. Wang2012 (mother-to-infant transmission)
• 2G12: Protective potency of PGT121 was evaluated in vivo in rhesus macaques. PGT121 efficiently protected against high-dose challenge of SHIV SF162P3 in macaques. Sterilizing immunity was observed in 5/5 animals administered 5 mg/kg antibody dose and in 3/5 animals administered 0.2 mg/kg, suggesting that a protective serum concentration for PG121 is in the single-digit mg/mL. PGT121was effective at serum concentration 600-fold lower than for 2G12 and 100-fold lower than for b12. Moldt2012a (immunoprophylaxis)
• 2G12: The unbinding kinetics of the gp120-2G12, Man(4)-2G12, and Man(5)-2G12 interactions were measured by single-molecule force spectroscopy. This is the first single-molecule study aimed at dissecting the carbohydrate-antibody recognition of the gp120-2G12 interaction. The study confirmed crystallographic models that show both the binding of the linear Man(4) arm to 2G12 and also the multivalent gp120 glycan binding to 2G12. Martines2012 (binding affinity)
• 2G12: Three mouse B cell lines expressing domain-exchanged 2G12 WT, the non-domain-exchanged 2G12 I19R variant, and 2G12 gl as IgM B cell receptors (BCRs) were used to determine the potential of carbohydrate immunogens to elicit Y-shaped or domain-exchanged antibodies in vivo. HIV envelope glycoproteins and candidate glycoconjugate vaccines were compared for their ability to activate these B cell lines. Several of these immunogens were able to activate both 2G12 WT and 2G12 I19R B cell lines, and the discrete cluster of oligomannose glycans could selectively activate the domain-exchanged 2G12 WT cells. None of the immunogens tested were able to activate the germ line 2G12 B cells. The engineered B cell lines were more sensitive than standard ELISA binding assays and may help in the design of immunogens that elicit 2G12-like domain-exchanged antibodies in vivo. Doores2013 (assay or method development, glycosylation)
• 2G12: A computational tool (Antibody Database) identifying Env residues affecting antibody activity was developed. As input, the tool incorporates antibody neutralization data from large published pseudovirus panels, corresponding viral sequence data and available structural information. The model consists of a set of rules that provide an estimated IC₅₀ based on Env sequence data, and important residues are found by minimizing the difference between logarithms of actual and estimated IC₅₀. The program was validated by analysis of MAb 8ANC195, which had unknown specificity. Predicted critical N-glycosylation for 8ANC195 were confirmed in vitro and in humanized mice. The key associated residues for each MAb are summarized in the Table 1 of the paper and also in the Neutralizing Antibody Contexts & Features tool at Los Alamos Immunology Database. West2013 (glycosylation, computational epitope prediction)
• 2G12: Identification of broadly neutralizing antibodies, their epitopes on the HIV-1 spike, the molecular basis for their remarkable breadth, and the B cell ontogenies of their generation and maturation are reviewed. Ontogeny and structure-based classification is presented, based on MAb binding site, type (structural mode of recognition), class (related ontogenies in separate donors) and family (clonal lineage). This MAb's classification: gp120 glycan-V3 site, type glycans and domain swapping, 2G12 class, 2G12 family. Kwong2012 (review, structure, broad neutralizer)
• 2G12: This review discusses the new research developments in bnAbs for HIV-1, Influenza, HCV. Models of the HIV-1 Env spike and of Influenza visrus spike with select bnAbs bound are shown. Burton2012 (review)
• 2G12: Somatic hypermutations are preferably found in CDR loops, which alter the Ab combining sites, but not the overall structure of the variable domain. FWR of CDR are usually resistant to and less tolerant of mutations. This study reports that most bnAbs require somatic mutations in the FWRs which provide flexibility, increasing Ab breadth and potency. To determine the consequence of FWR mutations the framework residues were reverted to the Ab's germline counterpart (FWR-GL) and binding and neutralizing properties were then evaluated. 2G12, which recognizes carbohydrates, was among the 17 bnAbs which were used in studying the mutations in FWR. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 2G12. Klein2013 (neutralization, structure, antibody lineage)
• 2G12: Antigenic properties of 2 biochemically stable and homogeneous gp140 trimers (A clade 92UG037 and C clade CZA97012) were compared with the corresponding gp120 monomers derived from the same percursor sequences. The trimers had nearly all the antigenic properties expected for native viral spikes and were markedly different from monomeric gp120. 2G12 bound trimers and monomers equally well, indicating that the epitope is fully accessible in both forms. Kovacs2012 (antibody binding site, neutralization, binding affinity)
• 2G12: Crystal structure and mechanistic analysis of 2F5-gp41 complex is reported. b12 has been referred as a BnAb directed against the exterior gp120 envelope glycoprotein. Ofek2004 (antibody interactions, structure)
• 2G12: Glycan shield of HIV Env protein helps to escape the Ab recognition. Several of the PGT BnAbs interact directly with the HIV glycan coat. Crystal structures of Fabs PGT127 and PGT128 showed that the high neutralizing potency was mediated by cross-linking Env trimers on the viral surface. 2G12 was discussed in terms of recognizing terminal dimannose and binding to glycan coat. Pejchal2011 (glycosylation, structure, broad neutralizer)
• 2G12: Intrinsic reactivity of HIV-1, a new property regulating the level of both entry and sensitivity to Abs has been reported. This activity dictates the level of responsiveness of Env protein to co-receptor, CD4 engagement and Abs. 2G12 has been used as a control CD4BS binding Ab in neutralization assays. Haim2011 (antibody interactions)
• 2G12: Glycan Asn332-targeting broadly cross-neutralizing (BCN) antibodies were studied in 2 C-clade infected women. The ASn332 glycan was absent on infecting virus, but the BCN epitope with Asn332 evolved within 6 months though immune escape from earlier antibodies. Plasma from the subject CAP177 neutralized 88% of a large multi-subtype panel of 225 heterologous viruses, whereas CAP 314 neutralized 46% of 41 heterologous viruses but failed to neutralize viruses that lack glycan at 332. CAP177 or CAP314 clones were not sensitive to 2G12. Moore2012 (neutralization, escape)
• 2G12: This study reports the isolation of a panel of Env vaccine elicited CD4bs-directed macaque mAbs and genetic and functional features that distinguish these Abs from CD4bs MAbs produced during chronic HIV-1 infection. 2G12 was used as a negative control Abs in competitive binding assay with non human primates mAbs. Sundling2012 (vaccine-induced immune responses)
• 2G12: The goal of this study was to improve the humoral response to HIV-1 by targeting trimeric Env gp140 to B cells. The gp140 was fused to a proliferation-inducing ligand (APRIL), B cell activation factor (BAFF) and CD40 ligand (CD40L). These fusion proteins increased the expression of activation-induced-cytidine deaminase (AID) responsible for somatic hypermutation, Ab affinity maturation, and Ab class switching. The Env-APRIL induced high anti-Env responses against tier1 viruses. 2G12 was used in BN-PAGE trimer shift assay. Melchers2012 (neutralization)
• 2G12: Existing structural and sequence data was analyzed. A set of signature features for potent VRC01-like (PVL) and almost PVL abs was proposed and verified by mutagenesis. 2G12 has been referred in discussing the breadth and potency of antiCD4 abs. West2012a (antibody lineage)
• 2G12: Synthesis of an engineered soluble heterotrimeric gp140 is described. These gp140 protomers were designed against clade A and clade B viruses. The heterotrimer gp140s exhibited broader anti-tier1 isolate neutralizing antibody responses than homotrimer gp140. 2G12 was used to determine and compare the immunogenicity of homo and heterotrimers gp140s. 2G12 didn't exhibit any difference in binding to homotrimeric clade A and clade B gp140 binding. Sellhorn2012 (vaccine antigen design)
• 2G12: This paper showed that nAb 2G12, which binds to gp120 N glycans with α (1,2)-linked mannose termini and inhibits replication after passive transfer to patients, neutralizes by slowing entry of adsorbed virus. It is suggested that 2G12 competitively inhibits interactions between gp120 V3 loop and the tyrosine sulfate containing amino terminus, thus reducing assembly of complexes that catalyze entry. Platt2012 (antibody interactions, glycosylation)
• 2G12: The use of computationally derived B cell clonal lineages as templates for HIV-1 immunogen design is discussed. 2G12 has been discussed in terms of immunogenic and functional characteristics of representative HIV-1 BnAbs and their reactions to antigens. Haynes2012 (antibody interactions, memory cells, vaccine antigen design, review, antibody polyreactivity, broad neutralizer)
• 2G12: Polyclonal B cell responses to conserved neutralization epitopes are reported. Cross-reactive plasma samples were identified and evaluated from 308 subjects tested. 2G12 was used as a control mAb in the comprehensive set of assays performed. Plasma samples C1-0763 and C1-0219 showed comparable activities with 2G12 in competition ELISA. Tomaras2011 (neutralization, polyclonal antibodies)
• 2G12: Role of envelope deglycosylation in enhancing antigenicity of HIV-1 gp41 epitopes is reported. The mechanism of induction of broad neutralizing Abs is discussed. The hypothesis of presence of "holes" in the naive B cell repertoires for unmutated B cell receptor against HIV-1 Env was tested. The authors inferred that glycan interferences control the binding of unmutated ancestor Abs of broad neutralizing mAb to Env gp41. Ma2011 (glycosylation, neutralization)
• 2G12: The rational design of vaccines to elicit broadly neutralizing antibodies to HIV-1 is discussed in relation to understanding of vaccine recognition sites, the structural basis of interaction with HIV-1 env and vaccine developmental pathways. 2G12 has been mentioned regarding the recognition of high-mannose glycans Kwong2011 (antibody binding site, glycosylation, neutralization, vaccine antigen design, review)
• 2G12: A single-cell Ab cloning method is described to isolate neutralizing Abs using truncated gp160 transfected cells as bait. Among the 15 Abs reported, only two are found to be broadly neutralizing and bind to a novel conformational HIV-1 spike epitope. 2G12 was used as a control in neutralizing assay. Klein2012 (neutralization)
• 2G12: Several antibodies including 10-1074 were isolated from B-cell clone encoding PGT121, from a clade A-infected African donor using YU-2 gp140 trimers as bait. These antibodies were segregated into PGT121-like (PGT121-123 and 9 members) and 10-1074-like (20 members) groups distinguished by sequence, binding affinity, carbohydrate recognition, neutralizing activity, the V3 loop binding and the role of glycans in epitope formation. 2G12 was used as a control in virus neutralization assay. Detail information on the binding and neutralization assays are described in the figures S2-S11. Mouquet2012a (glycosylation, neutralization, binding affinity)
• 2G12: YU2 gp140 bait was used to characterize 189 new MAbs representing 51 independent IgG memory B cell clones from 3 clade A or B HIV infected patients exhibiting broad neutralizing activity. 2G12 has been used as a positive control for epitope mapping and evaluating these anti-gp-140 antibodies and a non-sensitive control to DMR/AAA triple mutation. Mouquet2011 (neutralization)
• 2G12: A panel of glycan deletion mutants was created by point mutation into HIV gp160, showing that glycans are important targets on HIV-1 glycoproteins for broad neutralizing responses in vivo. Enrichment of high mannose N-linked glycan(HM-glycan) of HIV-1 glycoprotein enhanced neutralizing activity of sera from 8/9 patients. 2G12 was used as a control. Lavine2012 (neutralization)
• 2G12: Ab-driven escape and Ab role in infection control and prevention are reviewed. Main focus is on NAbs, but Ab acting through effector mechanisms are also discussed. 2G12 which was isolated in 1996 and discussed in the context of developing broadly cross-neutralizing antibodies. Overbaugh2012 (escape, review)
• 2G12: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared. 2G12 bound gp120 and Env-VLPs equivalently. There was no significant correlation between E168K+N189A WT VLP binding and 2G12 neutralization, while trimer VLP ELISA binding and neutralization exhibited a significant correlation. BN-PAGE shifts using digested E168K + N189A WT trimer VLPs exhibited prominence compared to WT VLPs. Tong2012 (neutralization, binding affinity)
• 2G12: The ability of several broadly neutralizing antibodies that bind gp10 or gp41 to inhibit cell-cell fusion between Clone69TRevEnv cells induced to express the viral envelope proteins, gp120/gp41 and highly CD4-positive SupT1 cells was investigated. Little or no inhibitory effect on cell-cell fusion was observed. MAbs b12, m14 IgG and 2G12 had moderate inhibitory activity; MAbs 4E10 and 2F5 had no inhibitory activity. Yee2011 (antibody interactions)
• 2G12: Plasma from 14 R5-tropic SHIV-infected macaques was screened for broadly neutralizing activity. A macaque with highly potent cross-clade plasma NAb response was identified. Longitudinal studies showed that the development of broad and autologous NAb responses occurred coincidentally in this animal. Serum-mapping studies, using pseudovirus point mutants and antigen adsorption assays, indicated that the plasma bNAbs are specific for epitopes that include carbohydrates and are critically dependent on the glycan at position 332 of Env gp120. MAb 2G12 was used for comparison. Walker2011a (neutralization, polyclonal antibodies)
• 2G12: The role of V1V2 in the resistance of HIV-1 to neutralizing Abs was studied using a panel of neutralization-sensitive and -resistant HIV-1 variants and through exchanging regions of Env between neutralization-sensitive and -resistant viruses. An increase in the length of the V1V2 loop and/or the number of potential N-linked glycosylation sites (PNGS) in that same region of Env was directly involved in the neutralization resistance. The virus that was sensitive to neutralization by autologous serum was also sensitive to neutralization by MAbs b12, 2G12, 2F5, and 4E10, while the virus that was resistant to neutralization by autologous serum was also resistant to neutralization by all of these antibodies except MAb 2G12. vanGils2011 (glycosylation, neutralization, escape)
• 2G12: A standardized proficiency testing program for measurements of HIV-1-specific NAbs in the TZM-bl assay was developed. Three rounds of optimization involving 21 different test laboratories were required to design the final proficiency testing kit. MAbs b12, 2G12, 2F5, 4E10 and TriMab (b12+2G12+2F5) were used for testing. Todd2012 (assay or method development)
• 2G12: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors. Peressin2011 (genital and mucosal immunity, dendritic cells)
• 2G12: The reactivity profiles of MAbs 4E10, 2F5 and 2G12 to those of four pathogenic autoAbs derived from patients with antiphospholipid-syndrome (APS), and to serum from a patient with systemic lupus erythematosus (SLE) were compared using an autoantigen microarray comprising 106 connective tissue disease-related autoantigens. The reactivity profiles of bNt anti-HIV-1 MAbs were distinct from those of pathogenic autoAbs. Singh2011 (antibody polyreactivity)
• 2G12: Broadly neutralizing antibodies circulating in plasma were studied by affinity chromatography and isoelectric focusing. The Abs fell in 2 groups. One group consisted of antibodies with restricted neutralization breadth that had neutral isoelectric points. These Abs bound to envelope monomers and trimers versus core antigens from which variable loops and other domains have been deleted. Another minor group consisted of broadly neutralizing antibodies consistently distinguished by more basic isoelectric points and specificity for epitopes shared by monomeric gp120, gp120 core, or CD4-induced structures. The pI values estimated for neutralizing plasma IgGs were compared to those of human anti-gp120 MAbs, including 5 bnMAbs (PG9, PG16, VRC01, b12, and 2G12), 2 narrowly neutralizing MAbs (17b and E51), and 3 nonneutralizing MAbs (A32, C11, and 19e). bnMAbs VRC01, 2G12 and b12 had basic pIs (8.1 to >9). Sajadi2012 (polyclonal antibodies)
• 2G12: Small sized CD4 mimetics (miniCD4s) were engineered. These miniCD4s by themselves are poorly immunogenic and do not induce anti-CD4 antibodies. Stable covalent complexes between miniCD4s and gp120 and gp140 were generated through a site-directed coupling reaction. These complexes were recognized by CD4i antibodies as well as by the HIV co-receptor CCR5 and elicited CD4i antibody responses in rabbits. A panel of MAbs of defined epitope specificities, was used to analyze the antigenic integrity of the covalent complexes using capture ELISA. MAb 2G12 was used to normalize the concentration of gp140 vs gp140-miniCD4 complex. Martin2011 (mimics, binding affinity)
• 2G12: Sensitivity to neutralization was studied in 107 full-length Env molecular clones from multiple risk groups in various locations in China. Neutralization sensitivity to plasma pools and bNAbs was not correlated. MAbs 2F5 and G12 failed to neutralize almost all viruses in the C/07/08/B'C subtype group. 2F5 was potent in neutralizing viruses in subtype B′ and CRF01_AE, while 2G12, could only neutralize a 6/9 of subtype B′ viruses and none of the CRF01_AE viruses. 23/24 2G12-resistant viruses lacked the glycan at position 295 or 332 or both. Shang2011 (glycosylation, neutralization, subtype comparisons)
• 2G12: The long-term effect of broadly bNAbs on cell-free HIV particles and their capacity to irreversibly inactivate virus was studied. MPER-specific MAbs potently induced gp120 shedding upon prolonged contact with the virus, rendering neutralization irreversible. The kinetic and thermodynamic requirements of the shedding process were virtually identical to those of neutralization, identifying gp120 shedding as a key process associated with HIV neutralization by MPER bNAbs. Neutralizing and shedding capacity of 7 MPER-, CD4bs- and V3 loop-directed MAbs were assessed against 14 divergent strains. Neutralization with 2G12 was reversible, as 2G12 immediately lost the majority of neutralization activity once access antibody was removed. 2G12 induced 30-60% shedding with 5/14 probed viruses, suggesting that although not a potent shedding inducer, 2G12 can not be considered incapable of inducing shedding. Ruprecht2011 (neutralization, kinetics)
• 2G12: Circulating HIV-1 virion-immune complexes (ICs), present in approximately 90% of acute subjects were quantified, and the levels and antibody specificity to those in chronic infection were compared. Similar to a nonneutralizing anti-gp41 MAb 7B2, purified plasma IgG from acute HIV-1 subjects bound both infectious and noninfectious virions. This was in contrast to the neutralizing antibody 2G12 MAb that bound predominantly infectious virions. Liu2011c (binding affinity)
• 2G12: Gold nanoparticles coated with self-assembled monolayers of synthetic oligomannosides [manno-gold glyconanoparticles (GNPs)], which are present in gp120, bound 2G12 with high affinity and interfered with 2G12/gp120 binding. GNPs coated with a linear tetramannoside could block the 2G12-mediated neutralization of a replication-competent virus under conditions that resemble the ones in which normal serum prevents infection of the target cell. Marradi2011 (glycosylation, neutralization)
• 2G12: Deglycosylations were introduced into the 24 N-linked glycosylation sites of a R5 env MWS2 cloned from semen. Mutants N156-T158A, N197-S199A, N262-S264A and N410-T412A conferred decreased infectivity and enhanced sensitivity to a series of antibodies and entry inhibitors. Mutant N156-T158A showed enhanced neutralization sensitivity to MAb 17b in the absence of soluble CD4, suggesting that deglycosylation in these sites on gp120 may be beneficial for the exposure of a CD4 induced epitope which only exists in the CD4-liganded form of gp120. Huang2012 (glycosylation, neutralization)
• 2G12: This study analyzed the neutralization sensitivity of sequential HIV-1 primary isolates during their natural evolution in 5 subtype B and CRF02_AG HIV-1 infected drug naive individuals to 13 anti-HIV-1 MAbs (including this MAb) directed at epitopes in the V2, V3, CD4bd and carbohydrates. Patient viruses evolved to become more sensitive to neutralization by MAbs directed at epitopes at V2, V3 and CDbd, indicating that cross sectional studies are inadequate to define the neutralization spectrum of MAb neutralization with primary HIV-1 isolates. Haldar2011 (neutralization)
• 2G12: This is a detailed systematic study of the molecular recognition of five synthetic oligomannosides 1–5 in solution by the antibody 2G12 by using ligand-based NMR techniques, specifically saturation transfer difference (STD) NMR spectroscopy and transferred NOE experiments. Enriquez-Navas2011 (glycosylation, structure)
• 2G12: The sensitivity to PG9 and PG16 of pseudotyped viruses was analysed carrying envelope glycoproteins from the viral quasispecies of three HIV-1 clade CRF01_AE-infected patients. It was confirmed that an acidic residue or a basic residue at position 168 in the V2 loop is a key element determining the sensitivity to PG9 and PG16. In addition, evidence is provided of the involvement of a conserved residue at position 215 of the C2 region in the PG9/PG16 epitopes. B clones were tested against 2G12 MAb recognizing a conformational glycan-dependent epitope on gp120 but 2G12 was not used for the CRF01_AE clones since all of them lacked the N332 residue, which constitutes one of the essential N-glycosylation sites of the 2G12 epitope. 2G12 sensitivity of B clones remained comparable, with only one resistant clone, 5008CL3, which became moderately sensitive. Thenin2012a (neutralization)
• 2G12: Given the potential importance of cell-associated virus during mucosal HIV-1 transmission, sensitivity of bNAbs targeting HIV-1 envelope surface unit gp120 (VRCO1, PG16, b12, and 2G12) and transmembrane domain gp41 (4E10 and 2F5) was examined for both cell-free and mDC-mediated infections of TZM-bl and CD4+ T cells. It was reported that higher gp120-bNAb concentrations, but not gp41-directed bNAb concentrations, are required The IC50 and IC90 for anti-gp120–directed bNAb 2G12, were significantly higher for almost all mDC-mediated virus transmission (Lai, NL4-3, Lai/Balenv), compared with cell-free HIV-1 infection.to inhibit mDC-mediated virus spread, compared with cell-free transmission. Only cell-free and mDC-mediated infection of 89.6 virus particles demonstrated no significant IC50 difference against 2G12. 2G12 did not readily bind mDCs in the absence of virus. Around 18% of the mDC–T cell synaptic junctions displayed colocalization of Gag-eGFP VLPs with 2G12. Furthermore, 2G12 did not localize at DC–T cell synaptic junctions in the absence of Gag-eGFP VLPs. Sagar2012 (neutralization, binding affinity)
• 2G12: To overcome the many limitations of current systems for HIV-1 virus-like particle (VLP) production, a novel strategy was developed to produce HIV-1 VLP using stably transfected Drosophila S2 cells by cotransfecting S2 cells with plasmids encoding an envelope glycoprotein (consensus B or consensus C), a Rev-independent Gag (Pr55) protein, and a Rev protein, along with a pCoBlast selection marker. Except for antigenic epitope PG16, all other broadly neutralizing antigenic epitopes 2G12, b12, VRC01, and 4E10 tested are preserved on spikes of HIV-1 VLP produced by S2 clones. Yang2012 (assay or method development, neutralization)
• 2G12: In order to increase recognition of CD4 by Env and to elicit stronger neutralizing antibodies against it, two Env probes were produced and tested - monomeric Env was stabilized by pocket filling mutations in the CD4bs (PF2) and trimeric Env was formed by appending trimerization motifs to soluble gp120/gp14. PF2-containing proteins were better recognized by bNMAb against CD4bs and more rapidly elicited neutralizing antibodies against the CD4bs. Trimeric Env, however, elicited a higher neutralization potency that mapped to the V3 region of gp120. Feng2012 (neutralization)
• 2g12: A way to produce conformationally intact, deglycosylated soluble, cleaved recombinant Env trimers by inhibition of the synthesis of complex N-glycans during Env production, followed by treatment with glycosidases under conditions that preserve Env trimer integrity is described to facilitate crystallography and immunogenicity studies. As expected, the glycan-dependent 2G12 did not bind to the deglycosylated trimers. Depetris2012 (glycosylation, binding affinity)
• 2G12: The sera of 113 HIV-1 seroconverters from three cohorts were analyzed for binding to a set of well-characterized gp120 core and resurfaced stabilized core (RSC3) protein probes, and their cognate CD4bs knockout mutants. 2G12 bound strongly to RSC3, RSC3/G367R and RSC3 Δ3711, weakly bound to RSC3 Δ3711/P363N, very weakly bound to gp120 core and did not bind to gp120 core D368R. Lynch2012 (binding affinity)
• 2G12: Sensitivity to bNAbs of primary R5 HIV-1 isolates sequentially obtained before and after AIDS onset was studied. End-stage disease HIV R5 isolates were more sensitive to neutralization by TriMab, an equimolar mix of the IgGb12, 2F5 and 2G12 antibodies, than R5 isolates from the chronic phase. The increased sensitivity correlated with low CD4+ T cell count at time of virus isolation and augmented viral infectivity. Envs from end-stage R5 variants had increased positive surface charge and reduced numbers of potential N-linked glycosylation sites (PNGS). These molecular changes in Env also correlated to sensitivity to neutralization by the individual 2G12 MAb. Molecular modeling suggested that the glycosylation sites lost at end-stage disease are located in close proximity to the 2G12 epitope. Borggren2011 (glycosylation, neutralization)
• 2G12: To test whether HIV-1 particle maturation alters the conformation of the Env proteins, a sensitive and quantitative imaging-based Ab-binding assay was used to probe the conformations of full-length and cytoplasmic tail (CT) truncated Env proteins on mature and immature HIV-1 particles. Binding of MPER-specific MAb Z13e1 to immature particles was greater than to mature virions and the increase was abolished by truncation of the gp41 CT. Z13e1 bound immature particles approximately 1.5 to 2 times as well as mature particles when the median binding signals were compared indicating that the recognized neutralization-sensitive epitopes undergo conformational masking during HIV-1 particle maturation. Joyner2011 (binding affinity)
• 2G12: Humoral responses to specific, linear gp41 epitopes were that were already known to be the target of broadly neutralizing antibodies were compared in a cohort of sub-Saharan mother-child pairs. TriMab positive-control Abs (2F5, 2G12, and b12) neutralized all viruses tested: the subtype B laboratory strains SF162 (R5-B) and IIIB (X4-B), and the low-sensitivity subtype C strains, primary isolates DU172 and DU156 (both R5-C). The TriMab control inhibited strain DU156 when all neutralization assays were performed on the DU156 HIV isolate (C-R5) with cord blood specimens from EUN babies. Diomede2012 (neutralization, mother-to-infant transmission, subtype comparisons)
• 2G12: The possibility to construct a polyepitope B-cell immunogen (TBI-2g12) containing linear mimetics of conformational epitopes and its immunogenic properties was examined. The aim was to select the most active peptide mimetic recognized by MAb 2G12 and to construct the protein immunogen by attaching the selected peptide mimotope VGAFGSFYRLSVLQS to a protein carrier. It was shown that the TBI-2g12 as well as the original TBI induce antibodies, that recognize HIV-1 proteins, TBI protein using ELISA and immunoblotting. Though only anti-TBI-2g12 serum recognized the synthetic peptide mimotope VGAFGSFYRLSVLQS, whereas the antibodies against original TBI don’t recognize it. The neutralization assay demonstrated that serum antibodies of the mice immunized with TBI-2g12 possess virus neutralizing activity suggesting that principal epitope responsible for virus neutralizing activity was formed from VGAFGSFYRLSVLQS peptide in the structure of TBI-2g12 protein. Karpenko2012 (mimotopes, neutralization)
• 2G12: 162 full-length envelope (env) clones were generated from plasma RNA obtained from 5 HIV-1 Clade B infected mother-infant pairs and their V1-V5 genotypes and phylogeny were extensively characterized. All clones from three infants were resistant to 2G12 and exhibited mutations eliminating one of five PNGS implicated in 2G12 binding. Most maternal clones from these pairs exhibited similar levels of 2G12 resistance, and displayed the corresponding mutations. Kishko2011 (neutralization, mother-to-infant transmission)
• 2G12: HIV-1 adaptation to neutralization by MAbs VRC01, PG9, PG16 was studied using HIV-1 variants from historic (1985-1989) and contemporary (2003-2006) seroconverters. 2G12 was included for comparison and neutralized 5% of contemporary viruses at IC50 < 1 μ g/ml and 14% at IC50 < 5 μ g/ml. TriMab construct, consisting of MAbs b12, 2F5 and 2G12 in equal concentrations, showed the highest neutralization correlation with 2F5 and little similarity with 2G12. Euler2011 (neutralization)
• 2G12: The neutralization potency of PG9, PG16, VRC01 and PGV04 was approximately 10-fold greater than that of MAbs b12, 2G12, 2F5 and 4E10. Falkowska2012 (neutralization)
• 2G12: Neutralizing antibody repertoires of 4 HIV-infected donors with remarkably broad and potent neutralizing responses were probed. 17 new monoclonal antibodies that neutralize broadly across clades were rescued. All MAbs exhibited broad cross-clade neutralizing activity, but several showed exceptional potency. Although 2G12 neutralized 32% of 162 isolates at IC50<50 μg/ml, it was almost 100-fold less potent than several new antibodies PGT 121-123 and 125-128, for which the median antibody concentration required to inhibit HIV activity by 50% or 90% (IC50 and IC90 values) was almost 100-fold lower than that of b12, 2G12 and 4E10. Walker2011 (neutralization)
• 2G12: Studies were conducted to determine whether differences in immunogenic potential exist between two previously reported primary Env antigens (Clade B primary Env antigens LN40 and B33) with closely related gene sequences and completely different phenotypic features. The B33 Env is resistant to MAb 2G12, while the LN40 Env, having the opposite phenotype of B33, is sensitive to MAb 2G12. Vaine2011 (neutralization)
• 2G12: HIV-1 subtype C env genes from 19 mother-infant pairs: 10 transmitting in utero (IU) and 9 transmitting intrapartum (IP) were analyzed. A severe genetic bottleneck during transmission was confirmed in all pairs. Compared to the maternal viral population, viruses transmitted IP tended to have shorter variable loops and fewer putative N-linked glycosylation sites than viruses transmitted IU. The pseudotyped viruses displayed some sensitivity to 4E10 and soluble CD4 but were resistant to 2G12, 2F5, and IgG1b12. Russell2011 (glycosylation, neutralization, mother-to-infant transmission)
• 2G12: The influence of potential N-linked glycosylation site (PNGS) N302 on 2G12 sensitivity was assessed based on chimeric envelope genes created by swapping the V1V2 domains of the two env clones. Both the exchange of the V1V2 domain and the introduction of the PNGS at N302 on the 2G12-sensitive clone induced a significant decrease in sensitivity to 2G12. In contrast, the reverse V1V2 exchange and the removal of the PNGS at N302 on the 2G12-resistant clone increased sensitivity to 2G12, confirming the influence of these regions on 2G12 sensitivity. It suggests that both the V1V2 loop and an additional PNGS in V3 might limit access to the 2G12 epitope. Chaillon2011 (glycosylation, neutralization, structure)
• 2G12: To elicit 2G12-like Ab response it was shown that Manα1→2Man motif was the primary carbohydrate neutralization determinant of HIV-1 that elicited Abs to the self oligomannose glycans. While 2G12 is known to bind to this motif, the specificity of the mannan immune serum (ΔMnn1: S. cerevisiae deficient in the α1→3 mannosyltransferase gene) seemed narrower than some alternative modes of binding postulated for 2G12. ΔMnn1 immune sera revealed fine carbohydrate specificity to Manα1→2Man units, closely matching that of 2G12. The sera also appeared to tolerate the presence of D1 glucosylation indicating perhaps a somewhat wider degree of monosaccharide or linkage specificity compared to 2G12. Dunlop2010 (antibody binding site)
• 2G12: The development and characterization of a tier 1 R5 SHIV, termed SHIV-1157ipEL is reported. SHIV-1157ipEL is a chimera of the "early", neutralization-sensitive SHIV-1157ip envelope and the "late", neutralization-resistant engineered backbone of SHIV-1157ipd3N4. Molecular modeling revealed a possible mechanism for the increased neutralization resistance of SHIV-1157ipd3N4 Env: V2 loops hindering access to the CD4 binding site, shown experimentally with NAb b12. Sequence analysis performed of the SHIV-1157ipEL-p showed a loss of N295, a key amino acid residue in the epitope of 2G12 that caused SHIV-1157ipEL to become resistant to 2G12. 2G12 only neutralized SHIV-SF162P4 out of the 4 C clade and 2 B clade SHIV strains tested. Siddappa2010 (neutralization, vaccine antigen design, subtype comparisons)
• 2G12: Purified MAb 2G12, produced by transient expression in Nicotiana benthamiana using replicating and non-replicating systems based on deleted versions of Cowpea mosaic virus (CPMV) RNA-2, was expressed and characterized based on biochemical properties, in vitro activity and neutralization capabilities. The plant derived purified 2G12 (delRNA-2 + RNA-1 or CPMV-HT) was not as pure as CHO-produced 2G12 (reference standard) although no significant differences were observed between 2G12 produced by delRNA-2 with RNA-1 or by CPMV-HT. Also, 2G12 glycosylation was not greatly affected by the presence of RNA-1 or CPMV-HT. The binding activity of plant derived 2G12 was slightly lower than CHO-produced 2G12 although its neutralization capability was similar to that of CHO-produced 2G12. Sainsbury2010 (glycosylation, neutralization, binding affinity)
• 2G12: This review discusses current understanding of Env neutralization by antibodies in relation to epitope exposure and how this insight might benefit vaccine design strategies. This MAb is in the list of current MAbs with notable cross-neutralizing activity. Pantophlet2010 (neutralization, variant cross-reactivity, review)
• 2G12: This review outlines the general structure of the gp160 viral envelope, the dynamics of viral entry, the evolution of humoral response, the mechanisms of viral escape and the characterization of broadly neutralizing Abs. The review discusses the special structure of 2G12 which allows it to overcome the glycan masking strategy that HIV-1 uses to protect itself from antibody recognition. It is noted also that 2G12 can neutralize a significant number of primary isolates from clade B, but is less effective against non-clade B viruses and is not active against most clade C. 2G12 provided protection in macaques against SHIV. Gonzalez2010 (neutralization, variant cross-reactivity, escape, review)
• 2G12: The expression and characterization of different glycoforms of V3-Fc fusion protein along with its binding to HIV-neutralizing Abs 2G12 and 447-52D was examined. The binding affinity of 2G12 was significantly high for the high-mannose type glycoforms of V3-Fc (V3-Fc-HM, V3-Fc-M9 and the two mutants:N301A and Fc-N297A) following a quick association/dissociation kinetic process, although it was not measurable for the complex type glycoform V3-Fc-CT. The affinity to 2G12 was reduced more by removal of the N-glycan at the N301 site than at the N297 site. Very high affinity to 2G12 was observed for gp120 with extremely slow dissociation rate. Yang2010a (glycosylation, binding affinity)
• 2G12: This review discusses recent rational structure-based approaches in HIV vaccine design that helped in understanding the link between Env antigenicity and immunogenicity. This MAb is mentioned in the context of immunogens based on the epitopes recognized by bNAbs. 2G12 adopts an unusual domain exchanged structure to recognize a conserved cluster of oligomannose residues on the outer domain of gp120 and has provided a basis for the design of immunogens to target the HIV-1 glycan shield. Walker2010a (neutralization, review)
• 2G12: 37 Indian clade C HIV-1 Env clones obtained at different time points from five patients with recent infection, were studied in neutralization assays for sensitivities to their autologous plasma antibodies and mAbs. All Env variants were resistant to 2G12, except those obtained from IVC-3 patient. This resistance was associated with the absence of N-linked glycosylation site at position 295 at the N-terminal base of V3 loop. The sensitivity of IVC-3 clones was due to the presence of N295, atypical of clade C. Ringe2010 (neutralization)
• 2G12: This review discusses strategies for design of neutralizing antibody-based vaccines against HIV-1 and recent major advances in the field regarding isolation of potent broadly neutralizing Abs. Sattentau2010 (review)
• 2G12: The effect of absence and presence of sCD4 on accessibility and binding of HIV-1 gp41 MPER-binding epitopes on CCR5-tropic pseudoviruses from five different clades to the mAbs was studied. The 2G12 N-sites 295, 332, 339, 386, 392 were examined. 2G12 showed high binding affinity to pseudoviruses from clade A (epitope mutant:tWFDIs), clade B (NWFDIT) and clade D (NWFsIT), and very low binding affinity to clade A (NWFDIs), clade B (sWFsIT), clade C (sWFsIT), clade D (NWFsIT) and clade CRF01_AE (NWFDIT) and no binding to clade C (sWFsIT) and clade CRF01_AE (NWFDIs). Peachman2010a (variant cross-reactivity, binding affinity, subtype comparisons)
• 2G12: Most of the 34 Env-pseudotyped viruses from HIV-1 CRF01_AE - infected plasma samples collected in China could efficiently infect target cells in the presence of high concentrations of 2G12 MAb. Only 1/34 viruses showed low 2G12 susceptibility and all viruses lacked one or more glycans at positions critical for 2G12 neutralization. Nie2010 (glycosylation, neutralization)
• 2G12: This review discusses the studies done on poly-reactive antibodies (binding to two different epitopes), and the importance of polyreactivity. Low polyreactivity has been reported for 2G12. Pluckthun2010 (review, antibody polyreactivity)
• 2G12: A lentiviral vector encoding the heavy and light chains of 2G12 was transduced in the primary human B cells and directed production of 2G12. NOD/SCID/γc mice were transplanted with human hematopoetic stem cells (hu-HSC) transduced with the vector and the animals were inoculated with HIV-1. Mice engrafted with the 2G12-transducted cells displayed a 70-fold reduction in plasma RNA levels and a 200-fold reduction in HIV-1 infected spleen cells compared to control mice, indicating inhibition of in vivo HIV infection by this gene therapy approach. Joseph2010
• 2G12: This paper shows that a highly neutralization-resistant virus is converted to a neutralization sensitive virus with a rare single mutation D179N in the C-terminal portion of the V2 domain for several antibodies. 2G12, however, did not neutralize any of the mutants tested. ORourke2010 (neutralization, variant cross-reactivity)
• 2G12: MAb m9 showed superior neutralization potency compared to 2G12 in a TZM-bl assay, where it neutralized all 15 isolates compared to 2G12 that neutralized only 4 clade B isolates but not clade A or C isolates. Zhang2010 (neutralization)
• 2G12: A side-by-side comparison was performed on the quality of Ab responses in humans elicited by three vaccine studies focusing on Env-specific Abs. Minimal presence of 2G12-like Abs was detected in the three vaccine trials. 17% of sera from the HVTN 203 trial, 0% of sera from the HVTN 041 trial, and 24% of sera from the DP6-001 trial were able to outcompete binding to 2G12 MAb. Vaine2010 (antibody interactions)
• 2G12: This review focuses on recent vaccine design efforts and investigation of broadly neutralizing Abs and their epitopes to aid in the improvement of immunogen design. NAb epitopes, NAbs response to HIV-1, isolation of novel mAbs, and vaccine-elicited NAb responses in human clinical trials are discussed in this review. Mascola2010 (review)
• 2G12: Naturally occurring human and experimentally induced murine and rabbit GBV-C E2 Abs were studied for their ability to neutralize diverse HIV-isolates and showed that broadly neutralizing HIV Abs were elicited on immunization of rabbits with GBV-C E2. MAb 2G12 neutralized R5 and dual R5-X4 HIV-1 isolates of subtypes A and B in primary human PBMCs. The TriMAb control including 2G12 did not neutralize the HIV-1 R5 isolate in TZM-bl cells but did in PBMCs. Mohr2010 (neutralization)
• 2G12: A mathematical framework is designed to determine the number of Abs required to neutralize a single trimer called the stoichiometry of trimer neutralization. 15 different virus antibody combinations divided into five groups based on antibody binding sites were used in the designed model. 2G12 is in a group by itself as it recognizes a carbohydrate-dependent epitope on gp120. The number of 2G12 Abs needed to neutralize a single trimer was estimated as 1 with 97 percent probability. Magnus2010
• 2G12: BanLec is a lectin isolated from the fruit of bananas that was shown to inhibit HIV-1 isolates of different subtypes and tropisms. Pretreatment of gp120 with BanLec inhibited recognition by 2G12 in a dose-dependent manner, indicating that BanLec inhibits HIV-1 by binding to high-mannose structures also recognized by 2G12. Swanson2010
• 2G12: Four human anti-phospholipid mAbs were reported to inhibit HIV-1 infection of human PBMC's by binding to monocytes and releasing soluble chemokines. The ability of different anti-phospholid mAbs to inhibit pseudovirus infection was studied. Four out of nine anti-phospholid mAbs inhibited HIV-1 infectivity in PBMC-based virus infection inhibition assay where a mixture of mAbs 2F5, IgG1b12, and 2G12 (TriMab) was used as a positive control. Moody2010 (neutralization)
• 2G12: A naturally occurring dimeric form of 2G12 was shown to have increased neutralization potency and increased ADCC activity compared to the monomeric form of 2G12. An ADCC-enhancing double mutation improved the ADCC activity of 2G12 monomer more than 2G12 dimer. Klein2010a (ADCC)
• 2G12: Targeted neutralizing epitopes have been identified based on the change in sensitivity to neutralization due to variations in known immunoepitopes studied in 17 subjects. The glycan removal by N332S mutant from gp120 outer domain decreased the neutralization of gp160 by 2G12. In addition, the N332S mutant escaped neutralization by two patient sera. Nandi2010 (neutralization, escape)
• 2G12: Molecular modeling was used to construct a 3D model of an anti-gp120 RNA aptamer, B40t77, in complex with gp120. Externally exposed residues of gp120 that participated in stabilizing interaction with the aptamer were mutated. Binding of 2G12 to gp120 was inhibited by B40t77, which is suggested to be due to distant conformational changes of gp120 induced by the aptamer. Joubert2010 (binding affinity, structure)
• 2G12: A yeast glycosylation mutant was created to expose numerous terminal Man1,2-Man residues. Although the yeast did not bind to 2G12, immunization of rabbits resulted in sera containing Manα1,2-Manα1,2-Man-specific Abs that cross-reacted with Env glycoproteins from HIV-1 subtypes A, B and C. Luallen2010 (glycosylation, vaccine antigen design)
• 2G12: 2G12 was shown to capture virion particles completely devoid of HIV-1 Env. Virus capture assay was modified with added incubation of virions and MAbs in solution followed by removal of unbound MAbs, which nearly eliminated the Env-independent binding by this Ab. This modification also allowed for relative affinity of 2G12 for virions to be quantified. There was an overall reduction in the efficiency of capture of molecular clones (MC) relative to pseudotyped virions by 2G12. In addition, trimeric JR-FL MC was captured more efficiently by 2G12 than nontrimeric Envs from JR-CSF MC virus. Leaman2010 (assay or method development, binding affinity)
• 2G12: The role of HIV-1 envelope spike density on the virion and the effect it has on MAb avidity, and neutralization potencies of MAbs presented as different isotypes, are reviewed. Engineering approaches and design of immunogens able to elicit intra-spike cross-linking Abs are discussed. Klein2010 (review)
• 2G12: 18 unique Env clones of subtype C HIV-1 derived from six African countries and Scotland were tested for their neutralization susceptibility by 2G12. 2G12 neutralized only one of the isolates. Koh2010a (neutralization)
• 2G12: Glycoconjugates were designed consisting of four- and eight-valent high-mannose HIV-1 related oligosaccharides clustered onto flexible polyamidoamine (PAMAM) dendrons and subsequently conjugated to well-characterized nontoxic diphtheria toxin mutant CRM197 as a carrier. The multivalent presentation of oligomannoses increased the avidity to 2G12. Antisera of mice and rabbits immunized with the glycoconjugates failed to recognize recombinant HIV-1 proteins. Kabanova2010 (glycosylation, vaccine antigen design, binding affinity)
• 2G12: The effect of presence and absence of V1 loop was assessed using two approaches: remove V1 loop from the soluble trimeric gp140 construct (ΔV1SF162gp140) and second, substitute the V1 loop on SF162gp140 construct with four different V1 loops from 89.6, YU2, JRFL, and HxB2 (heterologous HIV-1 viruses). Deletion or substitution of V1 loop did not affect neutralization by 2G12 and there was only a small change in binding affinity to 2G12. D368R modification to SF162gp120 did not affect the binding by 2G12, although it abrogated neutralization by 2G12 at lower MAb concentrations. Ching2010 (neutralization, binding affinity)
• 2G12: A hybrid nonself sugar was designed based on the crystal structure of D-fructose in complex with 2G12 Fab to elicit high 2G12 Ab response based on much enhanced (9 times) affinity of 2G12 for D-fructose compared to D-mannose. Introduction of nonself modifications into the D1 arm of high-mannose sugars led to additional interactions of nonself modifications to the 2G12 binding site resulting in enhanced antigenicity. The nonself glycan enhanced 2G12 binding compared to the self glycan, and the antibodies generated in immunized rabbits cross-reacted with the self glycan present in different conjugates, but did not bind the self D1 glycan motif when present on gp120. Doores2010c (glycosylation, binding affinity)
• 2G12: The effect of HIV-1 complement opsonization on 2G12 activity was evaluated in three instances: HIV-1 transcytosis through epithelial cells, HIV-1 attachment on immature monocyte derived dendritic cells (iMDDC), and infectivity of iMDDC. 2G12 was not able to inhibit HIV-1 transcytosis. 2G12 inhibited the attachment of non-opsonised HIV to iMDDC but had no effect on the opsonized HIV-1 attachment. 2G12 was able to inhibit production of both opsonized and non-opsonized HIV-1 in iMDDCs. Jenabian2010 (complement)
• 2G12: A germ line version of 2G12 was constructed that was not domain exchanged and did not detectably bind to gp120. Introducing increasing number of substitutions to germ line 2G12 resulted in domain exchanged wild type form of this Ab. Only 5-7 crucial substitutions were found necessary to induce considerable domain exchange of germ line 2G12; Ih19, Rh57, Eh75, Rh39, Ah14, Vh84 and Ph113. Huber2010 (antibody binding site)
• 2G12: Clustering analysis was performed to find patterns of neutralization reactivity for the dataset of 103 patients sera against 20 viruses. The clustering by five MAbs (including 2G12) against the 20 isolates was less statistically robust than that with serum titers, resulting in three clusters for both cases. The membership in an isolate cluster defined by serum titers was compared with its sensitivity to every MAb to understand the relationship of serum and MAb reactivity. Membership in all the three clusters did not correlate with sensitivity to 2G12. Doria-Rose2010 (neutralization)
• 2G12: The sensitivity of subtype C viruses to lectins GRFT, CV-N and SVN was analysed and compared to that of subtype A and B viruses which showed same sensitivity by all three viruses for all the three lectins. It was also examined whether lectin binding interfered with the access to the 2G12 epitope and there was competition among the compounds for virus capture. GRFT and CV-N inhibited the virus capture more effectively than SVN. Virus capture by 2G12 was inhibited for all three viruses using same amount of lectin concentrations. The results suggested overlap of 2G12 epitope with the binding sites of all the three lectins. Alexandre2010 (binding affinity)
• 2G12: Addition of bacterial endotoxin (LPS) had no effect on the potency of 2G12 neutralization in TZM-bl assay but addition of LPS in PBMC assay increased neutralization potency of 2G12. Endotoxin contamination was shown to mediate release of antiviral chemokines in PBMCs and is thus suggested to be able to cause false-positive results in PBMC-based neutralization assays. Geonnotti2010 (neutralization)
• 2G12: In order to overcome problems of the PBMC-based neutralization assay a novel approach was developed utilizing a platform based on Renilla luciferase (LucR) expressing HIV-1 proviral backbone. Env-IMC-LucR reporter viruses expressing HIV-1 envs from different virus strains were incubated with NAbs, such as 2G12, and used to infect donor PBMCs. The inhibition was assessed by measuring virus-encoded LucR activity in the cell lysates. There was a dosage dependent effect of 2G12 on virus infectivity. Variation in sensitivity to 2G12 was observed among different donor PBMCs, and this high variability was suggested to be a real biological effect attributable to use of different donor PBMCs, rather than assay-to-assay variability. Edmonds2010 (assay or method development, neutralization)
• 2G12: The identity of N-linked glycans from primary isolates of subtypes A, B and C was studied. Results showed highly conserved virus-specific glycan profile devoid of medial Golgi-mediated processing. When mutant viruses with glycosylation site deletions that disrupt the 2G12 epitope were analyzed, there was a modest decrease of Man8-9GlcNAc2 glycans, but the overall profile remained unperturbed. This confirmed the sensitivity of 2G12 for a small subset of Manα1-2Man glycans. Doores2010b (glycosylation)
• 2G12: Subtype B HIV-1 variants from historical seroconverters (individuals that seroconverted between 1985 and 1989) were equally sensitive to neutralization by 2G12 as variants isolated from contemporary seroconverters (ndividuals that seroconverted between 2003 and 2006). Bunnik2010a (neutralization, dynamics)
• 2G12: 17b was linked with sCD4 and the construct was tested for its neutralization breadth and potency. sCD4-17b showed significantly greater neutralization breadth and potency compared to 2G12, neutralizing 100% of HIV-1 primary isolates of subtypes A, B, C, D, F, CRF01_AE and CRF02_AG, while 2G12 neutralized some isolates of subtypes B and D. Unlike sCD4-17b, 2G12 was not equivalently active against virus particles generated from different producer cell types. Lagenaur2010 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: A set of Env variants with deletions in V1/V2 was constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Sensitivity of the evolved ΔV1V2 viruses was evaluated to study accessibility of their neutralization epitopes. 2G12 neutralized and bound to both cleaved and uncleaved ΔV1V2 variants more potently compared to the wild type virus, indicating better accessibility of the 2G12 epitope when the V1V2 domain is deleted. Bontjer2010 (neutralization, binding affinity)
• 2G12: Five different glycoforms of 2G12, generated in wild type and glycoengineered plants and in Chinese hamster ovary cells, were used to investigate the impact of Ab Fc glycosylation on the antiviral activity of the Ab. All five 2G12 glycoforms had similar binding profiles to cells expressing FcγRI, FcγRIIa or FcγRIIb. In contrast, two glycoforms of 2G12 lacking fucose showed significantly enhanced binding to cells expressing FcγRIIIa, compared to 2G12 glycoforms carrying core fucose. The two non-fucosylated forms of 2G12 also showed stronger antiviral activity against HIV-1 and SIV in ADCVI-assays compared to the fucosylated forms of 2G12. Forthal2010 (glycosylation, binding affinity)
• 2G12: A single amino acid substitution (I19R) was used to produce a nondomain-exchanged variant of 2G12 (2G12 I19R). 2G12 I19R was able to recognize the same mannose motifs on recombinant gp120, synthetic glycoconjugates, and on Candida albicans as the wild type 2G12. However, 2G12 I19R was unable to recognize the cluster of mannose motifs in the context of HIV envelope trimer, and was unable to neutralize 2G12-sensitive HIV-1 pseudovirions. Crystallographic structure of 2G12 I19R showed that this Ab and the wild type 2G12 have identical Fab binding units but that they display dramatically different juxtapositioning of their variable versus constant regions. These differences lead to remarkably different binding characteristics. Doores2010a (glycosylation, neutralization, binding affinity, structure)
• 2g12: Various UV-activatable azido- and iodo-based hydrophobic compounds have been studied for their ability to inactivate HIV-1 virus while preserving their surface antigenic structures. The virus was inactivated by treating it with azido-containing hydrophobic compounds and UV irradiation. The preservation of known neutralizing epitopes on the viral surface of treated virus was tested using the known neutralizing Abs. There was no significant effect on 2g12 recognition and capture of the virus treated with azido-compounds and irradiated with UV for 2 or 15 minutes compared to the untreated virus, hence no damage to its epitopes. Belanger2010 (binding affinity)
• 2G12: This review discusses recent research done to improve the production, quality, and cross-reactivity of binding Abs, neutralizing Abs, monoclonal Abs with broad neutralizing activity, antibody-dependent cell-mediated cytotoxicity (ADCC), antibody-dependent cell-mediated viral inhibition (ADCVI), and catalytic Abs. Studies focusing on several aspects of BNAb roles in vaccine development, and studies done to better understand the broad binding capacity of BNAbs are reviewed. Baum2010 (ADCC, neutralization, review)
• 2G12: Parent and GnTI (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps) viruses were equally sensitive to neutralization by 2G12, indicating that replacement of complex glycans does not affect the already exposed 2G12 epitope on the silent domain of the virus. Absence of the glycan at residue N301 (N301Q mutant virus) had no effect on 2G12 neutralization. Viruses subjected to removal of outer domain glycans by Endo H treatment were recognized less efficiently by 2G12. Binley2010 (glycosylation, neutralization)
• 2G12: Pseudoviruses containing Env mutations (V255E, S375N or A433T), which were in vitro selected with the small CD4-mimicking compound NBD-556, showed the same neutralization sensitivities as the wild type virus to 2G12. Yoshimura2010 (mimics, neutralization)
• 2G12: Neutralizing sensitivity of L669S mutant virus to 2G12 was not significantly different from the neutralizing sensitivity of the wild type virus. Shen2010 (neutralization)
• 2G12: Neutralization potency of 2G12 was compared to that of HK20 scFv in TZM-based assay using 45 Tier 1 and Tier 2 HIV isolates. 2G12 neutralized 12/45 isolates. In addition, 2G12 was used in TriMab, together with 2F5 and b12, to examine neutralization of 9 clade A, B, C, D and E isolates in PBMC assay. Here, TriMab neutralized 7 isolates with 2 not determined. Sabin2010 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: Using a humanized mouse model it was shown that passively transferred 2G12 dimer was more potent than 2G12 monomer at preventing CD4 T cell loss and suppressing increase in viral load in mice challenged with JR-CSF virus. 100µg/ml of combined 2G12 monomer and dimer significantly reduced the severity of HIV-1 infection in mice with high-dose challenge, but this 2G12 dose resulted in escape mutations at the N295 residue. Providing 2G12 dimers continuously at 5-25µg/ml by IgG tumor backpacks in mice resulted in effective protection against HIV-1, while complete escape to 2G12 neutralization was not observed. Luo2010 (immunoprophylaxis, neutralization, escape, immunotherapy)
• 2G12: B cell depletion in an HIV-1 infected patient using rituximab led to a decline in NAb titers and rising viral load. Recovery of NAb titers resulted in control of viral load, and the newly emerged virus population was examined. The common ancestor of this new viral population showed evidence of positive selection and presence of N339E mutation, which inhibited neutralization by 2G12 fourfold. However, there was no binding competition between patient sera and 2G12. Huang2010 (antibody interactions, escape)
• 2G12: The role of several N-glycosylation sites in 2G12 binding and neutralization was investigated on Envs of LN40 and B33 strains. Glycans at N295, N332, N386 and N392 were critical for 2G12 binding and neutralization. Substitutions in Envs which affect CD4 binding were also shown to have a strong effect on 2G12 neutralization. These residues were within and proximal to CD4bs but not involved in glycosylation. Increased avidity to CD4 did not correlate with 2G12 sensitivity, indicating that the determinants within CD4bs may act to reorient glycans on gp120. Duenas-Decamp2010 (antibody binding site, glycosylation, neutralization, kinetics, binding affinity)
• 2G12: Unlike for b12, decreasing neutralization sensitivity during the course of infection was not observed for 2G12 in 15 patients studied. Changes in three amino acid residues (154, 178 and 389) were found to confer resistance to b12, but they did not increase resistance of LAI strain to 2G12 neutralization. Bunnik2010 (neutralization)
• 2G12: Fusion of CD4 with 2G12 scFv resulted in CD4-scFv2G12 reagent with neutralization potency improved by inclusion of an IgG Fc region and by linkage of CD4 to the heavy chain of 2G12. The resulting CD4hc-IgG12G12 was, like 2G12, expressed as a mixture of monomers and dimers. CD4hc-IgG12G12 dimers showed comparable neutralization potencies with 2G12, and CD4hc-IgG12G12 monomers showed enhanced neutralization potencies. Unlike 2G12, CD4hc-IgG12G12 had the ability to neutralize some clade C HIV-1 strains. West2010 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: The specificities and structural analyses of 2G12 binding to Env are reviewed. This review also summarizes data on the evolution of HIV neutralizing Abs, principles of Env immunogen design to elicit broadly neutralizing Abs, and future critical areas of research for development of an Ab-based HIV vaccine. Hoxie2010 (vaccine antigen design, review)
• 2G12: Three 2G12 heavy chain mutants with multiple germ line amino acid substitutions in the VDJ region were created to investigate the mechanism of domain swapping in 2G12. There were qualitative structural differences between 2G12 mutants and 2G12 wild type, and the mutants failed to neutralize or to capture free virus. Structural analyses revealed that the domain-exchanged configuration of 2G12 was fostered by single or combined effects of 4 amino acid side chains that help stabilize the elbow region (H113). The proline at H113 was not required for the domain swapping capability of 2G12. 2G12-3H6 mutant, which had the whole Vh region exchanged with that of another Ab (3H6), lacked domain swapping capability, indicating that CDR3 and J region are not sufficient to promote Vh domain exchange. Gach2010 (neutralization, binding affinity, structure)
• 2G12: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 2G12 neutralization activity was compared to the three new broadly neutralizing mAbs. 2G12 did not compete for binding to gp120 with any of the new mAbs. 2G12 neutralized 67% of Tier 1 and 23% of Tier 2 viruses, the neutralization of Tier 2 viruses being inferior to that of the new MAb HJ16. 2G12 rarely neutralized clade C isolates. Corti2010 (neutralization)
• 2G12: 433 Abs were cloned from HIV envelope-binding memory B cells from 6 patients with broadly neutralizing sera. The Abs had neutralizing activity directed against several epitopes on gp120 and the majority neutralized Tier 1 viruses. Tier-2 neutralization was observed only with mixtures of MAbs, but only at high concentrations. 2G12 was used as a control and it neutralized 4/5 Tier 1 and 4/5 Tier 2 viruses. Scheid2009 (neutralization)
• 2G12: Exogenous epitope tags were introduced in different parts of three variable regions, V1, V2 and V4, of two HIV isolates, SF162 and SF33. Almost all SF162 and SF33 tagged Envs were as susceptible to neutralization by 2G12 as the wild type, except V4-tagged Envs, which were significantly more resistant to neutralization by this Ab compared to wild type. However, V4-tagged Envs were recognized by 2G12. Wallace2009 (antibody binding site, neutralization)
• 2G12: This review discusses obstacles to elicitation of protective NAbs, recent data on viral epitopes vulnerable to broadly NAbs, qualitative and quantitative implications of NAb response for vaccine development, and possible future areas of investigation to improve understanding of Env structure and stimulation of appropriate B cell responses. Stamatatos2009 (review)
• 2G12: The structure and dynamic of the virion spike and the 2G12 epitope are discussed. Challenges to eliciting broadly neutralizing anticarbohydrate response, such as weak protein-carbohydrate interactions and small size of glycan patches for Ab binding, are reviewed. 2G12 domain swapping solution to these problems and the implication of the data for immunogen design are discussed. Schief2009 (antibody binding site, review)
• 2G12: TZM-bl and PBMC systems were compared to investigate the influence of target cell environment on HIV entry inhibition. The sensitivity of TZM-bl system was confirmed by inhibitory capacity of 2G12, 2F5 and b12. Virus entry increased on addition of polycation additives, but neither concentration nor type of polycation had a significant impact on the inhibitory activity of 2G12. 2G12 was shown to be significantly less active on TZM-bl cells, where it failed to inhibit 12 viruses, while it failed to inhibit 9 viruses in PBMC assay. HIV isolates were less sensitive to inhibition by 2G12, 2F5 and 4E10, with up to 100-fold lower sensitivity in the TZM-bl assay. Rusert2009 (assay or method development, neutralization)
• 2G12: To examine the antigenicity of a defined Ab epitope on the functional envelope spike, a panel of chimeric viruses engrafted at different positions with the hemagglutinin (HA) epitope tag was constructed. The neutralization sensitivity of the all but three HA-tagged viruses to 2G12 was similar to the neutralization sensitivity of wild type virus to this Ab. The three viruses with HA-tag insertions in the V4 region were more resistant to 2G12 than the wild type virus. Pantophlet2009 (neutralization)
• 2G12: This review summarizes targets of autologous neutralizing Abs (AnAbs) in early and chronic infections. V1V2 is a frequent target of AnAbs, while V4 and V5 have marginal role and anti-V3 Abs do not contribute to autologous neutralization. In addition to variable regions, C3 is a neutralization target in subtype C viruses, and is thought to interact with V4. gp41 is thought to have marginal effect as a target of AnAbs, with only one study showing 4E10-resistant variants suggesting escape from AnAbs targeting this region. AnAb specificities and sequential development, and their role in preventing superinfection is also reviewed. The relatively high Ab titer required for prevention of superinfection and control of viremia, and the low inhibitory potential of b12, 2F5, 4E10 and 2G12 compared to antiretroviral drugs is discussed. Moore2009 (autologous responses, review)
• 2G12: This review describes obstacles that have been encountered in the development of an HIV-1 vaccine that induces broadly neutralizing Abs, and unusual features of existing broadly neutralizing Abs, such as 2G12. Importance of identification and characterization of new epitopes, and of B-cell stimulation, is discussed. Montefiori2009 (review)
• 2G12: An overview of the different expression strategies to over produce HIV neutralizing Abs, including 2G12, in plants. The attention is specially focused on expression strategies of Nef protein. Marusic2009 (review)
• 2G12: Env clones of 6 out of 12 viruses were shown to be highly sensitive to neutralization by 2G12 in PBMC assay but were not inhibited by 2G12 in TZM-bl assay. All 6 envelopes carried a mutation in the core epitope of 2G12. Viruses from patients receiving passive immunization with 2G12 were sensitive to 2G12 both in vivo and in PBMC assay. Upon emergence of 2G12 resistant viruses in vivo, the viruses were shown resistant to neutralization by 2G12 in PBMC assay. The study suggests that TZM-bl assay can fail to detect neutralizing activity of in vivo relevance but may be more prone to detect epitope mismatches. Causes of the observed differences between the PBMC and TZM-bl assays were due to virus producer cells and target cells, that could influence virus entry inhibition. Mann2009 (assay or method development, neutralization)
• 2G12: NAb specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. The integrity and specificity of gp120 beads in adsorption assay were validated by their ability to adsorb binding activity of 2G12. gp120 point mutation D368R was used to screen the sera for CD4bs- Abs, and it was shown that this mutant could adsorb binding activity of 2G12. To test for presence of coreceptor binding region MAbs in sera, gp120 I420 mutant was used. This mutant was recognized by 2G12 at equal levels as the wild type, and it could adsorb binding activity of 2G12 in adsorption assay. In some of the broadly neutralizing sera, the gp120-directed neutralization was mapped to CD4bs. Some sera were positive for NAbs against coreceptor binding region. A subset of sera also contained NAbs directed against MPER. Li2009c (assay or method development)
• 2G12: 2G12 domain swapping mode of epitope recognition is reviewed in detail. The review also summarizes on how different modes of Ab binding and recognition are used to overcome viral evasion tactics and how this knowledge may be used to re-elicit responses in vivo. Kwong2009a (antibody binding site, review)
• 2G12: The review discusses the implications of HIV-1 diversity on vaccine design and induction of neutralizing Abs, and possible novel approaches for rational vaccine design that can enhance coverage of HIV diversity. Patterns of within-clade and between-clade diversity in core epitopes of known potent neutralizing Abs, including 2G12, is displayed. Korber2009 (review)
• 2G12: 2G12 alone was not able to trigger complement-mediated lysis (CML) of 93BR020 and 92UG037 strains, however, it did so in combination with 4E10. Lysis experiments of viruses from three donors showed that 2G12 in combination with allotype-specific Abs Cw4 or Cw7 significantly increased CML. 2G12 in combination with Abs against HLA A1 resulted in significant reduction in CML. Hildgartner2009 (complement)
• 2G12: The effect of continuous 2G12 infusion on protection from infection and on viral load is reviewed. Haigwood2009 (immunoprophylaxis, review)
• 2G12: FcγR-mediated inhibition and neutralization of HIV by 2G12 and other MAbs is reviewed. The review also summarizes the role of ADCC and ADCVI Abs on HIV infection inhibition and neutralization. Forthal2009 (review)
• 2G12: A set of Env variants with deletions in V1/V2 were constructed. Replication competent Env variants with V1/V2 deletions were obtained using virus evolution of V1/V2 deleted variants. Most variants were found more sensitive to neutralization by 2G12 than the wild type, indicating that deletion of V1/V2 increases 2G12 epitope accessibility. Bontjer2009 (antibody binding site, neutralization)
• 2G12: This review summarizes novel approaches to mapping broad neutralizing activities in sera and novel technologies for targeted MAb retrieval. Binley2009 (assay or method development, review)
• 2G12: Resurfaced stabilized core 3 (RSC3) protein was designed to preserve the antigenic structure of the gp120 CD4bs neutralizing surface but eliminate other antigenic regions of HIV-1. RSC3 retained strong reactivity with 2G12. Memory B cells were selected that bound to RSC3 and full IgG mAbs were expressed. Binding profiles of the three newly detected mAbs (VRC1, VRC2 and VRC3) were compared to binding profile of 2G12. Wu2010 (binding affinity)
• 2G12: Glycosylation patterns of HIV-1 were altered using different glycosidase inhibitors or a mutant cell line. Recombinant production of gp120 in the presence of kifunensine resulted in increased neutralization by 2G12, while swainsonine and NB-DNJ treatment resulted in neutralization similar to the wild type. Doores2010 (glycosylation, neutralization)
• 2G12: In 25% of cases, the broad and potent neutralizing activity of sera from elite neutralizers displayed critical correlation to the N-linked glycosylation at position 332 of HIV-1. Although this N-linked glycan is important for formation of the 2G12 epitope, none of the donor sera inhibited 2G12 binding to gp120, indicating presence of NAbs distinct of 2G12. Unlike PG9 and PG16, 2G12 neutralized kifunensine-treated pseudoviruses with similar potency as wild type pseudoviruses. Walker2010 (glycosylation, neutralization, binding affinity)
• 2G12: Ab gene divergence analyses found that 2G12 Ab was significantly more divergent from the closest germline Abs than were hmAbs against other viruses. Germline-like 2G12 was constructed in a scFv format. It was shown that germline-like 2G12 did not bind to recombinant gp140 although the corresponding mature 2G12 showed binding. Xiao2009 (binding affinity, antibody sequence)
• 2G12: Patient sera from 13 HIV controllers and 75 chronic viremic patients were tested for the ability to block binding of 2G12 to Env JRFL gp140 oligomers. There was no difference observed between the controllers and chronic viremic patients. The NAb response was significantly lower in controllers, while ADCC was detected in all controllers but in only 40% of viremic patients. Lambotte2009 (elite controllers, neutralization)
• 2G12: One functional Env clone from each of 10 HIV-1 infected seroconverting individuals from India were analyzed for their sensitivity to MAbs and plasma pools of subtypes B, C and D. All 10 Envs were resistant to 2G12, and the resistance was associated with the absence of a PNLG at position 295. HIVIG neutralized all 10 Envs, and the Envs were most sensitive to neutralization by subtype C pool, followed by subtype D and B pools, respectively. Amino acid signature patterns that associated with neutralization clusters were found. Signature patterns included PNLG at positions 295, 392 and 448, which participate in the 2G12 epitope. Kulkarni2009 (glycosylation, neutralization, acute/early infection)
• 2G12: Combinations of loop alternations, filling hydrophobic pockets (F-mutations) and introduction of inter-domain cysteine pairs (D-mutations) were used to construct four immunogens with stabilized gp120 core. Modified truncations of the V1V2 and the V3 loop had no impact on 2G12 binding. However, introduction of stabilizing F and D mutations in one case slightly reduced 2G12 affinity and in other two cases slightly increased it. Dey2009 (binding affinity)
• 2G12: A review about the in vivo efficacy of 2G12 and other MAbs against HIV-1, and about inhibition of HIV-1 infection by Ab fragments Fab, scFv and engineered human Ab variable domains or "domain antibodies" (dAbs). Chen2009b (neutralization, immunotherapy, review)
• 2G12: Env derivatives from R3A TA1 virus with eliminated V1 and V2 regions, truncated V3, and deleted cleavage, fusion, and interhelical domains were able to bind 2G12. A membrane anchored variant of this outer domain glycoprotein was also shown to bind to 2G12. Truncations of the β20-β21 hairpin increased reactivity with 2G12. Replacement of the central 20 amino acids of the V3 loop with a basic hexapeptide further significantly increased binding to 2G12. Wu2009a (binding affinity)
• 2G12: During purification of 2G12 from mammalian cells, two forms of 2G12 were discovered, a monomeric and a dimeric form. The 2G12 dimer had an average increased potency of 82-fold compared to the monomer and was able to neutralize three out of 20 strains not neutralized by the monomer. Clade C strains were resistant to neutralization by both 2G12 dimer and monomer. A dimeric form of 2G12 was constructed that was more potent in neutralization of 2G12-sensitive strains than the monomeric form. There was no significant difference observed in binding of 2G12 dimers and monomers to gp120. West2009 (neutralization, kinetics, binding affinity)
• 2G12: 2G12 neutralization breadth and potency was compared to that of two broadly neutralizing Abs PG9 and PG16 in a panel of 162 multi-clade viruses. 2G12 exhibited lower neutralization potency than PG9 and PG16. 2G12 bound with high affinity to both monomeric gp120 and trimeric Env. Binding of 2G12 to Endo H and mock treated gp120 was determined. Walker2009a (neutralization, variant cross-reactivity, binding affinity)
• 2G12: NL4.3 virus was cultured with cyclotriazadisulfonamide (CADA) and CADA-resistant virus was selected. 2G12 MAb showed a slightly higher neutralizing potency against the CADA-resistant virus compared to wildtype. The mutations in CADA-resistant virus are suggested to stabilize the conformation of gp120 and reduce glycosylation. Vermeire2009 (neutralization)
• 2G12: Glyco-engineered tobacco plants were used for efficient expression of recombinant 2G12 with quantitative β1,4-galactosylation (AA structure). Antigen binding capacity of 2G12 glycoforms compared to CHO-derived 2G12 was 115-140%. Neutralization activity of fully galactosylated 2G12 was more than 3 times higher than that of other plant-derived glycoforms and CHO-derived 2G12. Strasser2009 (neutralization, binding affinity)
• 2G12: An analytical selection algorithm and a reduced virus screening panel were created for assessment of serum neutralizing activity. It is suggested that selection of pseudoviruses for neutralization assays should focus on the overall resistance profile of the pseudovirus and against MAbs b12, 4E10, 2F5 and 2G12. Neutralization profiles of all viruses used for screenings were determined for 2G12. Simek2009 (neutralization)
• 2G12: Substantial increase in neutralization potency (58-fold) of 2G12 was observed in cells expressing FcγRI against HIV 6535.3 virus strain while there was no effect on the neutralization potency of this Ab against QH0692 strain. With virus SC422661.8, FcγRIIa and FcγRIIb impaired the neutralizing activity of 2G12, suggesting possible infection enhancement. Perez2009 (enhancing activity, neutralization)
• 2G12: Aqueous two-phase partition system (ATPS) was used to successfully separate 2G12 from unclarified tobacco extract with a yield of 85%. ATPS was successfully combined with affinity chromatography and yielded Ab was stable without any major contaminating proteins or degraded Ab variants. Platis2009a (assay or method development)
• 2G12: Δ49-12a, a mutant virus derived from an in-vitro passaged virus with four residues removed from the V3 stem, was shown to be completely resistant to CCR5 inhibitors but was 3-fold more sensitive to neutralization by 2G12 compared to the parental R3A virus. TA1, a mutant with a 15 amino acid deletion of the distal half of V3, was resistant to neutralization by 2G12. Nolan2009 (neutralization)
• 2G12: Swarm analysis of viruses from one patient resulted in isolation of several different clones with different neutralization sensitivities against four HIV-1 positive sera. None of the clones were sensitive to neutralization by 2G12. ORourke2009 (neutralization, acute/early infection)
• 2G12: Binding of 2G12 to gp120 was not inhibited by YZ23, an Ab derived from mice immunized with eletcrophilic analogs of gp120 (E-gp120), indicating no overlap of these MAb epitopes. Nishiyama2009
• 2G12: Binding of 2G12 to various lipid antigens was studied. 2G12 did not bind to any lipids. Matyas2009
• 2G12: There was no association between 2G12 Abs and anticardiolipin in serum samples from slow progressors. Martinez2009 (autoantibody or autoimmunity)
• 2G12: By manipulation of the glycosylation machinery of S. cerevisiae a heavily glycosylated yeast protein, Pst1, was identified, that presents closely arrayed N-glycans. Pst1 produced in TM yeast bound 2G12 with high affinity and was able to inhibit 2G12 binding to gp120 more efficiently than a heterologous gp120 from the same subtype. Pst1 was also able to inhibit 2G12 neutralization of HxB and SF162 Env. Luallen2009 (antibody binding site, glycosylation, neutralization, kinetics, binding affinity)
• 2G12: Subtype A gp140 SOSIP trimers bound to 2G12. Sera from rabbits immunized with SOSIP gp140 and gp120 were unable to capture pseudovirions of the homologous virus by 2G12. 2G12 was unable to bind to the 295 N/A mutant of the virus. Kang2009
• 2G12: Five rhesus macaques were intravenously treated with 40mg/kg 2G12, which resulted in a high 2G12 serum concentration, and challenged with SHIV SF162P3. Three animals were protected against infection. One animal showed delayed and lower peak viremia compared to controls. Sequence analysis of one of the infected animals showed presence of T388A mutation disrupting the N-glycosylation consistent with escape. Thus, 2G12 can offer protection at relatively low titers, where a titer of 1:1 was sufficient to protect 60% of animals against infection. Vaginal concentrations of 2G12 and b12 were similar when compared in 3 animals, and thus unlikely to contribute to protection differences between the two MAbs. Hessell2009 (glycosylation, neutralization, escape, immunotherapy, rate of progression)
• 2G12: Ten new non-neutralizing, cross-reactive mAbs were found in immunized mice. 2G12 only reacted with a subset of different Env subtypes tested. 2G12 also reacted with cells expressing A1.con, B.con, B_17779 and B_MN Envs. None of the new mAbs could bind free virus particles while 2G12 did. Binding of 2G12 to B_JRFL oligomer was not blocked by any of the newly detected mAbs. Gao2009 (variant cross-reactivity)
• 2G12: The heavy and light chains of 2G12 were expressed in transgenic tobacco plants. The accumulation of the Ab chains was increased 2-3-fold by elastin-like peptide (ELP) fusion in both leaves and seeds of the plant. The quality of leaf-derived Abs was comparable to 2G12 generated in CHO cells, and the presence of ELP did not affect N-glycan processing nor intracellular trafficking. Plant-derived 2G12 lacking ELP was more efficient in neutralizing HIV-1 than CHO-2G12, but the fusion of ELP to either of the Ab chains significantly reduced the neutralization efficacy. Floss2009 (neutralization, kinetics, binding affinity)
• 2G12: An international collaboration (NeutNet) was organized to compare the performance of a wide variety of HIV-1 neutralization assays performed in different laboratories. Four neutralizing agents were evaluated: 4E10, 447-52D, sCD4 and TriMab (equal mixture of 2F5, 2G12 and 4E10). For TriMab, the mean IC50 values were always lower in the pseudovirus assays than in virus infectivity assays. In general, there were clear differences in assay sensitivities that were dependent on both the neutralizing agent and the virus. No single assay was capable of detecting the entire spectrum of neutralizing activities. Fenyo2009 (assay or method development, neutralization)
• 2G12: Gene encoding gp140 was fused with three trimerization motifs, T4F, GCN and ATC. gp140, gp140(-)(with mutations in the furin-cleavage site), gp140(-)T4F and gp140(-)GCN bound 2G12 as well, or better than, gp120. gp140(-)ATC bound 2G12 less strongly than gp120. Du2009 (binding affinity)
• 2G12: Four groups of Abs were detected in a CRF02_AG infected patient directed against mimotopes of MPER, V3, C1 and LLP2. Out of four pseudoviruses from 4 different time points of infection, only one showed moderate susceptibility to 2G12. Dieltjens2009 (neutralization)
• 2G12: A phylogenetic analysis of gp120 evolution was performed in patients with different patterns of disease progression. In the LNTP patient group, and in 2 NPs, many N-linked glycosylation sites were shown to be under positive selection and exposed on the surface, indicating that Abs binding close to or to 2G12 binding site exert selective pressure on the viral surface in some patients. Canducci2009 (glycosylation, rate of progression)
• 2G12: Neutralization profiles of cloned Envs derived from recent heterosexual infections by subtypes A, C, D, and A/D from Kenya were determined. The transmitted env variants were generally resistant to neutralization by 2G12, as only 4/31 variants were neutralized by this Ab. These were also the only variants that maintained all five PNGS within the 2G12 epitope. Blish2009 (neutralization, acute/early infection)
• 2G12: This report investigated whether mannose removal alters gp120 immunogenicity in mice. Approximately 55 mannose residues were removed from gp120 by mannosidase digestion creating D-gp120 for immunization. 2G12 was unable to bind to D-gp120, indicating that 2G12 epitope was eliminated and that the mannosidase digestion was functional. Banerjee2009 (glycosylation, binding affinity)
• 2G12: HIV-1 variants derived from 5 patients at different timepoints during chronic infection were analysed for their sensitivity to neutralization by b12, 2G12, 2F5 and 4E10. In four of the patients, almost all variants from all time points were resistant to neutralization by 2G12. In two of these patients, resistance to neutralization coincided with the absence of N-linked glycans at position 339 at all time points. In one patient, resistance to neutralization by 2G12 correlated with absence of N-linked glycans at positions 295, 332 and/or 339, and in the second patient, resistance correlated with absence of glycans at positions 295, 339, 386, and/or 339. In the fifth patient, early viruses were sensitive to neutralization by 2G12, but late variants were resistant, which coincided with the loss of N-linked glycans at either 386 or 392 positions. Bunnik2009 (glycosylation, neutralization, escape)
• 2G12: 2G12 neutralized infection of PBLs with various HIV-1 strains with high potency. However, 2G12 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including 2G12, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs. Chomont2008 (neutralization)
• 2G12: 5 loop structures surrounding the CD4 binding site in the gp120 liganded conformation were identified that may protect gp120 from Abs. Loops A, B, C and E were located in the C2, C3, C4 and C5 regions respectively, and loop D was situated in the V5 region. Binding of 2G12 to gp120 was unaffected by loop deletions, as this Ab bound equally to HIV-1 IIIB wild type and its loop B deletion mutant, and to HIV-1 89.6 wild type and its loop C deletion mutant. Berkower2008 (binding affinity)
• 2G12: A reference panel of recently transmitted Tier 2 HIV-1 subtype B envelope viruses was developed representing a broad spectrum of genetic diversity and neutralization sensitivity. The panel includes viruses derived from male-to-male, female-to-male, and male-to-female sexual transmissions, and CCR5 as well as CXCR4 using viruses. The envelopes displayed varying degrees of neutralization sensitivity to 2G12, with 11 of 19 envelopes sensitive to neutralization by this Ab. Schweighardt2007 (assay or method development, neutralization)
• 2G12: Pre-treatment of gp120 with 2G12 strongly inhibited induction of IL-10, indicating that interaction between gp120 and a mannose C-type lectin receptor is a critical trigger for IL-10 induction. Shan2007
• 2G12: Modeling of protein-protein interaction based on the gp120 crystal structure, X-ray crystal structure of 2G12 and its complexes with glycans, suggested that the glycans attached to N295 and N302 from the V3 loop are the two most likely involved in the conformational epitope of 2G12. Sirois2007 (review, structure)
• 2G12: A chimeric protein entry inhibitor, L5, was designed consisting of an allosteric peptide inhibitor 12p1 and a carbohydrate-binding protein cyanovirin (CNV) connected via a flexible linker. The L5 chimera inhibited 2G12-gp120 interaction, as did CNV alone, indicating that the chimera has the high affinity binding property of the CNV molecule. McFadden2007
• 2G12: This review summarizes data on possible vaccine targets for elicitation of neutralizing Abs and discusses whether it is more practical to design a clade-specific than a clade-generic HIV-1 vaccine. Development of a neutralizing Ab response in HIV-1 infected individuals is reviewed, including data that show no apparent division of different HIV-1 subtypes into clade-related neutralization groups. Also, a summary of the neutralizing activity of MAb 2G12 in different HIV-1 clades is provided. McKnight2007 (variant cross-reactivity, review)
• 2G12: HIV-1 passaged in the presence of chloroquine was observed to have lost two glycosylation sites important for 2G12 binding, at positions 332 and 397 in the gp120 region, indicating that the drug can alter the immunogenic properties of gp120. Naarding2007
• 2G12: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 2G12 structure and binding to HIV-1 envelope and current strategies to develop versions of the Env spike with functional trimer properties for elicitation of broadly neutralizing Abs, such as 2G12, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed. Phogat2007 (review)
• 2G12: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including 2G12 MAb, in vivo and in vitro activity of neutralizing Abs, the importance and downfalls of non-neutralizing Abs and antibodies that mediate antibody-dependent cellular cytotoxicity and the complement system, and summarizes data on areas that need future investigation on Ab-mediated immune control. Huber2007 (review)
• 2G12: A new high throughput method was developed for neutralization analyses of HIV-1 env genes by adding cytomegalovirus (CMV) immediate enhancer/promoter to the 5' end of the HIV-1 rev/env gene PCR products. The PCR method eliminates cloning, transformation, and plasmid DNA preparation steps in the generation of HIV-1 pseudovirions and allows for sufficient amounts of pseudovirions to be obtained for a large number of neutralization assays. Pseudovirions generated with the PCR method showed similar sensitivity to 2G12 Ab, indicating that the neutralization properties are not altered by the new method. Kirchherr2007 (assay or method development, neutralization)
• 2G12: 2G12 structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit 2G12-like Abs, are reviewed in detail. Lin2007 (vaccine antigen design, review, structure)
• 2G12: This review summarizes 2G12Ab epitope, properties and neutralization activity. 2G12 use in passive immunization studies in primates and possible mechanisms explaining protection against infection are discussed. Kramer2007 (immunotherapy, review)
• 2G12: gp120 proteins were developed with double mutation T257S+S375W, which alters the cavity at the epicenter of the CD4 binding region, and used to immunize rabbits. The ability of rabbit sera to affect binding of CD4 to unmodified gp120 proteins was tested. CD4 binding to gp120 was unaffected by 2G12. Dey2007a (antibody binding site)
• 2G12: The various effects that neutralizing and non-neutralizing anti-envelope Abs have on HIV infection are reviewed, such as Ab-mediated complement activation and Fc-receptor mediated activities, that both can, through various mechanisms, increase and decrease the infectivity of the virus. The importance of these mechanisms in vaccine design is discussed. The unusual features of the 2G12 MAb, and its neutralization capacities, are described. Willey2008 (neutralization, review)
• 2G12: Current insights into CTLs and NAbs, and their possible protective mechanisms against establishment of persistent HIV/SIV infection are discussed. Pre- and post-infection sterile and non-sterile protection of NAbs against viral challenge, and potential role of NAbs in antibody-mediated antigen presentation in modification of cellular immunity, are reviewed. Use of 2G12 in immunization experiments and its in vivo anti-viral activity in suppression of viral rebound in HIV-1 infected humans undergoing structured treatment interruptions are described. Yamamoto2008 (immunotherapy, supervised treatment interruptions (STI), review)
• 2G12: A yeast strain was produced (TM) with a deletion of genes encoding two key carbohydrate processing enzymes, Och1 and Mnn1, that resulted in efficient recognition of the TM yeast by 2G12 MAb. Four heavily glycosylated yeast proteins were isolated that supported 2G12 binding. Removal of high-mannose-type N-linked carbohydrates from the proteins resulted in loss of 2G12 recognition. Sera from rabbits immunized with TM yeast cells contained Abs that could cross-react with HIV-1 gp120 and that recognized a variety of clade B, C and SIV gp120 proteins. Like 2G12, binding of these Abs to Env proteins was abrogated by removal of N-linked high mannose glycans. The elicited Abs had 50-100-fold lower gp120 binding activity than 2G12, and the antiserum recognized a larger variety of mannose-dependent epitopes. There was no observed neutralizing activity of the sera. The results indicate that immunizations with TM yeast can elicit 2G12-like Abs. Luallen2008 (vaccine antigen design)
• 2G12: A mathematical model was developed and used to derive transmitted or founder Env sequences from individuals with acute HIV-1 subtype B infection. All of the transmitted or early founder Envs were sensitive to neutralization by 2G12. Keele2008 (neutralization, acute/early infection)
• 2G12: This review summarizes the obstacles that stand in the way of making a successful preventive HIV-1 vaccine, such as masked or transiently expressed Ab epitopes, polyclonal B-cell class switching, and inefficient, late, and not sufficiently robust mucosal IgA and IgG responses. Possible reasons why HIV-1 envelope constructs expressing 2G12 epitope fail to induce broadly neutralizing Abs are discussed. Haynes2008 (vaccine antigen design, review)
• 2G12: Transmission of HIV-1 by immature and mature DCs to CD4+ T lymphocytes was significantly higher for CXCR4- than for CCR5-tropic strains. In addition, preneutralization of X4 virus with 2G12 prior to capture efficiently blocked transmission to 36%, while transmission of R5 was blocked to 63%, indicating that 2G12 treatment results in more efficient transfer of X4 than of R5 HIV-1. vanMontfort2008 (co-receptor, neutralization, dendritic cells)
• 2G12: 2G12 did not neutralize a clade C SHIV strain in the TZM-bl based assay. Zhang2008 (neutralization)
• 2G12: Sera from both gp120 DNA prime-protein boost immunized rabbits and from protein-only immunized rabbits did not compete for binding to 2G12, indicating no elicitation of 2G12-like Abs by either of the immunization regimens. Vaine2008 (vaccine antigen design)
• 2G12: An R5 HIV variant, in contrast to its parental virus, was shown to infect T-cell lines expressing low levels of cell surface CCR5 and to infect cells in the absence of CD4. The variant was neutralized less efficiently by 2G12 than the parental virus, indicating conformational changes in gp120. These properties of the mutant virus were determined by alternations in gp41. Taylor2008 (co-receptor, neutralization)
• 2G12: In order to assess whether small molecule CCR5 inhibitor resistant viruses were more sensitive to neutralization by NAbs, two escape mutant viruses, CC101.19 and D1/85.16, were tested for their sensitivity to neutralization by 2G12, compared to the sensitivity of CC1/85 parental isolate and the CCcon.19 control isolate. The CC101.19 escape mutant has 4 sequence changes in V3 while the D1/85.16 has no sequence changes in V3 and relies on other sequence changes for its resistance. D1/85.16, but not CC101.19 escape variant, was markedly more sensitive to neutralization by 2G12 (approx. 50-fold). As 2G12 had no significantly higher affinity for gp120 from D1/85.16, the increased sensitivity of this virus is most likely due to alternation in the conformation or accessibility of the 2G12 epitope on its Env trimer. Overall, the study suggests that CCR5 inhibitor-resistant viruses are likely to be somewhat more sensitive to neutralization than their parental viruses. Pugach2008 (co-receptor, neutralization, escape, binding affinity)
• 2G12: The sensitivity of R5 envelopes derived from several patients and several tissue sites, including brain tissue, lymph nodes, blood, and semen, was tested against a range of inhibitors and Abs targeting CD4, CCR5, and various sites on the HIV envelope. All but one envelopes from brain tissue were macrophage-tropic while none of the envelopes from the lymph nodes were macrophage-tropic. Macrophage-tropic envelopes were also less frequent in blood and semen. There was a clear variation in sensitivity to 2G12, where most envelopes were sensitive, while some were resistant to neutralization by this Ab. There was a significant correlation between increased envelope macrophage-tropism and decreased 2G12 sensitivity. It is suggested that the macrophage-tropic brain variants are less protected by glycosylation due to absence of Abs in the brain, thus lacking N-glycosylation sites critical for 2G12 neutralization. Three of nine brain envelopes were resistant to 2G12, while only one of nine lymph node envelopes were resistant to 2G12. Peters2008a (antibody binding site, neutralization)
• 2G12: To examine sequence and conformational differences between subtypes B and C, several experiments were performed with 11 MAbs regarding binding and neutralization. Both binding and neutralization studies revealed that the 11 MAbs could be divided in three different groups, and that the most differences between the subtypes were located in the stem and turn regions of V3. 2G12 was used as control in neutralization assays, and was able to neutralize JR-FL and SF162 isolates, as well as a chimeric SF162 variant with a JR-FL-like V3 sequence. Patel2008 (neutralization)
• 2G12: Contemporaneous biological clones of HIV-1 were isolated from plasma of chronically infected patients and tested for their functional properties. The clones showed striking functional diversity both within and among patients, including differences in infectivity and sensitivity to inhibition by 2G12. There was no correlation between clonal virus infectivity and sensitivity to 2G12 inhibition, indicating that these properties are dissociable. The sensitivity to 2G12 inhibition was, however, a property shared by viruses from a given patient, suggesting that the genetic determinants that define this sensitivity may lie in regions that are not necessarily subject to extensive diversity. Nora2008 (neutralization)
• 2G12: A peptide 2G12.1, that binds to 2G12, was derived by screening of phage-displayed peptide libraries with 2G12. Comparison of the crystal structure of the Fab 2G12 bound to 2G12.1 peptide, and 2G12 bound to carbohydrate, revealed that 2G12 binding to peptide and carbohydrate occurs through different Ab interactions. The 2G12.1 peptide occupied a site different from, but adjacent to, the primary carbohydrate binding site on 2G12. Thus, this does not support structural mimicry of the peptide to the native carbohydrate epitope on gp120. In addition, the 2G12.1 peptide was not an immunogenic mimic of the 2G12 epitope either, since the sera from mice immunized with the peptide did not bind gp120. Menendez2008 (mimics, structure)
• 2G12: Maize was evaluated as a potential inexpensive large-scale production system for therapeutic antibodies against HIV. 2G12 was expressed in maize endosperm. In vitro cell assays demonstrated that the HIV-neutralizing properties of the maize-produced 2G12 MAb were equivalent to those of Chinese hamster ovary cell-derived MAb 2G12. Rademacher2008
• 2G12: Neutralization susceptibility of CRF01_AE Env-recombinant viruses, derived from blood samples of Thai HIV-1 infected patients in 2006, was tested to 2G12. Most of the 35 viruses tested replicated efficiently in the presence of 2G12, in spite of highly conserved PNLG sites recognized by this Ab, indicating that CRF01_AE is not susceptible to neutralization by 2G12. These results suggest that the protein structure , including conformation of the CD4 binding domain, may somehow be different between CRF01_AE and subtype B Env gp120. Utachee2009 (neutralization)
• 2G12: Concentrations of neutralizing Abs in long-term non-progressors (LNTPs) were significantly higher than the concentrations in asymptomatic subjects and subjects with AIDS, with no statistically significant difference between the two latter groups. Amino acid substitutions in the 2G12 epitope were found in both asymptomatic subjects and subjects with AIDS, while no such mutations were found among LNTPs. Eight different mutations were found at five N-glycosylation linked sites: 295V/T/D/K, 297I, 332E. 334N, and 386D. The mutation rates of the conserved 2G12 neutralization epitopes were significantly different among LNTPs, asymptomatic patients, and patients with AIDS. Wang2008 (escape, rate of progression)
• 2G12: Synergy of 2F5 with MAbs 2G12, D5, and peptide C34 was examined. 2G12 exhibited synergy in inhibition of HIV-1 89.6 with MAb 2F5. 2G12 was not as synergistic when combined with D5 as 2F5 was. Hrin2008 (antibody interactions)
• 2G12: A series of peptide conjugates were constructed via click reaction of both aryl and alkyl acetylenes with an internally incorporated azidoproline 6 derived from parent peptide RINNIPWSEAMM. Many of these conjugates exhibited increase in both affinity for gp120 and inhibition potencies at both the CD4 and coreceptor binding sites. None of the high affinity peptides inhibited the interactions of YU2 gp120 with 2G12 Ab. The aromatic, hydrophobic, and steric features in the residue 6 side-chain were found important for the increased affinity and inhibition of the high-affinity peptides. Gopi2008
• 2G12: Three constructs of the outer domain (OD) of gp120 of subtype C, fused with Fc, were generated for immunization of mice: OD(DL3)-Fc (has 29 residues from the center of the V3 loop removed), OD(2F5)-Fc (has the same deletion reconstructed to contain the sequence of 2F5 epitope), and the parental OD-Fc molecule. All OD variants contained substitutions at residues 295 and 394 that reintroduced the 2G12 epitope into the used sequence. All three OD-variants reacted with 2G12, indicating that the isolated outer domain is conformationally immobile. Despite the presence of the 2G12 epitope, none of the sera from mice immunized with the three OD-constructs showed 2G12-like reactivity. Chen2008a (vaccine antigen design)
• 2G12: The goal of the study was to measure NAb responses in patients infected with HIV-1 prevalent subtypes in China. g160 genes from plasma samples were used to establish a pseudovirus-based neutralization assay. 2G12 neutralized 33% of subtype B clones but not subtype BC and AE clones. Chong2008 (neutralization, subtype comparisons)
• 2G12: To investigate B-cell responses immediately following HIV-1 transmission, Env-specific Ab responses to autologous and consensus Envs in plasma donors were determined. Broadly neutralizing Abs with specificity similar to 2G12 did not appear during the first 40 days after plasma virus detection. Tomaras2008 (acute/early infection)
• 2G12: The neutralization profile of early R5, intermediate R5X4, and late X4 viruses from a rhesus macaque infected with SHIV-SF162P3N was assessed. 2G12 neutralized all three viruses with similar low potency. Tasca2008 (co-receptor, neutralization)
• C2G12: Neutralization of HIV-1 IIIB LAV isolate by 2G12 was within the same range as the neutralization of the virus by natural antibodies from human sera against the gal(α1,3)gal disaccaride linked to CD4 gp120-binding peptides, indicating that the activity of natural antibodies can be re-directed to neutralize HIV-1. Perdomo2008 (neutralization)
• 2G12: A new purification method was developed using a high affinity peptide mimicking CD4 as a ligand in affinity chromatography. This allowed the separation in one step of HIV envelope monomer from cell supernatant and capture of pre-purified trimer. Binding of 2G12 to gp120SF162 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the miniCD4 allows the separation of HIV-1 envelope with intact 2G12 epitope. gp140DF162ΔV2 was purified by the miniCD4 method to assess its ability to capture gp140 trimers. Binding of 2G12 to gp140DF162ΔV2 purified by the miniCD4 affinity chromatography and a multi-step method was comparable, suggesting that the SF162 trimer antigenicity was preserved. Martin2008 (assay or method development, binding affinity)
• 2G12: A divalent Man9ClcNAc2 glycopeptide, that binds to 2G12, was covalently coupled to the OMPC carrier and used as immunogen to test its efficacy to induce 2G12-like neutralizing Ab response. High levels of carbohydrate-specific Ab were induced in both guinea pigs and rhesus macaques, but these Ab showed poor recognition of recombinant gp160 and failed to neutralize a panel of subtype B isolates. Sera from HIV-1 positive individuals was tested for binding to the synthetic antigen but failed to recognize the mimetics, although two of the patients showed presence of 2G12-like Abs. These results suggest that presentation of Man9ClcNAc2 on the constrained cyclic scaffold is insufficient to induce a polyclonal response that recognizes native 2G12 epitope. Joyce2008 (mimotopes, neutralization, vaccine antigen design)
• 2G12: MAb 2G12 binds to gp120 and is essentially inactive after CD4 engagement, with a neutralization half-life of less than 1 minute. Thus, the binding site for 2G12 on gp120 is unavailable once the CD4-induced conformational changes in gp120 have occurred. Gustchina2008 (antibody binding site, neutralization, kinetics)
• 2G12: Variable domains of three heavy chain Abs, the VHH, were characterized. The Abs were isolated from llamas, who produce immunoglobulins devoid of light chains, immunized with HIV-1 CRF07_BC, to gp120. It was hypothesized that the small size of the VHH, in combination with their protruding CDR3 loops, and their preference for cleft recognition and binding into active sites, may allow for recognition of conserved motifs on gp120 that are occluded from conventional Abs. 2G12 provided some inhibition of binding of the three neutralizing VHH Abs to gp120, suggesting that 2G12 imposes steric hinderance to binding of the VHH Abs to gp120. Forsman2008 (antibody interactions)
• 2G12: 24 broadly neutralizing plasmas from HIV-1 subtype B and C infected individuals were investigated using a series of mapping methods to identify viral epitopes targeted by NAbs. In competitive virus capture assays on 2G12 coated plates, some of the subtype B plasmas, and two of the subtype C plasmas, inhibited virus capture. Mutant versions of JR-FL trimers were designed to selectively eliminate neutralization epitopes, but the plasma titers against the 2G12-eliminated mutant were similar to those against the wildtype. This indicated that very few, if any, 2G12-like Abs were present in the plasmas, and that a fraction of patients developed Abs that overlap the 2G12 epitope but do not neutralize the virus. Binley2008 (neutralization, binding affinity)
• 2G12: 32 human HIV-1 positive sera neutralized most viruses from clades A, B, and C. Two of the sera stood out as particularly potent and broadly reactive. Two CD4-binding site defective mutant Env proteins were generated to evaluate whether Abs to the CD4-binding site are involved in the neutralizing activity of the two sera. The integrity of the wildtype and mutant proteins was tested for their reactivity to 2G12. Li2007a (binding affinity)
• 2G12: A recombinant gp120-Fc bound to 2G12, indicating it was conformationally intact. 2G12 binding to gp120 was inhibited by the soluble recombinant extracellular domain (ECD) of DC-SIGN in a dose-dependent fashion, but 2G12 did not inhibit binding of gp120 to DC-SIGN. Many single, double, and triple N-glycan mutations in the 2G12 epitope did not affect binding of gp120 to DC-SIGN, however, some of the N-glycan sites within the 2G12 epitope were shown to be optimally positioned to significantly contribute to DC-SIGN binding. Thus, it is suggested that DC-SIGN can bind to a flexible combination of N-glycans on gp120, both within and outside of the 2G12 epitope, but that its optimal binding site overlaps with specific N-glycans within the 2G12 epitope. Hong2007 (binding affinity)
• 2G12: HIV-1 env clones resistant to cyanovirin (CV-N), a carbohydrate binding agent, showed amino acid changes that resulted in deglycosylation of high-mannose type residues in the C2-C4 region of gp120. Compared to their parental virus HIV-1 IIIB, these CV-N resistant viruses were also completely resistant to 2G12, as they lost one or more 2G12 binding glycans on gp120. Hu2007 (neutralization, escape)
• 2G12: Chemical inhibition of mammalian glycoprotein synthesis with the plant alkaloid kifunensine resulted in an abundance of oligomannose-type glycans on the cell surface, and binding of 2G12 to previously non-antigenic self proteins and cells. Expression of gp120 in the presence of kifunensine also increased both binding and valency of gp120 to 2G12. Scanlan2007 (antibody binding site, binding affinity)
• 2G12: The ability of 2G12 to neutralize recently transmitted viruses was examined in four homosexual and two parenteral transmission couples. The vast majority of recently transmitted viruses from homosexual recipients were resistant to neutralization by 2G12, although viruses isolated later in the course of infection showed increased sensitivity to 2G12 in one of the patients. In the parenteral transmission, one of the recipients had early viruses resistant to 2G12 neutralization, and one had viruses somewhat sensitive to 2G12 neutralization. The neutralization sensitivity patterns of recipient viruses to 2G12 did not correlate to the neutralization sensitivity patterns of their donors in the homosexual couples, while the HIV-1 variants from the one of the two parenteral pairs were similarly resistant to neutralization by 2G12. 12% of 2G12 resistant viruses had all five PNGS of the 2G12 epitope. 88.5% of the 2G12 resistant viruses lacked at least one of the five PNGS, and viruses isolated later in infection that had become sensitive to 2G12 neutralization had restored the 2G12 epitope. Quakkelaar2007a (neutralization, acute/early infection, mother-to-infant transmission)
• 2G12: Three MAbs, 2G12, 4E10 and 2F5, were administered to ten HIV-1 infected individuals treated with ART during acute and early infection, in order to prevent viral rebound after interruption of ART. MAb infusions were well tolerated with essentially no toxicity. Viral rebound was not prevented, but was significantly delayed in 8/10 patients. 2G12 activity was dominant among the MAbs used. Baseline susceptibility to 2G12 was inversely correlated with the time to viral rebound. Escape from 2G12 was associated with viral rebound. Long-term suppression of viremia was achieved in 3/10 patients. Mehandru2007 (escape, immunotherapy, supervised treatment interruptions (STI))
• 2G12: MBL, a lectin present in human serum that recognizes mannose-rich N-glycans, was shown to mediate increased HIV-1 infectivity, and to reduce 2G12-mediated neutralization of HIV-1. Marzi2007 (neutralization)
• 2G12: The study compared Ab neutralization against the JR-FL primary isolate and trimer binding affinities judged by native PAGE. There was direct quantitative relationship between monovalent Fab-trimer binding and neutralization, implying that neutralization begins as each trimer is occupied by one Ab. In BN-PAGE, neutralizing Fabs, 2G12 in particular, and sCD4 were able to shift JR-FL trimers. In contrast, most non-neutralizing Fabs bound to monomer, but their epitopes were conformationally occluded on trimers, confirming the exclusive relationship of trimer binding and neutralization. For 2G12, there was a ladder of partially and fully liganded trimers Crooks2008 (neutralization, binding affinity)
• 2G12: Five amino acids in the gp41 N-terminal region that promote gp140 trimerization (I535, Q543, S553, K567 and R588) were considered. Their influence on the function and antigenic properties of JR-FL Env expressed on the surfaces of pseudoviruses and Env-transfected cells was studied. Various non-neutralizing antibodies bind less strongly to the Env mutant, but neutralizing antibody binding is unaffected. There was no difference in 2G12 binding to wild type and mutant JR-FL, and 2G12 inhibited infection of the two pseudoviruses with comparable potencies. Dey2008 (binding affinity)
• 2G12: The study explores how the V1 loop of Env influences the neutralization susceptibilities of heterologous viruses to antibodies elicited by the SF162gp140 immunogen. All viruses expressing the WT Envs were susceptible to neutralization by 2G12. Replacement of the V1 loops by that of SF162 did not alter the neutralization susceptibilities of the viruses. Ching2008 (neutralization)
• 2G12: Molecular mechanism of neutralization by MPER antibodies, 2F5 and 4E10, was studied using preparations of trimeric HIV-1 Env protein in the prefusion, the prehairpin intermediate and postfusion conformations. MAb 2G12 was used to analyze antigenic properties of construct 92UG-gp140-Fd, derived from isolate 92UG037.8 and stabilized by a C-terminal foldon tag. 92UG-gp140-Fd binds 2G12 with high affinity. Frey2008 (binding affinity)
• 2G12: The study explores the development of a carbohydrate immunogen that could elicit 2G12-like neutralizing ABs to contribute to an AIDS vaccine. Specifically, the study describes the development of neoglycoconjugates displaying variable copy numbers of synthetic tetramannoside (Man(4) on bovine serum albumin (BSA) molecules by conjugation to Lys residues. Immunization of rabbits with BSA-(Man(4))(14) elicits significant serum Ab titers to Man(4). However, these Abs are unable to bind gp120. Astronomo2008 (vaccine antigen design)
• 2G12: Addition of a glycosylation site at position V295N in three different subtype C envelope clones (COT9.6, COT6.15 and Du151.2) resulted in increase in binding of 2G12. However, only one of the viral clones (COT9.6) became sensitive to neutralization by 2G12 at high Ab concentrations. Introduction of glycosylation site at position 448 in COT6.15 further increased its binding to 2G12 and resulted in viruses more sensitive to neutralization. Furthermore, addition of glycosylation at position 442 increased binding and neutralization sensitivity of the corresponding viruses to 2G12, and deletion of glycosylation at position 386 resulted in reduction in binding and resistance to neutralization by 2G12. Gray2007a (antibody binding site, neutralization, binding affinity, subtype comparisons)
• 2G12: A D386N change in the V4 region, which results in restoration of N-glycosylation at this site, did not have any impact on the neutralization of a mutant virus by 2G12 compared to wildtype. Also, there was no association between increased sensitivity to 2G12 neutralization and enhanced macrophage tropism. Dunfee2007 (antibody binding site)
• 2G12: This review summarizes data on the development of HIV-1 centralized genes (consensus and ancestral) for induction of neutralizing antibody responses. Functionality and conformation of native epitopes in proteins based on the centralized genes was tested and confirmed by binding to 2G12 and other MAbs. Antibodies induced by immunization with these centralized proteins did not, however, have the breadth and potency compared to that of 2G12 and other broadly neutralizing MAbs. Gao2007 (antibody binding site, neutralization, vaccine antigen design, review)
• 2G12: Macaques were immunized with either CD4, gp120, cross-linked gp120-human CD4 complex (gp120-CD4 XL), and with single chain complex containing gp120 rhesus macaque CD4 domains 1 and 2 (rhFLSC). Sera from the rhFLSC immunized animals showed slightly higher competition titers, being able to block gp120-CD4 complex interactions with 2G12 slightly more efficiently than sera from animals immunized with the three other proteins. DeVico2007 (neutralization)
• 2G12: 2G12-blocking activity was very low in all of the sera from guinea pigs immunized with gp120 protein, or with three types of VLPs: disulfide-shackled functional trimers (SOS-VLP), uncleaved nonfunctional Env (UNC-VLP), naked VLP bearing no Env. Crooks2007 (neutralization, vaccine antigen design)
• 2G12: Interactions of this Ab with gp120 monomer and two cleavage-defective gp140 trimers were studied. It was shown that 2G12 interactions with the soluble monomers and trimers were minimally affected by GA cross-linking of the proteins, indicating that the 2G12 epitope was maintained after cross-linking. This Ab was associated with a small entropy change upon gp120 binding. This Ab was shown to have a kinetic advantage as it bound to gp120 faster than other less neutralizing Abs. Yuan2006 (antibody binding site, antibody interactions, kinetics, binding affinity)
• 2G12: No significant levels of 2G12 were shown to bind to HA/gp41 expressed on cell surfaces and this Ab did not stain cells expressing HA/gp41 in a fluorescence assay. However, it did bind to HIV 89.6 Env expressing cells. Ye2006 (antibody binding site, binding affinity)
• 2G12: Viruses with wild-type HIV-1JR-FL Envs were neutralized by this Ab at much lower concentrations than HIV-1 YU2 Env viruses. Yang2006 (neutralization, binding affinity)
• 2G12: SHIV SF162p4 virus used as challenge in ISCOM vaccinated macaques was shown to be highly sensitive to neutralization by this Ab. Pahar2006 (neutralization)
• 2G12: All subtype C env-pseudotyped clones derived from individuals in acute/early stage of HIV-1 infection were highly resistant to neutralization by this Ab, since each of the clones lacked a PNLG at one or more critical epitope positions. The sensitivity of clones to a mix of Abs IgG1b12, 2G12 and 2F5 was tracked to IgG1b12. Li2006a (neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
• 2G12: This Ab was used as a control since its epitope is independent of either V1/V2 or V3 domains confirmed in its equal neutralization of SF162 and variants SF162(JR-FL V3), SF162(JR-FL V1/V2) and SF162(JR-FL V1/V2/V3). This Ab was also shown to neutralize viruses with V3 sequences from several different subtypes (B, F, A1, H, C, CRF02_AG and CRF01_AE). Krachmarov2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: Binding of 2G12 to wt gp120 and two constructs with 5 and 9 residues deleted in the middle of the beta3-beta5 loop in the C2 region of gp120 was examined. The deletions of the loop residues did not affect the conformation of 2G12 epitope as 2G12 Ab binding and kinetics were identical for the wt gp120 and both constructs. Rits-Volloch2006 (antibody binding site, kinetics, binding affinity)
• 2G12: This Ab was used as a positive control in the neutralization assay. At the highest Ab concentrations, 2G12 was able to neutralize several primary isolates but not all, with a neutralization pattern similar to that of rabbit sera immunized with monovalent and polyvalent DNA-prime/protein-boost Env from different HIV-1 subtypes. At a reduced concentrations, 2G12 showed much weaker neutralizing activities. Wang2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: Novel approaches based on sequential (SAP) and competitive (CAP) antigen panning methodologies, and use of antigens with increased exposure of conserved epitopes, for enhanced identification of broadly cross-reactive neutralizing Abs are reviewed. Previously known broadly neutralizing human mAbs are compared to Abs identified by these methods. Zhang2007 (review)
• 2G12: This Ab was used in the analysis of clade C gp140 (97CN54) antigenicity and was shown not to bind to this molecule, as the glycan epitope is absent. Sheppard2007a (binding affinity)
• 2G12: 2 glycosylation site additions to asparagines 295 and 392 on the clade C gp120 backbone (gp120CN54+) were used to reconstruct the 2G12 epitope, as the gp120CN54+ construct showed excellent reactivity with 2G12. gp120CN54+ and an Fc tagged outer domain of gp120 (ODCN54+-Fc) bound equally well to 2G12, while Fc fusion to gp120CN54+ reduced 2G12 binding, indicating partial occlusion of the 2G12 epitope. Chen2007a (antibody binding site, binding affinity)
• 2G12: Pseudoviruses derived from gp120 Env variants that evolved in multiple macaques infected with SHIV 89.6P displayed a range of degrees of virion-associated Env cleavage. Pseudoviruses with higher amount of cleaved Env were more sensitive to neutralization by 2G12, as they contained peripheral glycan N386, not present in the wildtype 89.6P. Blay2007 (neutralization)
• 2G12: Carbohydrate-binding agents, including 2G12, are reviewed regarding to their antiviral activity, resistance development, and their potential use as therapeutic agents. Balzarini2007 (review)
• 2G12: Increased neutralization sensitivity was observed for (R5)X4 viruses from timepoints both early and late after emergence of X4 compared to their coexisting R5 variants in one patient, and only for the early (R5)X4 viruses in another patient. In a third patient, in contrast, late (R5)X4 viruses were found to be significantly more resistant to 2G12 neutralization than their coexisting R5 variants. Bunnik2007 (co-receptor, neutralization)
• 2G12: Neutralization sensitivity of maternal and infant viruses to 2G12 close to transmission timepoint was shown to be poor. Even the viruses from one mother, that were shown to be sensitive to maternal Abs and pooled plasma, were not neutralized by 2G12, indicating that Abs in plasma are not directed to this Ab epitope. Rainwater2007 (neutralization, mother-to-infant transmission)
• 2G12: 2G12-neutralized HIV-1 captured on Raji-DC-SIGN cells or immature monocyte-derived DCs (iMDDCs) was successfully transferred to CD4+ T lymphocytes, indicating that the 2G12-HIV-1 complex was disassembled upon capture by DC-SIGN-cells. vanMontfort2007 (neutralization, dendritic cells)
• 2G12: Synthetic monomeric D1 arm oligosaccharide, corresponding to the D1 arm of Man9 which has a high affinity to 2G12, and its fluorinated derivative interacted with 2G12 only weakly. However, when four units of synthetic D1 arm tetrasaccharide were introduced to a cyclic decapeptide template, it showed high affinity to 2G12. Introduction of two T-helper epitopes onto the template did not affect 2G12 binding, indicating that the construct could be used as a new type of immunogen for raising carbohydrate-specific neutralizing Abs against HIV. Wang2007b (mimotopes, vaccine antigen design, kinetics, binding affinity)
• 2G12: Infusion of a MAb cocktail (4E10, 2G12 and 2F5) into HIV-1 infected subjects was shown to be associated with increased levels of serum anti-cardiolipin and anti-phosphatidylserine Ab titers, and increased coagulation times. In the absence or in the presence of adult and neonate plasma, 2G12 did not bind to either phosphatidylserine nor to cardiolipin, and did not induce significant prolongations of clotting times in human plasma, indicating that infusion of 2G12 was not responsible for autoreactivity and prolonged clotting times. Vcelar2007 (antibody interactions, autoantibody or autoimmunity, binding affinity, immunotherapy)
• 2G12: The major infectivity and neutralization differences between a PBMC-derived HIV-1 W61D strain and its T-cell line adapted counterpart were conferred by the interactions of three Env amino acid substitutions, E440G, D457G and H564N. Chimeric Env-pseudotyped virus Ch5, containing all three of the mutations, was equally neutralization sensitive to 2G12 as Ch2, which did not contain any of these mutations. Beddows2005a (neutralization)
• 2G12: Four primary isolates (PIs), Bx08, Bx17, 11105C and Kon, were tested for binding and neutralization by 2G12. 2G12 was only able to neutralize Bx08, but bound well to both Bx08 and Bx17 and less well to 11105C and Kon. There was no direct correlation between binding and neutralization of the four PIs by 2G12. CD4-induced gp120 shedding resulted in a decrease of 2G12 binding to Bx08. Presence of gp160 depleted of the principal immunodominant domain (PID) significantly decreased capture of Bx17 and Kon by 2G12. Presence of both gp160ΔPID and PID slightly improved the inhibition of virus capture compared to PID peptide alone, revealing an additive effect. Burrer2005 (neutralization, binding affinity)
• 2G12: A panel of 60 HIV-1 isolates, with complete genome sequences available, was formed for neutralization assay standardization. It comprises of 10 isolates from each of the subtypes A, B, C, D, CRF01_AE and CRF02AG, with majority of the viruses being of R5 phenotype and few of X4 phenotype. Neutralization profile of each isolate was assessed by measuring neutralization by sCD4, a cocktail of MAbs including 2G12, 2F5 and IgG1b12, and a large pool of sera collected from HIV-1 positive patients. The MAb cocktail neutralized with >50% a large portion of the isolates (51/60) including: 10 subtype A isolates, 8 subtype B isolates, 8 subtype C isolates, 9 subtype D isolates, 7 CRF-01_AE isolates, and 9 CRF_02AG isolates. Brown2005a (assay or method development, neutralization, subtype comparisons)
• 2G12: The unique structure of the 2G12 MAb, and the reasons for its unique ability to recognize oligomannose chains on the silent face of the gp120, are reviewed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed. Burton2005 (antibody binding site, review, structure)
• 2G12: SFV-gp140(-GCN4) was constructed for analysis of its immunogenic properties in animal models. Both gp120 and gp140(-GCN4) secreted from rSFV-infected cells were recognized by 2G12, suggesting that the proteins retained their native folding. Forsell2005 (antibody binding site)
• 2G12: Monomeric gp120 and trimeric gp140CF proteins synthesized from an artificial group M consensus Env gene (CON6) bound efficiently to 2G12, indicating correct exposure of the 2G12 epitope. A mix of 2G12, 2F5 and b12 MAbs (TriMab2) was used for neutralization assessment of some subtype B isolates, but showed no significant neutralization. Gao2005a (antibody binding site, neutralization)
• 2G12: 2G12 neutralized viral isolates HXBc2, SF162, 89.6 and BaL. ADA isolate was poorly neutralized and the YU2 isolate was not neutralized. Neutralization was concentration dependent, as higher MAb concentration resulted in higher % of neutralization. The exception was the YU2 isolate, where higher concentration of 2G12 resulted in enhancement of viral infection. Grundner2005 (enhancing activity, neutralization)
• 2G12: 2G12 bound with a higher maximal mean fluorescence intensity (MFI) to Env protein on the surface of cells producing gp140Δct-pseudotyped neutralization resistant 3.2P strain, than to the Env of pseudotyped neutralization sensitive HXBc2. Neutralization assays with the pseudotyped viruses showed that 2G12 neutralized both viruses with same potency. Furin co-transfection did not have an effect on the reactivity of pseudoviruses with 2G12 or on their neutralization sensitivity. Presence or absence of sialic acid residues did not affect Env reactivity with 2G12. Herrera2005 (antibody binding site, neutralization, binding affinity)
• 2G12: Why broadly neutralizing Abs, such as 2G12, 2F5 and 4E10, are extremely rare, and their protective abilities and potential role in immunotherapy are discussed. Julg2005 (neutralization, immunotherapy, review)
• 2G12: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alternations of both gp41 and gp120. The alternations did not affect virus CD4 binding, coreceptor binding site exposure, or infectivity of the virus, but did result in increased relative neutralization resistance of the LLP-2 mutant virus to 2G12, compared with wildtype virus. The increased neutralization resistance of LLP-2 virus was associated with decreased 2G12 binding to its epitope. Kalia2005 (antibody binding site, neutralization, binding affinity)
• 2G12: A series of genetically modified Env proteins were generated and expressed in both insect and animal cells to be monitored for their antigenic characteristics. For 2G12, two of the modified proteins expressed in insect cells, dV1V2 mutant (V1V2 deletions) followed by the dV2 mutant, showed higher binding to the Ab than the wildtype Env did, indicating that V1V2 deletion exposes epitopes against 2G12 better than other proteins. Unlike for most of the other MAbs, 3G mutant (mutations in 3 glycosylation sites) did not show a higher binding affinity to 2G12. When expressed in animal cells, only dV2 mutant resulted in higher binding to 2G12, while all other modified proteins showed lower binding compared to the wildtype. Kang2005 (antibody binding site, binding affinity)
• 2G12: Full-length gp160 clones were derived from acute and early human HIV-1 infections and used as env-pseudotyped viruses in neutralization assays for their characterization as neutralization reference agents. 12 out of 19 pseudoviruses were neutralized by 2G12, as were SF162.LS and IIIB strains but not the MN strain. Resistance to 2G12 was generally associated with lack of N-glycosylation sites, except in one case, where the clone was resistant to neutralization in spite of presence N-glycosylation sites. Two clones lacked N-glycosylation at residues 339 and 386, but remained sensitive to 2G12. A mixture of IgG1b12, 2F5 and 2G12 (TriMab) exhibited potent neutralizing activity against all Env-pseudotyped viruses except one. 7 out of 12 Env-pseudotyped viruses were more sensitive to neutralization by 2G12 than their uncloned parental PBMC-grown viruses. Li2005a (assay or method development, neutralization)
• 2G12: Pseudoviruses expressing HIV-1 envelope glycoproteins from BL01, BR07 and 89.6 strains were compared in neutralization assays to replication competent clone derived from transfection of 293T cells (IMC-293T) and to the IMC-293T derived from a single passage through PBMC (IMC-PBMC). The neutralization responses of pseudoviruses and corresponding IMC-293T to 2G12 were similar, while a significant decrease in viral neutralization sensitivity to 2G12 was observed for all three IMC-PBMC viruses. The decrease was associated with an increase in average virion envelope glycoprotein content on the PBMC-derived virus. Louder2005 (assay or method development, neutralization)
• 2G12: 2G12 was used as isolating template for screening of a phage library in order to develop mimotopes that target carbohydrate antigens of gp120. Specific binding of 2G12 to three phages expressing peptides was observed, however, 2G12 did not bind to the peptides themselves. Pashov2005a (assay or method development)
• 2G12: 2G12 neutralized JR-FL, but not YU2 HIV-1 strain. 2G12 and other neutralizing mAbs recognized JR-FL cleavage-competent and cleavage-defective env glycoproteins, while non-neutralizing Abs only recognized JR-FL cleavage-defective glycoproteins. It is suggested that an inefficient env glycoprotein precursor cleavage exposes non-neutralizing determinants, while only neutralizing regions remain accessible on efficiently cleaved spikes. For YU2, both cleavage-competent and -defective glycoproteins were recognized by both neutralizing and non-neutralizing Abs. Pancera2005 (antibody binding site, neutralization, binding affinity)
• 2G12: A short review of 2F5 and 4E10 interaction with autoantigens, epitope accessibility, structure, neutralizing capability, and the reasons for their infrequent appearance in nature. Immunotherapy and escape to 2G12 is also discussed. Nabel2005 (escape, immunotherapy, review)
• 2G12: Viruses containing substitutions at either L568 or K574 of the gp41 hydrophobic pocket were resistant to D5-IgG1 but were as sensitive to 2G12 as the wildtype virus. Miller2005
• 2G12: This short review summarizes recent findings of the role of neutralizing Abs in controlling HIV-1 infection. Certain neutralizing MAbs and their potential role in immunotherapy and vaccination, as well as the reasons for their poor immunogenicity, are discussed. Montefiori2005 (antibody binding site, therapeutic vaccine, escape, immunotherapy)
• 2G12: Virions containing a single point mutation Y706C in gp41 had a 10-fold increase in binding to 2G12 compared to wildtype. This, together with the same p24 supernatant levels after transfection with wildtype and mutant virus, indicated that the mutant virions contained more envelope on a per-particle basis. Poon2005 (antibody binding site, binding affinity)
• 2G12: Escape mutations in HR1 of gp41 that confer resistance to Enfuvirtide reduced infection and fusion efficiency and also delayed fusion kinetics of HIV-1. They also conferred increased neutralization sensitivity to a subset of neutralizing MAbs that target fusion intermediates or with epitopes exposed following receptor interactions. Enhanced neutralization correlated with reduced fusion kinetics. None of the mutations had a significant effect on 2G12 neutralization of virus. Reeves2005 (antibody binding site, drug resistance, neutralization, escape, HAART, ART)
• 2G12: There was no difference found in the neutralization sensitivity of viruses isolated from acutely and from chronically infected HIV-1 patients to this Ab, suggesting that the glycosylation sites manifesting the epitope of 2G12 are well conserved throughout the course of infection. Rusert2005 (antibody binding site, neutralization, acute/early infection)
• 2G12: This review summarizes data on the role of NAb in HIV-1 infection and the mechanisms of Ab protection, data on challenges and strategies to design better immunogens that may induce protective Ab responses, and data on structure and importance of MAb epitopes targeted for immune intervention. The importance of standardized assays and standardized virus panels in neutralization and vaccine studies is also discussed. Srivastava2005 (antibody binding site, neutralization, vaccine antigen design, binding affinity, immunotherapy, review, structure)
• 2G12: Six acutely and eight chronically infected patients were passively immunized with a mix of 2G12, 2F5 and 4E10 neutralizing Abs during treatment interruption. Two chronically and four acutely infected individuals showed evidence of a delay in viral rebound during Ab treatment suggesting that NAbs can contain viremia in HIV-1 infected individuals. All subjects with virus sensitive to 2G12 developed Ab escape mutants resulting in loss of viremia and failure to treatment. In several cases resistance to 2G12 emerged rapidly. Plasma levels of 2G12 were substantially higher than those of 2F5 and 4E10, and the 2G12 levels exceeded the in vitro required 90% inhibitory doses by two orders of magnitude in subjects that responded to Ab treatment. This suggested that high levels of NAbs are required for inhibition in vivo. Trkola2005 (neutralization, acute/early infection, escape, immunotherapy, early treatment, HAART, ART, supervised treatment interruptions (STI))
• 2G12: Ab neutralization of viruses with mixtures of neutralization-sensitive and neutralization-resistant envelope glycoproteins was measured. It was concluded that binding of a single Ab molecule is sufficient to inactivate function of an HIV-1 glycoprotein trimer. The inhibitory effect of the Ab was similar for neutralization-resistant and -sensitive viruses indicating that the major determinant of neutralization potency of an Ab is the efficiency with which it binds to the trimer. It was also indicated that each functional trimer on the virus surface supports HIV-1 entry independently, meaning that every trimer on the viral surface must be bound by an Ab for neutralization of the virus to be achieved. Yang2005b (neutralization)
• 2G12: A substantial fraction of soluble envelope glycoprotein trimers contained inter-subunit disulfide bonds. Reduction of these disulfide bonds had little effect on binding of the 2G12 to the glycoprotein, indicating that the inter-S-S bonds had no impact on the exposure of 2G12 epitope. Yuan2005 (antibody binding site)
• 2G12: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1. McCann2005 (antibody binding site, antibody interactions, neutralization, vaccine antigen design, variant cross-reactivity, immunotherapy, review, structure)
• 2G12: 2G12 was investigated in different neutralization formats, including the standard format that measures activity over the entire infection period and several formats that emphasize various stages of infection. The activity of 2G12 was induced in the post-CD4 format and was less pronounced in the standard format. 2G12 did not neutralize after CD4/CCR5 engagement. HIV-1+ human plasma mediated high-levels of post-CD4 neutralization indicating presence of b12 and 2G12 -like Abs. Crooks2005 (antibody binding site, assay or method development, neutralization)
• 2G12: This review summarizes data on the polyspecific reactivities to host antigens by the broadly neutralizing MAbs IgG1b12, 2G12, 2F5 and 4E10. It also hypothesizes that some broadly reactive Abs might not be routinely made because they are derived from B cell populations that frequently make polyspecific Abs and are thus subjected to B cell negative selection. Haynes2005a (antibody interactions, review)
• 2G12: This review summarizes data that indicate that the V3 region of HIV-1 may be an epitope to target for the induction of protective Abs. Data shows that the V3 region can induce broadly-reactive, cross-neutralizing Abs, that it is partially exposed during various stages of the infectious process, and that it is immunogenic. 2G12 is the only highly neutralizing MAb targeting the carbohydrate region of gp120, suggesting that this region does not induce protective Abs. The carbohydrate epitope is poorly immunogenic and 2G12 has an aberrant structure probably extremely rare in the human Ab repertoire. Zolla-Pazner2005 (antibody binding site, variant cross-reactivity, review)
• 2G12: In addition to gp120-gp41 trimers, HIV-1 particles were shown to bear nonfunctional gp120-gp41 monomers and gp120-depleted gp41 stumps on their surface. 2G12 effectively neutralized wildype virus particles. 2G12 was found to bind to both nonfunctional monomers and to gp120-gp41 trimers. Binding of 2G12 to trimers correlated with its neutralization of wildtype virus particles. Monomer binding did not correlate with neutralization, but it did correlate with virus capture. It is hypothesized that the nonfunctional monomers on the HIV-1 surface serve to divert the Ab response, helping the virus to avoid neutralization. Moore2006 (antibody binding site, neutralization, binding affinity)
• 2G12: A carbohydrate mimetic peptide with central motif versions RYRY and YPYRY was shown to precipitate human IgG Ab that bind to gp120 and to immunoprecipitate gp120 from transfected cells. 2G12 showed significant binding only to the PYPY motif version of the peptide. Pashov2006 (mimotopes)
• Macaques were immunized with SF162gp140, ΔV2gp140, ΔV2ΔV3gp140 and ΔV3gp140 constructs and their antibody responses were compared to the broadly reactive NAb responses in a macaque infected with SHIV SF162P4, and with pooled sera from humans infected with heterologous HIV-1 isolates (HIVIG). 2G12 recognized all four gp140 proteins equally. Low titers of Abs capable of blocking the binding of 2G12 were present in the sera from the SHIV-infected macaque, but were absent in the sera from the gp140-immunized animals. Derby2006 (antibody binding site)
• 2G12: Development of neutralizing Abs and changes to Env gp120 were analyzed in SHIV infected macaques during a period of 1 year. 4 macaques showed little viral divergence while the remaining 7 showed significant env divergence from the inoculum, associated with higher titers of homologous NAbs. In five of the 7 divergent animals, the glycosylation site N386, which is a part of the 2G12 epitope, was significantly added. Glycosylation sites N392, on the inner domain of gp120, and N295, on the silent face, also forma a part of the 2G12 epitope, and were found to be highly conserved. Blay2006 (antibody binding site)
• 2G12: 2G12 did not inhibit binding of Fc-gp120 to CD4, however, it inhibited binding of Fc-gp120, and of the virus itself, to the CCR5 coreceptor and to the DC-SIGN. Thus 2G12 probably inhibits HIV-1 by two mechanisms: blocking of gp120-CCR5 and of gp120-DC-SIGN interactions. Pre-incubation of virus with sCD4 did not affect its neutralization by 2G12. This Ab was also shown to effectively inhibit trans-infection of virus from primary monocyte-derived dendritic cells (MDDCs) to CD4+ T-cells. Attachment of Fc-gp120 to MDDCs and PBLs was partially inhibited by 2G12, while b12 and sCD4 did not inhibit binding to MDDCs but did inhibit binding to PBLs. The results indicate that Env attachment is mediated through DC-SIGN and other receptors on MDDCs while it is predominantly mediated by CD4 and CCR5 on PBLs. Binley2006 (antibody binding site, co-receptor, neutralization, binding affinity, dendritic cells)
• 2G12: A fusion protein (FLSC R/T-IgG1) that targets CCR5 was expressed from a synthetic gene linking a single chain gp120-CD4 complex containing an R5 gp120 sequence with the hinge-Ch2-Ch3 portion of human IgG1. The fusion protein did not activate the co-receptor by binding. In cell-line based assays, the FLSC R/T-IgG1 was less potent in neutralizing R5 HIV-1 primary isolates than 2G12, while in PBMC assays they were comparable. Vu2006 (neutralization)
• 2G12: Env-pseudotyped viruses were constructed from the gp160 envelope genes from seven children infected with subtype C HIV-1. 2G12 failed to neutralize any of the seven viruses, correlating with the absence of crucial N-linked glycans that define 2G12 epitope on these viruses. When this Ab was mixed with IgG1b12 and 2F5, the neutralization was similar as to IgGb12 alone, indicating that the majority of the pool activity was due to IgG1b12. When 4E10 was added to this mix, all isolates were neutralized. Gray2006 (neutralization, variant cross-reactivity, responses in children, mother-to-infant transmission)
• 2G12: Pharmacokinetic properties of this Ab were studied in HIV infected patients infused with high doses of 2G12. The Ab did not elicit an endogenous immune response and had distribution and systemic clearance values similar to other Abs. The elimination half-life was measured to 21.8 days, which is significantly longer than the elimination half-life of 4E10 and 2F5. Joos2006 (kinetics, immunotherapy)
• 2G12: Inhibition of 2G12 binding to gp120 by 2G12-like Abs in sera from long-term non-progressors (LTNP) was determined. 2G12-like Abs were present in almost all sera from LTNPs but at a lower levels than b12. Higher 2G12-like Ab levels were significantly associated with the broadest neutralizing activity in sera from LNTPs. Braibant2006 (enhancing activity, neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: Neutralization rates and rate constants for the neutralization of clade B primary isolates SF33, SF162 and 89.6 by this Ab were determined. Statistically significant neutralization was not observed for isolate SF162. It was shown that neutralization sensitivity is not associated with neutralization of cell-associated or free virus. Davis2006 (neutralization, variant cross-reactivity, kinetics)
• 2G12: Cloned Envs (clades A, B, C, D, F1, CRF01_AE, CRF02_AG, CRF06_cpx and CRF11_cpx) derived from donors either with or without broadly cross-reactive neutralizing antibodies were shown to be of comparable susceptibility to neutralization by 2G12. Cham2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 2G12: The ability of this Ab to inhibit viral growth was increased when macrophages and immature dendritic cells (iDCs) were used as target cells instead of PHA-stimulated PBMCs. It is suggested that inhibition of HIV replication by this Ab for macrophages and iDCs can occur by two distinct mechanisms, neutralization of infectivity involving only the Fab part of the IgG, and, an IgG-FcγR-dependent interaction leading to endocytosis and degradation of HIV particles. Holl2006 (neutralization, dendritic cells)
• 2G12: Viruses with cleavage-competent 2G12-knockout Env and cleavage-defective Env able to bind 2G12 were constructed. The amount of Env precipitated by 2G12 was same when the two pseudotyped virus variants were mixed as with the wildtype alone, suggesting formation of heterotrimers consisting of both cleavage-competent and defective Envs. The presence of nonfunctional Envs on the surface of infectious virions did not affect the neutralization by 2G12. The neutralization by the CD4-binding agents was also unaffected by 2G12 binding to uncleaved Env indicating that the function of a trimer is unaffected sterically by the binding of an antibody to adjacent trimer. Herrera2006 (neutralization, binding affinity)
• 2G12: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The neutralizing activity of 2G12 was higher in iMDDCs than in PHA-stimulated PBMCs. A 90% reduction of HIV infection was observed without induction of MDDC maturation by this MAb. Blockade of FcgammaRII on iMDDCs decreased the anti-HIV activity of 2G12 while increased expression of FcgammaRI increased inhibition of HIV by 2G12, suggesting the involvement of these receptors in the HIV-inhibitory activity of this Ab. Holl2006a (neutralization, dendritic cells)
• 2G12: G1 and G2 recombinant gp120 proteins, consisting of 2F5 and 4E10, and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120, were tested as an immunogen to see if they could elicit MPER antibody responses. Deletion of V1/V2 from gp120 or its replacement with G1 and G2 grafts, did not greatly affect binding of 2G12 to gp120. Shortening of the N and C termini of the V3 loop nearly abolished binding of 2G12. Law2007 (vaccine antigen design)
• 2G12: This review describes the effectiveness of the current HIV-1 immunogens in eliciting neutralizing antibody responses to different clades of HIV-1. It also summarizes different evasion and antibody escape mechanisms, as well as the most potent neutralizing MAbs and their properties. MAbs reviewed in this article are: 2G12, IgG1b12, 2F5, 4E10, A32, 447-52D and, briefly, D50. Novel immunogen design strategies are also discussed. Haynes2006a (antibody binding site, neutralization, variant cross-reactivity, escape)
• 2G12: 2G12 was used as a negative control to investigate the relationship of MAb 412d epitope to the CCR5 binding site of gp120. These two MAbs were incubated with soluble CD4 and ADA gp120 in the presence of a peptide shown to block the association of gp120-CD4 with CCR5. As expected, the presence of the peptide did not inhibit precipitation of gp120 by 2G12, since it binds an epitope distinct from the CCR5 binding domain, while it did inhibit the 412d. Choe2003 (antibody binding site)
• 2G12: The gp140δCFI protein of CON-S M group consensus protein and gp140CFI and gp140CF proteins of CON6 and WT viruses from HIV-1 subtypes A, B and C were expressed in recombinant vaccinia viruses and tested as immunogens in guinea pigs. 2G12 was shown to bind specifically to all recombinant proteins except for the subtype B gp140δCF and subtype A gp140δCFI. The specific binding of this Ab to CON-S indicated that its conformational epitope was intact. This Ab also bound specifically to the two tested subtype B gp120 proteins. Liao2006 (antibody binding site, vaccine antigen design, subtype comparisons)
• 2G12: Cross-neutralization was limited in this study. 2G12 neutralized subtype A strain UG273 and subtype B strains US2, NL4-3, and IIIB. It did not neutralize subtype C strain ETH2220, subtype D UG270, CRF01 A/E ID12; subtype F BZ163; nor subtype G BCF06. 3 HIV-2 strains and SIVmac 251 were also not neutralized. 2G12 bound to MN and NDK, but did not neutralize them. Neutralization resistance was selected in culture using strains NL43 and IIIB. NL43 escaped via loss of the glycosylation sequon at positions 295-297, IIIB escaped via sequon losses at positions 392-394 and 295-297, or 406-408, as expected from earlier studies defining critical mannose residues for 2G12 binding. The loss of the mannose actually enhanced mannose-specific lectin inhibition of the virus. Huskens2007 (antibody binding site, neutralization, variant cross-reactivity, escape, subtype comparisons)
• 2G12: Binding of 2G12 to gp120 was not significantly affected by the small molecule HIV-1 entry inhibitor IC9564. IC9564 induces conformational change of gp120 to allow CD4i antibody 17b to bind, but inhibits CD4-induced gp41 conformational changes. Huang2007 (antibody binding site)
• 2G12: The neutralizing activity of this antibody for the JR-FL Env variant with the N160K/E160K mutations was measured in comparison with the neutralizing activity of 2909, which was found to be higher. Honnen2007 (neutralization, variant cross-reactivity)
• 2G12: Controlled attachment of Ab-bound HIV to cells was not affected by the presence of this Ab. However, the virus was still efficiently neutralized indicating that binding of 2G12 to the cell-free virus interferes with a step of infection subsequent to cell attachment. Haim2007 (antibody binding site, neutralization, kinetics)
• 2G12: This Ab was used to help define the antigenic profile of envelopes used in serum depletion experiments to attempt to define the neutralizing specificities of broadly cross-reactive neutralizing serum. It bound to JR-FL and JR-CSF gp120 monomers and to a lesser extent to core JR-CSF gp120 monomer. Dhillon2007 (antibody binding site, neutralization)
• 2G12: SOSIP Env proteins are modified by the introduction of a disulfide bond between gp120 and gp41 (SOS), and an I559P (IP) substitution in gp41, and form trimers. The KNH1144 subtype A virus formed more stable trimers than did the prototype subtype B SOSIP Env, JRFL. The stability of gp140 trimers was increased for JR-FL and Ba-L SOSIP proteins by substituting the five amino acid residues in the N-terminal region of gp41 with corresponding residues from KNH1144 virus. b12, 2G12, 2F5, 4E10 and CD4-IgG2 all bound similarly to the WT and to the stabilized JRFL SOSIP timers, suggesting that the trimer-stabilizing substitutions do not impair the overall antigenic structure of gp140 trimers. Dey2007
• 2G12: 15 subtype A HIV-1 envelopes from early in infection were not neutralized by 2G12, likely because of a deletion or shift in one or more of the 5 glycosylation sites associated with 2G12 recognition. SF162 was neutralized as expected. Blish2007 (neutralization, acute/early infection, subtype comparisons)
• 2G12: This Ab was found to be able to bind to a highly stable trimeric rgp140 derived from a HIV-1 subtype D isolate containing intermonomer V3-derived disulfide bonds and lacking gp120/gp41 cleavage. Billington2007
• 2G12: Yeast display was compared to phage display and shown to select all the scFv identified by phage display and additional novel antibodies. Biotinylated C11 and 2G12 were used to minimize selection of non-gp120 specific clones from the yeast displayed antibody library; these MAbs were used as they have unique epitopes with limited overlap with most known epitopes. Bowley2007 (assay or method development)
• 2G12: Four consensus B Env constructs: full length gp160, uncleaved gp160, truncated gp145, and N-linked glycosylation-site deleted (gp160-201N/S) were compared. All were packaged into virions, and all but the fusion defective uncleaved version mediated infection using the CCR5 co-receptor. Primary isolate Envs were completely resistant or just somewhat sensitive to neutralization by 2G12 while the consensus B constructs were sensitive. Thus the 2G12 epitope is present on the consensus B Env glycoprotein and was not influenced by the Env modifications in this study. Kothe2007 (vaccine antigen design, variant cross-reactivity)
• 2G12: Newborn macaques were challenged orally with the highly pathogenic SHIV89.6P and then treated intravenously with a combination of IgG1b12, 2G12, 2F5 and 4E10 one and 12 hours post-virus exposure. All control animals became highly viremic and developed AIDS. In the group treated with mAbs 1 hour post-virus exposure, 3/4 animals were protected from persistent systemic infection and one was protected from disease. In the group treated with mAbs 12 hour post-virus exposure, one animal was protected from persistent systemic infection and disease was prevented or delayed in two animals. IgG1b12, 2G12, and 4E10 were also given 24 hours after exposure in a separate study; 4/4 treated animals become viremic, but with delayed and lower peak viremia relative to controls. 3/4 treated animals did not get AIDS during the follow up period, and 1 showed a delayed progression to AIDS , while the 4 untreated animals died of AIDS. Thus the success of passive immunization with NAbs depends on the time window between virus exposure and the start of immunoprophylaxis. Ferrantelli2007 (immunoprophylaxis)
• 2G12: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. 2G12 had diminished binding to both antigen constructs. Selvarajah2005 (vaccine antigen design, vaccine-induced immune responses)
• 2G12: Concanavalin A (ConA) binds to mannose and blocks 2G12 binding, but 2G12 does not block ConA binding. ConA binding is less sensitive to mutations in glycosylation sites than 2G12. Furthermore, ConA neutralizes HIV-1 at a post-CD4 binding step. Thus, this report indicates that designing antigens based on the HIV-1 mannose residues that bind ConA may be an effective vaccine strategy, as antibodies elicited might be broadly cross-reactive. Pashov2005 (vaccine antigen design)
• 2G12: Passive immunization of 8 HIV-1 infected patients with 4E10, 2F5 and 2G12 (day 0, 4E10; days 7, 14 and 21 4E10+2G12+2F5; virus isolated on days 0 and 77) resulted in 0/8 patients with virus that escaped all three NAbs. Three patients had viruses that escaped 2G12, and two of these were sequenced. Each had lost two of the glycosylation sites required for 2G12 binding (one had 295 N->D and 332 N->T changes, the other had 295 N->T and 392 N->T changes). In a companion in vitro study, resistance to a single MAb emerged in 3-22 weeks, but triple combination resistance was slower and characterized by decreased viral fitness. In contrast to the in vivo escape study, only one N was lost in the in vitro experiments, a 386 N->K change in a triple resistant mutant. The lack of resistance to the combination of MAbs in vivo and the reduced fitness of the escape mutants selected in vitro suggests passive immunotherapy may be of value in HIV infection. Nakowitsch2005 (escape, immunotherapy)
• 2G12: Nine anti-gp41 bivalent Fabs that interacted with either or both of the six-helix bundle and the internal coiled-coil of N-helices of gp41 were selected from a non-immune human phage display library. The IC50 the range for the inhibition of LAV ENV-mediated cell-fusion was 6-61 ug/ml -- for context, 2F5 and 2G12 (IC50s of 0.5-1.5 ug/ml) were about an order of magnitude more potent in this assay than the best Fabs generated here. Louis2005 (neutralization)
• 2G12: Retrovirus inactivation for vaccine antigen delivery was explored through lipid modification by hydrophobic photoinduced alkylating probe 1.5 iodonaphthylazide (INA). The viral proteins were shown to be structurally intact in the treated non-infectious virus, through the preservation of antibody binding sites for polyclonal anti-gp120 serum, and for broadly neutralizing MAbs 2G12, b12 and 4E10, although the modifications of the lipid disabled viral infection. Raviv2005 (vaccine antigen design)
• 2G12: This study is about the V2 MAb C108g, that is type-specific and neutralizes BaL and HXB2. JR-FL is a neutralization resistant strain; modification of JRFL at V2 positions 167 and 168 (GK->DE) created a C108g epitope, and C108g could potently neutralize the modified JR-FL. The modification in V2 also increased neutralization sensitivity to V3 MABs 4117c, 2219, 2191, and 447-52D, but only had minor effects on neutralization by CD4BS MAb 5145A, and broadly neutralizing MAbs IgG1b12, 2G12, and 2F5. Pinter2005 (antibody binding site)
• 2G12: The HIV-1 Bori-15 variant was adapted from the Bori isolate for replication in microglial cells. Bori-15 had increased replication in microglial cells and a robust syncytium-forming phenotype, ability to use low levels of CD4 for infection, and increased sensitivity to neutralization by sCD4 and 17b. Four amino acid changes in gp120 V1-V2 were responsible for this change. Protein functionality and integrity of soluble, monomeric gp120-molecules derived from parental HIV-1 Bori and microglia-adapted HIV-1 Bori-15 was assessed in ELISA binding assays using CD4BS MAbs F105 and IgG1b12, glycan-specific 2G12, and V3-specific 447-52D, and were unchanged. Association rates of sCD4 and 17b were not changed, but dissociation rates were 3-fold slower for sCD4 and 14-fold slower for 17b. Martin-Garcia2005 (antibody binding site)
• 2G12: Sera from subtype A infected individuals from Cameroon have antibodies that react strongly with subtype A and subtype B V3 loops in fusion proteins, and neutralize SF162 pseudotypes, while sera from 47 subtype B infected individuals reacted only with subtype B V3s. Sera from Cameroon did not neutralize primary A or B isolates, due to indirect masking by the V1/V2 domain rather than due to loss of the target epitope. Neutralization by Cameroonian sera MAbs was blocked by Clade A and B V3 loop fusion proteins, while NAbs to non-V3 epitopes, 2F5, 2G12, and b12, were not blocked. Krachmarov2005 (antibody binding site, variant cross-reactivity, subtype comparisons)
• 2G12: Of 35 Env-specific MAbs tested, only 2F5, 4E10, IgG1b12, and two CD4BS adjacent MAbs (A32 and 1.4G) and gp41 MAbs (2.2B and KU32) had binding patterns suggesting polyspecific autoreactivity, and similar reactivities may be difficult to induce with vaccines because of elimination of such autoreactivity. Unlike the other three broadly neutralizing human anti-HIV-1 MAbs, 2G12 has no indication of polyspecific autoreactivity. Haynes2005 (antibody binding site)
• 2G12: 2909 is a human anti-Env NAb that was selected by a neutralization assay and binds to the quaternary structure on the intact virion. ELISA-based competition assays and subsequent mutational analysis determined that the CD4BS and V2 and V3 loops contribute to the 2909 epitope: 2909 binding was inhibited by MAbs 447-52d (anti-V3), 830A (anti-V2), and IgG1b12 (anti-CD4BS) and sCD4. 2909 was not inhibited by MAbs 670, 1418, nor 2G12; in fact, 2G12 enhanced 2909 binding. Gorny2005
• 2G12: Precise characterization of 2G12 binding to carbohydrate was undertaken; the 2G12 Fab was co-crystallized with four oligomannose derivatives, Man4, Man5, Man7 and Man8. 2G12 recognizes the terminal Manα1-2Man both in the context of the D1 arm (Manα1-2Manα1-2Man) and D3 arm (Manα1-2Manα1-6Man) of the Man9GlcNAc2 moiety, but not the D2 arm. This gives the 2G12 more binding flexibility than previously thought, as only the D1 arm binding had been shown previously. Calarese2005 (antibody binding site, structure)
• 2G12: The lack of glycosylation sites at residues Asn 295 and Thy 394 within C-clade gp120s generally causes the loss of 2G12 recognition. Introduction of glycans in the subtype C strain HIV-1CN54 at these positions restored 2G12 binding, and addition of just a single glycan partially restored binding (V295N + A394T >> V295N > A395T). 2G12 epitope recovery decreased b12 binding. Chen2005 (antibody binding site)
• 2G12: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it binds to the neutralizing MAb 2G12. It masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120. Pantophlet2004 (vaccine antigen design)
• 2G12: Infusions of 2F5 and 2G12 intravenously administered 24h prior to vaginal SHIV-89.P challenge are able to protect macaques from infections. Animals that receive a IL-2 adjuvanted DNA immunization SIV Gag and HIV Env have T-cell responses and lower viral loads, but were not protected. Suboptimal levels of 2F5 and 2G12 were not able to confer sterile protection in combination with the T-cell responses stimulated by DNA immunizations. Mascola2003
• 2G12: Nabs against HIV-1 M group isolates were tested for their ability to neutralize 6 randomly selected HIV-1 O group strains. 2G12 did not neutralize O group strains, although it was included in a quadruple combination of b12, 2F5, 2G12, and 4E10, that neutralized the six Group O viruses between 62-97%. Ferrantelli2004a (variant cross-reactivity)
• 2G12: Neonatal rhesus macaques were exposed orally to a pathogenic SHIV, 89.6P. 4/8 were given an intramuscular, passive immunization consisting of NAbs 2G12, 2F5 and 4E10, each given at a different body sites at 40 mg/kg per Ab, at one hour and again at 8 days after exposure to 89.6P. The four animals that were untreated all died with a mean survival time of 5.5 weeks, the four animals that got the NAb combination were protected from infection. This model suggests Abs may be protective against mother-to-infant transmission of HIV. Ferrantelli2004 (mother-to-infant transmission)
• 2G12: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. 2G12 primarily neutralized B clade viruses with sporadic neutralization of A, D, and two AC recombinants, and no C or CRF01 (E) isolates. Envelopes from subtypes C and E have generally lost critical glycans for 2G12 binding. Binley2004 (variant cross-reactivity, subtype comparisons)
• 2G12: Env sequences were derived from 4 men at primary infection and four years later; the antigenicity in terms of the ability to bind to 2G12, 2F5 and IgG1b12 was determined. 2G12 bound primarily to late clones in 3 of the 4 patients, and to both early and late in the other patient. Neither 2F5 nor IgG1b12 showed a difference in binding affinity to early or late envelopes. The number of glycosylation sites increased in the three patients. The ability to bind to 2G12 correlated perfectly with having all three sites known to be important for binding: N295 in C2, N332 in C3, and N392 in the V4 loop. Dacheux2004 (antibody binding site, acute/early infection, kinetics)
• 2G12: Crystal structure analysis of Fab 2G12 alone or complexed with Manα1-2Man or Man9GlcNac2 demonstrates that the exchange of VH domains forms stable dimers for gp120 binding. Two Fabs assemble in an interlocked VH domain swapped dimer, providing an extended surface for multivalent interaction with the cluster of oligomannose on gp120, allowing high-affinity recognition of repeated epitopes in the carbohydrate structure. Ala substitutions of the 2G12 VH/VH' interface residues Ile H19, Arg H57, Phe H77, Tyr H80, Val H84 and Pro H113 result in the loss of 2G12-gp120 JR-FL binding. Calarese2003 (antibody binding site, antibody sequence, structure)
• 2G12: Synthetic mannose Man9 clusters arranged on a scaffold were used to mimic the epitope of 2G12. Bi-, tri, and tetra-valent clusters had a 7-, 22-, and 73-fold higher affinities for 2G12 than the monomers, suggesting that 2G12 binds best to multiple carbohydrate moieties. 2G12 bound larger mannose oligosaccharides with higher affinity: Ma9GlcNAc bound 210- and 74-fold more effectively that Man6GlcNac and Man5GlcNAc, respectively. Wang2004 (antibody binding site)
• 2G12: This review discusses research presented at the Ghent Workshop of prevention of breast milk transmission and immunoprophylaxis for HIV-1 in pediatrics (Seattle, Oct. 2002), and makes the case for developing passive or active immunoprophylaxis in neonates to prevent mother-to-infant transmission. Macaque studies have shown that passive transfer of NAb combinations (for example, IgG1b12, 2G12, 2F5, and 4E10; or 2G12 and 2F5) can confer partial or complete protection to infant macaques from subsequent oral SHIV challenge. Safrit2004 (immunoprophylaxis, mother-to-infant transmission)
• 2G12: A primary isolate, CC1/85, was passaged 19 times in PBMC and gradually acquired increased sensitivity to FAb b12 and sCD4 that was attributed to changes in the V1V2 loop region, in particular the loss of a potential glycosylation site. The affinity for sCD4 was unchanged in the monomer, suggesting that the structural impact of the change was manifested at the level of the trimer. The passaged virus, CCcon19, retained an R5 phenotype and its neutralization susceptibility to other Abs was essentially the same as CC1/85. The IC50 for 2G12 was 1.8 for CC1/85, and was 4.2 for CCcon19, so both the primary and passaged viruses were neutralized. Pugach2004 (variant cross-reactivity, viral fitness and reversion)
• 2G12: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neutralization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype. 2G12 was the only MAb that neutralized JRFL more efficiently than SF162, with a 6-fold lower ND50 for JRFL. 2G12 also had a higher affinity for JRFL. Pinter2004 (variant cross-reactivity)
• 2G12: An antigen panel representing different regions of gp41 was generated, and sera from 23 individuals were screened. 2G12 was a control, binding to gp120 but to none of the gp41 peptides in the experiment. Opalka2004 (assay or method development)
• 2G12: A set of HIV-1 chimeras that altered V3 net charge and glycosylation patterns in V1V2 and V3, involving inserting V1V2 loops from a late stage primary isolate taken after the R5 to X4 switch, were studied with regard to phenotype, co-receptor usage, and MAb neutralization. The loops were cloned into a HXB2 envelope with a LAI viral backbone. It was observed that the addition of the late-stage isolate V1V2 region and the loss of V3-linked glycosylation site in the context of high positive charge gave an X4 phenotype. R5X4 viruses were more sCD4 and 2G12 neutralization resistant than either R5 or X4, but the opposite pattern was observed for b12. Addition of the late stage V1V2 altered neutralization for both MAbs, but this alteration was reversed with the loss of the V3 glycan. Nabatov2004 (antibody binding site, co-receptor)
• 2G12: Mice susceptible to MV infection were intraperitoneally immunized with native HIV-1 89.6 env gp160 and gp140 and δV3 HIV-1 89.6 mutants expressed in live attenuated Schwarz measles vector (MV). The gp160ΔV3 construct raised more cross-reactive NAbs to primary isolates. A HIVIG/2F5/2G12 combination was used as a positive control and could neutralize all isolates. Lorin2004 (vaccine antigen design)
• 2G12: 2G12 was used as a positive control in a study that showed that A32-rgp120 complexes open up the CCR5 co-receptor binding site, but did not induce neutralizing antibodies with greater breadth among B subtype isolates than did uncomplexed rgp120 in vaccinated guinea pigs. Liao2004 (vaccine antigen design)
• 2G12: A set of oligomeric envelope proteins were made from six primary isolates for potential use as vaccine antigens: 92/UG/037 (clade A), HAN2/2 (clade B), 92/BR25/025 (clade C), 92/UG/021 (clade D), 93/BR/029 (clade F) and MVP5180 (clade O). This was one of a panel of MAbs used to explore folding and exposure of well characterized epitopes. The clade C isolate BR25 is apparently misfolded, as conformation-dependent antibodies did not bind to it. 2G12 bound to clade A, B, D and F HIV-1 primary isolates. Polyclonal sera raised in rabbits against these antigens cross-bound the other antigens, but none of the sera had neutralizing activity. Jeffs2004 (vaccine antigen design, subtype comparisons)
• 2G12: The peptide 12p1 (RINNIPWSEAMM) inhibits direct binding of YU2 gp120 or Env trimer to CD4, CCR5 and MAb 17b in a concentration-dependent allosteric manner. 12p1 is thought to bind to unbound gp120 near the CD4 binding site, with a 1:1 stoichiometry. 12p1 also inhibited MAb F105 binding; presumably because F105 favors an unactivated conformation, but not MAbs 2G12 or b12. The 1:1 stoichiometry, the fact that the peptide binding site is accessible on the trimer, the non-CD4 like aspect of the binding, and an ability to inhibit viral infection in cell cultures make it a promising lead for therapeutic design. Biorn2004
• 2G12: This paper is a review of anti-HIV-1 Envelope antibodies. This unique epitope is formed from carbohydrates. The mechanism of MAb neutralization is thought to be steric inhibition of CCR5 binding. 2G12 neutralizes many TCLA strains and about 40% of primary isolates tested. Gorny2003 (review)
• 2G12: A gp120 molecule was designed to focus the immune response onto the IgG1b12 epitope. Ala substitutions that enhance the binding of IgG1b12 and reduce the binding of non-neutralizing MAbs were combined with additional N-linked glycosylation site sequons inhibiting binding of non-neutralizing MAbs; b12 bound to the mutated gp120. C1 and C5 were also removed, but this compromised b12 binding. Pantophlet2003b (vaccine antigen design)
• 2G12: scFv 4KG5 reacts with a conformational epitope. Of a panel of MAbs tested, only NAb b12 enhanced 4KG5 binding to gp120. MAbs to the V2 loop, V3 loop, V3-C4 region, and CD4BS diminished binding, while MAbs directed against C1, CD4i, C5 regions didn't impact 4KG5 binding. These results suggest that the orientation or dynamics of the V1/V2 and V3 loops restricts CD4BS access on the envelope spike, and IgG1b12 can uniquely remain unaffected. 2G12 had no impact on 4KG5 binding. Zwick2003a (antibody interactions)
• 2G12: The broadly neutralizing antibodies 2F5 and 2G12 were class-switched from IgG to IgA and IgM isotypes. Neutralizing potency was increased with valence for 2G12 so the IgM form was most potent, but for 2F5 the IgG form was most potent. Eight primary isolates were tested including two subtype A isolates. The polymeric IgM and IgA Abs, but not the corresponding IgGs, could interfere with HIV-1 entry across a mucosal epithelial layer, although they were limited in a standard neutralization assay. All isotypes could interact with activated human sera, presumably through complement, to inhibit HIV replication. Wolbank2003 (complement, genital and mucosal immunity, isotype switch, variant cross-reactivity, subtype comparisons)
• 2G12: The antiviral response to intravenously administered MAbs 2F5 and 2G12 was evaluated in 7 HAART-naïve asymptomatic HIV-1 infected patients during a treatment period of 28 days. MAb therapy reduced plasma HIV RNA in 3/7 patients during the treatment period, and transiently reduced viral load in two more. CD4 counts were up in 3/7 through day 28, and transiently increased in three more. Vigorous complement activation was observed after 48/56 Ab infusions. Virus derived from 2/7 patients could be neutralized by 2G12, and escape from 2G12 was observed in both cases after infusion; one year after the infusion, isolates were again sensitive to 2G12. Stiegler2002 (complement, variant cross-reactivity, escape, immunotherapy)
• 2G12: Env genes derived from uncultured brain biopsy samples from four HIV-1 infected patients with late-stage AIDS were compared to env genes from PBMC samples. Brain isolates did not differ in the total number or positions of N-glycosylation sites, patterns of coreceptor usage, or ability to be recognized by gp160 and gp41 MAbs. 2G12 was the only MAb tested to recognize all blood and brain isolates from all four patients by gp120 immunoprecipitation. Ohagen2003 (variant cross-reactivity)
• 2G12: AC10 is a subject who was given treatment early after infection, and had a viral rebound after cessation of therapy, which then declined to a low level. The polyclonal sera from AC10 could potently neutralize the rebound virus, and NAb escape followed with a neutralizing response against the escape variant and subsequent escape from that response. Viral loads remained low in this subject despite escape. The rebound isolate that was potently neutralized by autologous sera was not particularly neutralization sensitive, as it resisted neutralization by sCD4 and MAbs IgG1b12, 2G12 and 2F5, and was only moderately sensitive to sera from other HIV+ individuals that had high titers of NAbs to TCLA strains. Montefiori2003 (acute/early infection, escape)
• 2G12: Polyclonal Abs raised against soluble trivalently linked N35CCG-N13 and N34CCG, the internal trimeric core of the coiled-coil ectodomain, inhibit HIV-1 Env-mediated cell fusion at levels comparable to 2G12. Louis2003 (vaccine antigen design)
• 2G12: Thermodynamics of binding to gp120 was measured using isothermal titration calorimetry for sCD4, 17b, b12, 48d, F105, 2G12 and C11 to intact YU2 and the HXBc2 core. The free energy of binding was similar, except for 2G12, which might not have bound well to the carbohydrate additions on the Drosophila expressed core. Enthalpy and entropy changes were divergent, but compensated. Not only CD4 but MAb ligands induced thermodynamic changes in gp120 that were independent of whether the core or the full gp120 protein was used. Non-neutralizing CD4BS and CD4i MAbs (17b, 48d, 1.5e, b6, F105 and F91) had large entropy contributions to free energy (mean: 26.1 kcal/mol) of binding to the gp120 monomer, but the potent CD4BS neutralizing MAb b6 had a much smaller value of 5.7 kcal/mol. The high values suggest surface burial or protein folding an ordering of amino acids. 2G12 had an entropy value of -1.6. These results suggest that while the trimeric Env complex has four surfaces, a non-neutralizing face (occluded on the oligomer), a variable face, a neutralizing face and a silent face (protected by carbohydrate masking), gp120 monomers further protect receptor binding sites by conformational or entropic masking, requiring a large energy handicap for Ab binding not faced by other anti-gp120 Abs. Kwong2002 (antibody binding site)
• 2G12: MAbs IgG1b12, 2G12, 2F5 and 4E10 were tested for their ability to neutralize two primary HIV-1 clade A isolates (UG/92/031 and UG/92/037) and two primary HIV-1 clade D isolates (UG/92/001 and UG/92/005). 4E10 demonstrated the most potent cross-neutralization activity. Quadruple administration of MAbs IgG1b12, 2G12, 2F5, and 4E10 induced strong synergistic neutralization of 4 clade A isolates (UG/92/031, UG/92/037, RW/92/020 and RW/92/025) as well as 5 clade D isolates (UG/92/001,UG/9/005, /93/086/RUG/94/108, UG/94/114). The authors note this combination of 4 MAbs neutralizes primary HIV A, B, C, and D isolates. Kitabwalla2003 (antibody interactions, immunoprophylaxis, variant cross-reactivity, mother-to-infant transmission, subtype comparisons)
• 2G12: This paper shows that binding of CD4BS MAbs to Env blocks the conformational shift that allows co-receptor CCR5 binding and CD4-independent mediated cell fusion. CD4BS MAbs IgG1b12, F91 and F105 and their Fab counterparts (except for C11, used as a negative control) inhibited CD4-independent JR-FL and YU-2 gp120-CCR5 binding to CCR5-expressing Cf2Th cells and syncytium formation. The carbohydrated binding MAb 2G12 also inhibited CD4-independent syncytium formation. Raja2003 (co-receptor)
• 2G12: To begin to design vaccine antigens that can mimic the carbohydrate structure, the gp120 peptide 336-342 was synthesized with Man(9), Man(6), and Man(5) moieties attached. Singh2003 (vaccine antigen design)
• 2G12: Review of current neutralizing antibody-based HIV vaccine candidates and strategies of vaccine design. Strategies for targeting of the epitopes for NAbs 2F5, 2G12, 4E10, b12, and Z13 are described. They have shown that both N-glycans, at 295N and 332N are required for 2G12 binding, emphasizing the oligosaccharide cluster nature of the epitope, and suggest the uniqueness of the target structure may not result in autoimmune reactions. Wang2003 (vaccine antigen design, review)
• 2G12: Most plasma samples of patients from early infection had NAb responses to early autologous viruses, and NAbs against heterologous strains tended to be delayed. Serial plasma samples were tested against serial isolates, and neutralization escape was shown to be rapid and continuous throughout infection. Autologous neutralization-susceptible and resistant viruses from four patients were tested for susceptibility to neutralizing Ab responses using MAbs 2G12, IgG1b12 and 2F5. No correlation was established, all viruses tested were susceptible to at least one of the neutralizing MAbs. Two patients that did not have an autologous NAb response also did not evolve changes in susceptibility to these MAbs, while one patient with a pattern of autologous neutralization and escape acquired a 2G12 sensitive virus at month 6, and lost IgG1b12 sensitivity at month 21. Richman2003 (autologous responses, acute/early infection, escape)
• 2G12: This review discusses the importance and function of protective antibody responses in animal model studies in the context of effective vaccine development. SHIV models have shown protection using high levels of MAbs can prevent infection, and partial protection that can influence disease course can be obtained from modest levels of NAbs. SHIV challenges studies conducted with infusions of combinations of MAbs b12, 2G12, and 2F5 are reviewed. Mascola2003a (immunoprophylaxis, review)
• 2G12: This study investigates the effects of glycosylation inhibitors on the binding between HIV-1 gp120 and mannose-binding lectin (MBL). Mannosidase I inhibitor deoxymannojirimycin (dMM) inhibits formation of complex and hybrid N-linked saccharides and yields virus with more mannose residues. dMM added during viral production significantly enhanced the binding 2F5 and 2G12, but not IgG1b12 in a viral capture assay. Hart2003 (antibody binding site)
• 2G12: UK1-br and MACS2-br are R5 isolates derived from brain tissue samples from AIDS patients with dementia and HIV-1 encephalitis; both are neurotropic, but only UK1-br induced neuronal apoptosis and high levels of syncytium formation in macrophages. UK1-br Env had a greater affinity for CCR5 than MACS-br, and required low levels of CCR5 and CD4 for cell-to-cell fusion and single round infection. PBMC infected with UK1-br and MACS2-br virus isolates were resistant to neutralization by MAb 2G12. UK1-br was more sensitive than MACS2-br to IgG1b12, 2F5 and CD4-IgG2 neutralization. Gorry2002 (brain/CSF, co-receptor)
• 2G12: Four newborn macaques were challenged with pathogenic SHIV 89.6 and given post exposure prophylaxis using a combination of NAbs 2F5, 2G12, 4E10 and IgG1b12. 2/4 treated animals did not show signs of infection, and 2/4 macaques maintained normal CD4+ T cell counts and had a lower delayed peak viremia compared to the controls. Ferrantelli2003 (immunoprophylaxis, mother-to-infant transmission)
• 2G12: A sCD4-17b single chain chimera was made that can bind to the CD4 binding site, then bind and block co-receptor interaction. This chimeric protein is a very potent neutralizing agent, more potent than IgG1b12, 2G12 or 2F5 against Ba-L infection of CCR5-MAGI cells. It has potential for prophylaxis or therapy. Dey2003 (co-receptor)
• 2G12:The MAb B4e8 binds to the base of the V3 loop, neutralizes multiple primary isolates and was studied for interaction with other MAbs. B4e8 and 2G12 enhanced each other's binding, and gave synergistic neutralization. B4e8 could neutralize R5X4 virus 92HT593 better than 2G12, while 2G12 was better at neutralizing R5 virus 92US660. Cavacini2003 (antibody interactions)
• 2G12: This study examined Ab interactions, binding and neutralization with a B clade R5 isolate (92US660) and R5X4 isolate (92HT593). Abs generally bound and neutralized the R5X4 isolate better than the R5 isolate. Anti-gp41 MAb F240 did not affect binding of 2G12 to either R5X4 and R5 isolates, and anti-V3 MAb B4a1 increased 2G12 binding to R5X4 virions but not R5. Neutralization with B4al and 2G12 was additive for the R5X4 virus, and was enhanced for the R5 virus. Cavacini2002 (antibody interactions, co-receptor, variant cross-reactivity)
• 2G12: Neutralization assays with rsCD4, MAbs, and serum samples from SHIV-infected macaques and HIV-1 infected individuals were used to characterize the antigenic properties of the env glycoprotein of six primary isolate-like or TCLA SHIV variants. 2G12 neutralized the five SHIV strains tested, HXBc2, KU2, 89.6, 89.6P and KB9, in MT-2 cells. Crawford1999 (variant cross-reactivity)
• 2G12: The SOS mutant envelope protein introduces a covalent disulfide bond between gp120 surface and gp41 transmembrane proteins into the R5 isolate JR-FL by adding cysteines at residues 501 and 605. Pseudovirions bearing this protein bind to CD4 and co-receptor bearing cells, but do not fuse until treatment with a reducing agent, and are arrested prior to fusion after CD4 and co-receptor engagement. 2G12 is able to neutralize both the wildtype and SOS protein comparably, but 2G12 could not neutralize SOS when added post-attachment. Binley2003 (vaccine antigen design)
• 2G12: IgG1b12 neutralized many South African (5/8) and Malawian (4/8) clade C primary HIV-1 isolates, being more effective than 2F5 which neutralized only two Malawian and no South African isolates. 2G12 did not neutralize any of the 16 isolates. Bures2002 (subtype comparisons)
• 2G12: SOS-Env is a mutant protein engineered to have a disulfide bond between gp120 and gp41. Cells expressing SOS-Env due not fuse with target cells expressing CD4 and CCR5, although the fusion process proceeds to an intermediate state associated with CD4 and co-receptors, prior to the formation of the six helix bundle that allows fusion.2G12 was used to monitor surface expression of SOS-Env compared to wildtype. Abrahamyan2003b (co-receptor, vaccine antigen design)
• 2G12: 2G12 was used as a positive control to test for a NAb activity in mice intranasally immunized with gp120 or gp140 with IL-12 and Cholera Toxin B. Albu2003
• 2G12: NIH AIDS Research and Reference Reagent Program: 1476.
• 2G12: UK Medical Research council AIDS reagent: ARP3030.
• 2G12: CD4BS MAbs b12 (neutralizing) and 205-42-15, 204-43-1, 205-46-9 (non-neutralizing) all cross-competed for binding to monomeric gp120, indicating the topological proximity of their epitopes, however, the non-neutralizing CD4BS MAbs did not interfere with the neutralization activity of MAb b12 -- 2G12 was used to normalize and as a control in these experiments. Herrera2003 (antibody interactions)
• 2G12: Alanine scanning mutagenesis was used to compare substitutions that affected anti-CD4BS NAb b12 -- rec gp120s were engineered to contain combinations of Alanine substitutions that enhanced b12 binding, and while binding of b12 to these gp120 monomers was generally maintained or increased, binding by five non-neutralizing anti-CD4bs MAbs (b3, b6, F105, 15e, and F91) was reduced or completely abolished -- 2G12 binding was largely unperturbed, indicating these proteins were not grossly misfolded. Pantophlet2003 (antibody binding site)
• 2G12: Review of NAbs that discusses mechanisms of neutralization, passive transfer of NAbs and protection in animal studies, and vaccine strategies. Liu2002 (review)
• 2G12: Review of NAbs that notes 2G12 alone or in combination with other MAbs can protect some macaques against SHIV infection, that it has strong ADCC activity, and that it is safe and well tolerated in humans. Ferrantelli2002 (immunoprophylaxis)
• 2G12: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002 (antibody binding site)
• 2G12: Rhesus macaques were better protected from vaginal challenge with SHIV89.6D (MAb 2G12, 2/4; MAbs 2F5/2G12, 2/5; and HIVIG/2F5/2G12, 4/5 infected) than from intravenous challenge (MAb 2G12, 0/3; MAbs 2F5/2G12, 1/3; and HIVIG/2F5/2G12, 3/6 infected)-- the animals that were infected by vaginal challenge after Ab infusion had low or undetectable viral RNA levels and modest CD4 T-cell decline. Mascola2002 (genital and mucosal immunity, immunoprophylaxis)
• 2G12: HIV-1 gp160deltaCT (cytoplasmic tail-deleted) proteoliposomes (PLs) containing native, trimeric envelope glycoproteins from R5 strains YU2 and JRFL, and X4 strain HXBc2, were made in a physiologic membrane setting as candidate immunogens for HIV vaccines -- 2F5 bound to gp160deltaCT with a reconstituted membrane ten-fold better than the same protein on beads, while such an affinity difference was not seen with F105 and 2G12 -- anti-CD4BS MAbs IgG1b12 and F105, A32 (C1-C4), C11 (C1-C5), and 39F (V3) MAbs bound gp160deltaCT PLs indistinguishably from gp160deltaCT expressed on the cell surface. Grundner2002 (antibody binding site, vaccine antigen design)
• 2G12: Truncation of the gp41 cytoplasmic domain of X4, R5, and X4R5 viruses forces a conformation that more closely resembles the CD4 bound state of the external Envelope, enhancing binding of CD4i MAbs 17b and 48d and of CD4BS MAbs F105, b12, and in most cases of glycosylation site dependent MAb 2G12 and the anti-gp41 MAb 246D -- in contrast, binding of the anti-V2 MAb 697D and the anti-V3 MAb 694/98D were not affected -- viruses bearing the truncation were more sensitive to neutralization by MAbs 48d, b12, and 2G12 -- the anti-C5 MAb 1331A was used to track levels of cell surface expression of the mutated proteins. EdwardsBH2002 (antibody binding site)
• 2G12: A modified gp140 (gp140deltaCFI), with C-term mutations intended to mimic a fusion intermediate and stabilize trimer formation, retained antigenic conformational determinants as defined by binding to CD4 and to MAbs 2F5, 2G12, F105, and b12, and enhanced humoral immunity without diminishing the CTL response in mice injected with a DNA vaccine. Chakrabarti2002 (vaccine antigen design)
• 2G12: Passive immunization of neonate macaques with a combination of F105+2G12+2F5 conferred complete protection against oral challenge with SHIV-vpu+ or -- the combination b12+2G12+2F5 conferred partial protection against SHIV89.6 -- such combinations may be useful for prophylaxis at birth and against milk born transmission -- the synergistic combination of IgG1b12, 2G12, 2F5, and 4E10 neutralized a collection of HIV clade C primary isolates. Xu2002 (antibody interactions, immunoprophylaxis, mother-to-infant transmission)
• 2G12: Uncleaved soluble gp140 (YU2 strain, R5 primary isolate) can be stabilized in an oligomer by fusion with a C-term trimeric GCN4 motif or using a T4 trimeric motif derived from T4 bacteriophage fibritin -- stabilized oligomer gp140 delta683(-FT) showed strong preferential recognition by NAbs IgG1b12 and 2G12 relative to the gp120 monomer, in contrast to poorly neutralizing MAbs F105, F91, 17b, 48d, and 39F which showed reduced levels of binding, and MAbs C11, A32, and 30D which did not bind the stabilized oligomer. Yang2002 (antibody binding site)
• 2G12: Ab binding characteristics of SOS gp140 were tested using SPR and RIPA -- SOS gp140 is gp120-gp41 bound by a disulfide bond -- NAbs 2G12, 2F5, IgG1b12, CD4 inducible 17b, and 19b bound to SOS gp140 better than uncleaved gp140 (gp140unc) and gp120 -- non-neutralizing MAbs 2.2B (binds to gp41 in gp140unc) and 23A (binds gp120) did not bind SOS gp140 -- 2G12 complexes with SOS gp140 or with gp120 had a very unusual linear structure. Schulke2002 (antibody binding site, vaccine antigen design)
• 2G12: Alanine scanning mutagenesis used in conjunction with competition and replacement studies of N-linked carbohydrates and sugars suggest that the 2G12 epitope is formed from mannose residues contributed by the glycans attached to N295 and N332, with the other N-linked carbohydrates in positions N339, N386, and N392 playing a role in maintaining conformation relevant to 2G12 binding -- N295A and N332A mutants showed essentially unchanged anti-CD4BS NAb b12 binding affinities, while N339A, N386A and N392A mutants displayed significantly lowered b12 affinity, presumably due to conformational changes. Scanlan2002 (antibody binding site)
• 2G12: The 2G12 epitope is composed of carbohydrates involving high-mannose and hybrid glycans of residues 295, 332, and 392, with peripheral glycans from 386 and 448 contributing on either flank, and with little direct gp120 protein surface involvement -- these mannose residues are proximal to each other near the chemokine receptor binding surface. Sanders2002 (antibody binding site)
• 2G12: The fusion process was slowed by using a suboptimal temperature (31.5 C) to re-evaluate the potential of Abs targeting fusion intermediates to block HIV entry -- preincubation of E/T cells at 31.5 C enabled polyclonal anti-N-HR Ab and anti-six-helix bundle Abs to inhibit fusion, indicating six-helix bundles form prior to fusion -- the preincubation 31.5 C step did not alter the inhibitory activity of neutralizing Abs anti-gp41 2F5, or anti-gp120 2G12, IG1b12, 48d, and 17b. GoldingH2002 (antibody binding site)
• 2G12: A phase I trial in seven HIV+ individuals was conducted with MAbs 2F5 and 2G12 -- no clinical or laboratory abnormalities were observed throughout the study -- eight infusions were administered over a 4-week period (total dose 14 g) -- the elimination half-life (t_1/2) was calculated to be 7.94 (range, 3.46--8.31) days for 2F5 and 16.48 (range, 12.84--24.85) days for 2G12. Armbruster2002 (kinetics, immunotherapy)
• 2G12: Chloroquine reduces the HIV-1-infectivity of H9 IIIB cells, apparently through altering the conformation of envelope -- there is a reduction of reactivity of 2G12 to its epitope in chloroquine treated cultures. Savarino2001 (antibody binding site)
• 2G12: Twenty HIV clade C isolates from five different countries were susceptible to neutralization by anti-clade B MAbs in a synergistic quadruple combination of mAbs IgG1b12, 2G12, 2F5, and 4E10. Xu2001 (antibody interactions, variant cross-reactivity, subtype comparisons)
• 2G12: A combination of MAbs IgG1b12, 2F5, and 2G12 was given postnatally to four neonates macaques that were then challenged with highly pathogenic SHIV89.6P -- one of the four infants remained uninfected after oral challenge, two infants had no or a delayed CD4(+) T-cell decline. HofmannLehmann2001 (immunoprophylaxis, mother-to-infant transmission)
• 2G12: A panel of 12 MAbs was used to identify those that could neutralize the dual-tropic primary isolate HIV-1 89.6 -- six gave significant neutralization at 2 to 10 ug/ml: 2F5, 50-69, IgG1b12, 447-52D, 2G12, and 670-D six did not have neutralizing activity: 654-D, 4.8D, 450-D, 246-D, 98-6, and 1281 -- no synergy, only additive effects were seen for pairwise combinations of MAbs, and antagonism was noted between gp41 MAbs 50-69 and 98-6, as well as 98-6 and 2F5. Verrier2001 (antibody interactions)
• 2G12: A luciferase-reporter gene-expressing T-cell line was developed to facilitate neutralization and drug-sensitivity assays -- luciferase and p24 antigen neutralization titer end points were found comparable using NAb from sera from HIV+ donors, and MAbs 2F5, 2G12 and IgG1b12. Spenlehauer2001 (assay or method development)
• 2G12: Neutralizing synergy between MAbs 1b12, 2G12 and 2F5 was studied using surface plasmon resonance to determine the binding kinetics for these three MAbs with respect to monomeric and oligomeric Env protein gp160 IIIB -- the 2G12 epitope is highly accessible on both monomeric and oligomeric Envs, 1b12 is highly accessible on monomers but not oligomers, and 2F5 on neither form -- binding of 2G12 exposes the 2F5 epitope on gp160 oligomers -- 2G12-gp160 oligomer interactions were best fitted to a two state model, with the first complex having a high association constant and fast dissociation, stabilized by conformational changes induced by the binding of a second MAb. ZederLutz2001 (antibody binding site, antibody interactions, kinetics)
• 2G12: Structural aspects of the interaction of neutralizing Abs with HIV-1 Env are reviewed -- Env essentially has three faces, one is largely inaccessible on the native trimer, and two that exposed but have low immunogenicity on primary viruses -- neutralization is suggested to occur by inhibition of the interaction between gp120 and the target cell membrane receptors as a result of steric hindrance and it is noted that the attachment of approximately 70 IgG molecules per virion is required for neutralization, which is equivalent to about one IgG molecule per spike -- the 2G12, 17b and b12 epitopes are discussed in detail -- although it is potently neutralizing, 2G12 does not interfere with CD4 and coreceptor binding, and this Ab specificity is uncommon in sera from HIV-1-infected individuals. Poignard2001 (antibody binding site, review)
• 2G12: Moore and colleagues review structural aspects of gp120 and how they relate to antigenic domains, and review the data concerning the lack of a clear relationship between genetic subtype and serotype -- an exception exists for human MAb 2G12, which does not recognize CRF01 envelopes because of an unusual additional disulfide bond in the V4 loop region that appears to be unique to the subtype E, CRF01 gp120 protein. Moore2001 (antibody binding site, review)
• 2G12: SF162DeltaV2 is a virus that has a 30 amino acids deletion in the V2 loop that does not abrogate its infectivity but renders it highly susceptible to neutralization -- when incorporated into a codon-optimized DNA vaccine with a CMV promoter and delivered by gene gun, SF162DeltaV2 gave higher neutralizing Ab titers against SF162 than did SF162 itself, and Abs that cross-neutralized non-homologous primary isolates were obtained only when SF162DeltaV2, but not intact SF162, was used as the immunogen -- Control MAbs 2F5 and 2G12 could neutralize all of the following primary isolates: 91US056(R5), 92US714(R5), 92US660(R5), 92HT593(R5X4), and BZ167(R5X4), while after the first protein boost, the sera from two SF162DeltaV2 immunized macaques could neutralize 91US056(R5), 92US714(R5), 92US660(R5) and ADA(R5), but not 92HT593(R5X4) or 92US657(R5) -- the pattern of cross-recognition shifted after the second boost. Barnett2001a (vaccine antigen design)
• 2G12: Review of studies in macaques that have shown immune control of pathogenic SHIV viremia, improved clinical outcome, and protection, and the implications of the observations for HIV vaccines. Mascola2001 (review)
• 2G12: Neutralization synergy between anti-HIV NAbs b12, 2G12, 2F5, and 4E10 was studied -- a classic fixed-ratio method was used, as well as a method where one Ab was fixed at a low neutralization titer and the other was varied -- using primary isolates, a two-four fold enhancement of neutralization was observed with MAb pairs, and a ten-fold enhancement with a quadruple Ab combination -- no synergy was observed with any MAb pair in the neutralization of TCLA strain HXB2 -- there was no evidence for cooperativity of binding between b12 and 2G12 to envelope spikes expressed on the cell surface of TCLA or primary isolates. Zwick2001c (antibody interactions)
• 2G12: SHIV-HXBc2 is a neutralization sensitive non-pathogenic virus, and several in vivo passages through monkey's yielded highly pathogenic SHIV KU-1 -- HXBc2 and the KU-1 clone HXBc2P3.2 differ in 12 amino acids in gp160 -- substitutions in both gp120 and gp41 reduced the ability of sCD4, IgG1b12, F105 and AG1121 to Env achieve saturation and full occupancy, and neutralize KU-1 -- 17b and 2F5 also bound less efficiently to HXBc2P3.2, although 2G12 was able to bind both comparably. Si2001
• 2G12: Six mutations in MN change the virus from a high-infectivity neutralization resistant phenotype to low-infectivity neutralization sensitive -- V3, CD4BS, and CD4i MAbs are 20-100 fold more efficient at neutralizing the sensitive form -- 2G12 was an exception and could not neutralize MN in either form. Park2000
• 2G12: To determine the antigenicity of virus killed by thermal and chemical inactivation, retention of conformation-dependent neutralization epitopes was examined, and exposure of CD4BS epitopes was found to be enhanced (MAbs IgG1b12, 205-46-9, and 205-43-1) -- binding to 2G12 and 447-52D epitopes was essentially unaltered -- the 17b CD4i epitope was also exposed. Grovit-Ferbas2000 (vaccine antigen design)
• 2G12: A triple combination of 2F5, F105 and 2G12 effectively neutralized perinatal infection of macaque infants when challenged with SHIV-vpu+ -- the mean plasma half-life was 14.0 +/- 7.9 days, the longest of the three Abs. Baba2000 (immunoprophylaxis, mother-to-infant transmission)
• 2G12: A mini-review of observations of passive administration of IgG NAbs conferring protection against intervenous or vaginal SHIV challenge, that considers why IgG MAbs might protect against mucosal challenge. Database note: First author "RobertGuroff" is also found as "Robert-Guroff" on annotated papers in this database. RobertGuroff2000 (genital and mucosal immunity, immunoprophylaxis, review)
• 2G12: The MAbs with the broadest neutralizing activity, IgG1b12, 2G12 and 2F5, all have high affinity for the native trimer, indicating that they were raised in an immune response to the oligomer on the virion surface rather than dissociated subunits -- a disulfide linked gp120-gp41 (SOS gp140) was created to mimic the native conformation of Env and explore its potential as an immunogen -- SOS gp140 is recognized by NAbs IgG1b12, 2G12, and CD4-IgG2, and also by anti-V3 MAbs 19b and 83.1 -- SOSgp140 is not recognized by C4 region MAbs that neutralize only TCLA strains, G3-42 and G3-519 -- nor did it bind C11, 23A, and M90, MAbs that bind to gp120 C1 and C5, where it interacts with gp41 -- MAbs that bind CD4 inducible epitopes, 17b and A32 were very strongly induced by CD4 in SOS gp140 -- anti-gp41 MAbs that bind in the region that interacts with gp120, 7B2, 2.2B, T4, T15G1 and 4D4, did not bind to SOSgp140, in contrast to 2F5, which binds to the only gp41 epitope that is well exposed in native gp120-gp41 complexes. Binley2000 (antibody binding site, vaccine antigen design)
• 2G12: Because HIV-1 is most often transmitted across mucosal surfaces, the ability of passive transfer of infused HIVIG/2F5/2G12 to protect against mucosal exposure of macaques to pathogenic SHIV 89.6PD was studied -- HIVIG/2F5/2G12 protected 4/5 animals against vaginal challenge, 2F5/2G12 combined protected 2/5 animals, and 2G12 alone protected 2/4 animals -- in contrast, Mascola and co-workers had previously shown single MAbs could not protect against intervenous challenge -- Ab treated animals that got infected through vaginal inoculation had low viral loads and only modest declines in CD4 counts -- the infused Abs were detected in the nasal, vaginal, and oral mucosa. Mascola2000a (genital and mucosal immunity, immunoprophylaxis)
• 2G12: Combinations of HIVIG, 2F5, 2G12 were administered in passive-transfer experiments 24 hours prior to challenge with pathogenic SHIV 89.6PD -- 3/6 animals given HIVIG/2F5/2G12 were completely protected, the others had reduced viremia and normal CD4 counts -- 1/3 monkeys given 2F5/2G12 showed transient infection, the other two had reduced viral load -- all monkeys that received HIVIG, 2F5, or 2G12 alone became infected and developed high-level plasma viremia, although animals that got HIVIG or 2G12 had a less profound CD4 T cell decline. Mascola1999 (antibody interactions)
• 2G12: Review of the neutralizing Ab response to HIV-1. Parren1999 (review)
• 2G12: Hu-PBL-SCID mice were infected with HIV-1s JRCSF and SF162 to study the effect of NAbs on an established infection -- no significant differences in the initial rate of decrease in viral load or the plateau levels of viral RNA between the b12 treated and control mice were seen -- in most of the Ab treated mice b12 escape mutants were observed with varying patterns of mutations -- a combination of b12, 2G12 and 2F5 protected 1/3 mice, and an isolate from one of the other two was resistant to neutralization by all three MAbs. Poignard1999 (antibody interactions, escape)
• 2G12: A Semliki Forest virus (SFV) expression system carrying BX08 Env was used to study the conformation of gp120 Env -- intracytoplasmic gp120 was recognized by the anti-V3 MAbs K24 and F5.5, while gp120 at the plasma membrane was detected only by conformation dependent MAbs 2G12, 670-D and 694/98D and not V3 MAbs -- expression in rat brain also showed that surface expressed Env was recognized only by the conformation-dependent Abs and not by anti-V3 Abs. Altmeyer1999
• 2G12: rgp120 derived from a R5X4 subtype B virus was used to vaccinate healthy volunteers and the resulting sera were compared with sera from HIV-1 positive subjects and neutralizing MAbs -- 2G12 was able to bind with low affinity to the rgp120 monomer HIV-1 W61D. Beddows1999
• 2G12: A meeting summary presented results regarding neutralization --MAbs 2G12 and 2F5 tested for their ability to neutralize primary isolate infection of genetically engineered cell lines (cMAGI and others, presented by T. Matthews, A. Trkola, J. Bradac) -- an advantage of such cells lines over PBMCs is that markers (X-Gal) can be added for staining to simplify the assay -- the consensus of the meeting was that these engineered cell lines did not improve the sensitivity of detection of primary isolate neutralization -- D. Burton and J. Mascola presented results concerning passive immunization and protection of hu-PBL-SCID mice and macaques, respectively, and both found combinations of MAbs that were able to achieve 99% neutralization in vitro corresponded to efficacy in vivo. Montefiori1999 (review)
• 2G12: Infection of dendritic cells cultured from CD14+ blood cells or from cadaveric human skin was blocked by neutralizing MAbs IgG1b12, or 2F5 and 2G12 delivered together, but not by control non-neutralizing anti-gp120 MAb 4.8D, indicating that NAbs could interrupt early mucosal transmission events. Frankel1998 (genital and mucosal immunity)
• 2G12: In a study of the influence of the glycan at position 306 of the V3 loop on MAb recognition, 2G12 was found to neutralize an HIV-BRU mutant virus that lacks the V3 loop glycan and has a mutation at the tip of the loop more efficiently than it neutralizes HIV-BRU. Schonning1998 (antibody binding site)
• 2G12: The complete V, J and D(H) domain was sequenced -- unlike non-neutralizing anti-gp41 MAb 3D6, five neutralizing MAbs (2F5, 2G12, 1B1, 1F7, and 3D5) showed extensive somatic mutations giving evidence of persistent antigenic pressure over long periods -- 2G12 D(H) has the best homology to a D(H) segment between D3-22 and D4-23, a region not usually considered for heavy-chain rearrangement because it lacks associated recombination signals in the flanking regions, Kunert et al. suggest this may be why Abs that compete with 2G12 are rare. Kunert1998 (antibody sequence)
• 2G12: Review of the antigenic and receptor binding-domains of gp120 in relation to the structure of the molecule -- MAbs are discussed by category (anti-V2, anti-V3, CD4i, CD4BS...), however as 2G12 binds to a rarely immunogenic region, and it is dependent on glycosylation, it was discussed individually. Wyatt1998a (review)
• 2G12: Neutralization synergy was observed when the MAbs 694/98-D (V3), 2F5 (gp41), and 2G12 (gp120 discontinuous) were used in combination, and even greater neutralizing potential was seen with the addition of a fourth MAb, F105 (CD4 BS). Li1998 (antibody interactions)
• 2G12: MAbs 2G12, 2F5 and b12 are broadly neutralizing, as are some human polyconal sera, but this paper describes a set of primary isolates that are resistant to all three MAbs and 2 broadly neutralizing sera -- results indicate that resistance levels of pediatric isolates might be higher than adult isolates -- resistance in general did not seem to be conferred by a loss of binding affinity for gp120 or gp41, rather by a more global perturbation of oligomeric Envelope. Parren1998a (variant cross-reactivity)
• 2G12: Induces complement-mediated lysis in MN but not primary isolates -- primary isolates are refractive to CML. Takefman1998 (complement, variant cross-reactivity)
• 2G12: Notes that 2G12 and 2F5, potent neutralizing antibodies, were identified by screening for cell surface (oligomeric Envelope) reactivity. Fouts1998 (antibody binding site)
• 2G12: A wide range of neutralizing titers was observed that was independent of co-receptor usage. Trkola1998 (co-receptor, variant cross-reactivity)
• 2G12: A panel of MAbs were shown to bind with similar or greater affinity and similar competition profiles to a deglycosylated or variable loop deleted core gp120 protein (Delta V1, V2, and V3), thus such a core protein produces a structure closely approximating full length folded monomer -- MAb 2G12 was the only exception to this, showing reduced binding efficiency. Binley1998 (antibody binding site)
• 2G12: Does not compete with binding of MAb generated in response to gp120-CD4 complex, CG10. Sullivan1998 (antibody interactions)
• 2G12: Ab from gp120 vaccinated individuals prior to infection, who subsequently became HIV infected, could not achieve 90% neutralization of the primary virus by which the individuals were ultimately infected -- these viruses were not particularly refractive to neutralization, as determined by their susceptibility to neutralization by MAbs 2G12, IgG1b12, 2F5 and 447-52D. Connor1998
• 2G12: Enhances Hx10 binding to CD4 positive or negative HeLa cells, but inhibited binding to CD4+ T-cell line A3.01 -- neutralizes Hx10 infection of the HeLa cells. Mondor1998
• 2G12: Summary of the implications of the crystal structure of gp120 combined with what is known about mutations that reduce NAb binding -- probable mechanism of neutralization by 2G12 is unknown, but dependent on proper glycosylation and 2G12 is predicted to be oriented toward the target cell when bound, so neutralization may be due to steric hindrance -- mutations in positions N 295, T 297, S 334, N 386, N 392 and N 397 HXBc2 (IIIB) decrease 2G12 binding, and the binding region is 25 angstroms from the CD4 binding site -- probably the Ab binds in part to carbohydrates, which may account for both its broad reactivity and the scarcity of Abs in the same competition group. Wyatt1998 (antibody binding site)
• 2G12: The MAb and Fab binding to the oligomeric form of gp120 and neutralization were highly correlated -- authors suggest that neutralization is determined by the fraction of Ab sites occupied on a virion irrespective of the epitope. Parren1998 (antibody binding site)
• 2G12: Post-exposure prophylaxis was effective when MAb 694/98-D was delivered 15 min post-exposure to HIV-1 LAI in hu-PBL-SCID mice, but declined to 50% if delivered 60 min post-exposure, and similar time constraints have been observed for HIVIG, 2F5 and 2G12, in contrast to MAb BAT123 that could protect when delivered 4 hours post infection. Andrus1998 (immunoprophylaxis)
• 2G12: Neutralizes TCLA strains and primary isolates. Parren1997 (variant cross-reactivity)
• 2G12: Review that discusses this MAb -- reacts with residues at the base of the V3 loop and V4, and most of the changes that reduce binding are glycosylation sites -- it is not clear whether the binding site is peptidic or direct carbohydrate. Burton1997 (antibody binding site, review)
• 2G12: Viral binding inhibition by 2G12 was strongly correlated with neutralization (all other neutralizing MAbs tested showed some correlation except 2F5). Ugolini1997 (antibody binding site)
• 2G12: Using concentrations of Abs achievable in vivo, the triple combination of 2F5, 2G12 and HIVIG was found to be synergistic to have the greatest breadth and magnitude of response against 15 clade B primary isolates. Mascola1997 (antibody interactions, variant cross-reactivity)
• 2G12: Review: MAbs 2F5, 2G12 and IgG1b12 have potential for use in combination with CD4-IgG2 as an immunotherapeutic or immunoprophylactic -- homologous MAbs to these are rare in humans and vaccine strategies should consider including constructs that may enhance exposure of these MAbs' epitopes. Moore1997 (immunoprophylaxis, immunotherapy, review)
• 2G12: One of 14 human MAbs tested for ability to neutralize a chimeric SHIV-vpu+, which expressed HIV-1 IIIB Env -- 2G12 was a strong neutralizer of SHIV-vpu+ -- all Ab combinations tested showed synergistic neutralization -- 2G12 has synergistic response with MAbs 694/98-D (anti-V3), 2F5, F105, and b12. Li1997 (antibody interactions)
• 2G12: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 2G12 bound monomer, and weakly bound oligomer and neutralized JRFL. Fouts1997 (antibody binding site)
• 2G12: A JRCSF variant that was selected for IgG1b12 resistance remained sensitive to MAbs 2G12 and 2F5, for combination therapy. Mo1997 (escape)
• 2G12: In a multilab evaluation of monoclonal antibodies, only IgG1b12, 2G12, and 2F5 could neutralize at least half of the 9 primary test isolates at a concentration of < 25 mug per ml for 90% viral inhibition -- neutralized 6 of 9 primary isolates. DSouza1997 (variant cross-reactivity)
• 2G12: Review: Only four epitopes have been described which can stimulate a useful neutralizing response to a broad spectrum of primary isolates, represented by the binding sites of MAbs: 447-52-D, 2G12, Fab b12, and 2F5. Sattentau1996 (review)
• 2G12: Neutralizes primary isolates, HXB2, and chimeric virus with gp120 from primary isolates in an HXB2 background. McKeating1996b (variant cross-reactivity)
• 2G12: Neutralizes JR-FL -- inhibits gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study. Trkola1996b (co-receptor)
• 2G12: Review: exceptional capacity to neutralize primary isolates in terms of both breadth and potency -- one of three MAbs (IgG1b12, 2G12, and 2F5) generally accepted as having significant potency against primary isolates. Poignard1996 (variant cross-reactivity, review)
• 2G12: Review: binding site is distinct from CD4BS MAbs epitope and is unique among known gp120 MAbs, human or rodent. Moore1995c (review)
• 2G12: Binding weakly enhanced by some anti-C1, -C4, -V3, and CD4 binding site MAbs -- unusual in that 2G12 binding neither enhanced or inhibited the binding of other MAbs included in the study. Moore1996 (antibody interactions)
• 2G12: Conformationally sensitive epitope destroyed by mutations altering the N-linked glycosylation sites near the base of the V3 loop and the amino-terminal flank of the V4 loop. Trkola1996 (ADCC, antibody binding site)
• 2G12: Highly potent Cross-clade neutralizing activity. Trkola1995a (subtype comparisons)
• 2G12: Human MAb generated by electrofusion of PBL from HIV-1+ volunteers with CB-F7 cells. Buchacher1994 (antibody generation)

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Beddows2005a Simon Beddows, Natalie N. Zheng, Carolina Herrera, Elizabeth Michael, Kelly Barnes, John P. Moore, Rod S. Daniels, and Jonathan N. Weber. Neutralization Sensitivity of HIV-1 Env-Pseudotyped Virus Clones is Determined by Co-Operativity between Mutations Which Modulate the CD4-Binding Site and Those That Affect gp120-gp41 Stability. Virology, 337(1):136-148, 20 Jun 2005. PubMed ID: 15914227. Show all entries for this paper.

Belanger2010 Julie M. Belanger, Yossef Raviv, Mathias Viard, Michael Jason de la Cruz, Kunio Nagashima, and Robert Blumenthal. Characterization of the Effects of Aryl-Azido Compounds and UVA Irradiation on the Viral Proteins and Infectivity of Human Immunodeficiency Virus Type 1. Photochem. Photobiol., 86(5):1099-1108, Sep-Oct 2010. PubMed ID: 20630026. Show all entries for this paper.

Berkower2008 Ira Berkower, Chiraag Patel, Yisheng Ni, Konstantin Virnik, Zhexin Xiang, and Angelo Spadaccini. Targeted Deletion in the beta20--beta21 Loop of HIV Envelope Glycoprotein gp120 Exposes the CD4 Binding Site for Antibody Binding. Virology, 377(2):330-338, 1 Aug 2008. PubMed ID: 18519142. Show all entries for this paper.

Billington2007 J. Billington, T. P. Hickling, G. H. Munro, C. Halai, R. Chung, G. G. Dodson, and R. S. Daniels. Stability of a Receptor-Binding Active Human Immunodeficiency Virus Type 1 Recombinant gp140 Trimer Conferred by Intermonomer Disulfide Bonding of the V3 Loop: Differential Effects of Protein Disulfide Isomerase on CD4 and Coreceptor Binding. J. Virol., 81(9):4604-4614, May 2007. PubMed ID: 17301129. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Binley2000 J. Binley, R. Sanders, B. Clas, N. Schuelke, A. Master, Y. Guo, F. Kajumo, D. Anselma, P. Maddon, W. Olson, and J. Moore. A Recombinant Human Immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intramolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion associated structure. J. Virol., 74:627-43, 1999. PubMed ID: 10623724. Show all entries for this paper.

Binley2003 James M. Binley, Charmagne S. Cayanan, Cheryl Wiley, Norbert Schülke, William C. Olson, and Dennis R. Burton. Redox-Triggered Infection by Disulfide-Shackled Human Immunodeficiency Virus Type 1 Pseudovirions. J. Virol., 77(10):5678-5684, May 2003. PubMed ID: 12719560. Show all entries for this paper.

Binley2004 James M. Binley, Terri Wrin, Bette Korber, Michael B. Zwick, Meng Wang, Colombe Chappey, Gabriela Stiegler, Renate Kunert, Susan Zolla-Pazner, Hermann Katinger, Christos J. Petropoulos, and Dennis R. Burton. Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal Antibodies. J. Virol., 78(23):13232-13252, Dec 2004. PubMed ID: 15542675. Show all entries for this paper.

Binley2006 James M. Binley, Stacie Ngo-Abdalla, Penny Moore, Michael Bobardt, Udayan Chatterji, Philippe Gallay, Dennis R. Burton, Ian A. Wilson, John H. Elder, and Aymeric de Parseval. Inhibition of HIV Env Binding to Cellular Receptors by Monoclonal Antibody 2G12 as Probed by Fc-Tagged gp120. Retrovirology, 3:39, 2006. PubMed ID: 16817962. Show all entries for this paper.

Binley2008 James M. Binley, Elizabeth A. Lybarger, Emma T. Crooks, Michael S. Seaman, Elin Gray, Katie L. Davis, Julie M. Decker, Diane Wycuff, Linda Harris, Natalie Hawkins, Blake Wood, Cory Nathe, Douglas Richman, Georgia D. Tomaras, Frederic Bibollet-Ruche, James E. Robinson, Lynn Morris, George M. Shaw, David C. Montefiori, and John R. Mascola. Profiling the Specificity of Neutralizing Antibodies in a Large Panel of Plasmas from Patients Chronically Infected with Human Immunodeficiency Virus Type 1 Subtypes B and C. J. Virol., 82(23):11651-11668, Dec 2008. PubMed ID: 18815292. Show all entries for this paper.

Binley2009 James Binley. Specificities of Broadly Neutralizing Anti-HIV-1 Sera. Curr. Opin. HIV AIDS, 4(5):364-372, Sep 2009. PubMed ID: 20048699. Show all entries for this paper.

Binley2010 James M Binley, Yih-En Andrew Ban, Emma T. Crooks, Dirk Eggink, Keiko Osawa, William R. Schief, and Rogier W. Sanders. Role of Complex Carbohydrates in Human Immunodeficiency Virus Type 1 Infection and Resistance to Antibody Neutralization. J. Virol., 84(11):5637-5655, Jun 2010. PubMed ID: 20335257. Show all entries for this paper.

Biorn2004 Alyssa C. Biorn, Simon Cocklin, Navid Madani, Zhihai Si, Tijana Ivanovic, James Samanen, Donald I. Van Ryk, Ralph Pantophlet, Dennis R. Burton, Ernesto Freire, Joseph Sodroski, and Irwin M. Chaiken. Mode of Action for Linear Peptide Inhibitors of HIV-1 gp120 Interactions. Biochemistry, 43(7):1928-1938, 24 Feb 2004. PubMed ID: 14967033. Show all entries for this paper.

Blay2006 W. M. Blay, S. Gnanakaran, B. Foley, N. A. Doria-Rose, B. T. Korber, and N. L. Haigwood. Consistent Patterns of Change During the Divergence of Human Immunodeficiency Virus Type 1 Envelope from That of the Inoculated Virus in Simian/Human Immunodeficiency Virus-Infected Macaques. J. Virol., 80(2):999-1014, Jan 2006. PubMed ID: 16379001. Show all entries for this paper.

Blay2007 Wendy M. Blay, Theresa Kasprzyk, Lynda Misher, Barbra A. Richardson, and Nancy L. Haigwood. Mutations in Envelope gp120 Can Impact Proteolytic Processing of the gp160 Precursor and Thereby Affect Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Pseudoviruses. J. Virol., 81(23):13037-13049, Dec 2007. PubMed ID: 17855534. Show all entries for this paper.

Blish2007 Catherine A. Blish, Wendy M. Blay, Nancy L. Haigwood, and Julie Overbaugh. Transmission of HIV-1 in the Face of Neutralizing Antibodies. Curr. HIV Res., 5(6):578-587, Nov 2007. PubMed ID: 18045114. Show all entries for this paper.

Blish2009 Catherine A. Blish, Zahra Jalalian-Lechak, Stephanie Rainwater, Minh-An Nguyen, Ozge C. Dogan, and Julie Overbaugh. Cross-Subtype Neutralization Sensitivity Despite Monoclonal Antibody Resistance among Early Subtype A, C, and D Envelope Variants of Human Immunodeficiency Virus Type 1. J. Virol., 83(15):7783-7788, Aug 2009. PubMed ID: 19474105. Show all entries for this paper.

Bontjer2009 Ilja Bontjer, Aafke Land, Dirk Eggink, Erwin Verkade, Kiki Tuin, Chris Baldwin, Georgios Pollakis, William A. Paxton, Ineke Braakman, Ben Berkhout, and Rogier W. Sanders. Optimization of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins with V1/V2 Deleted, Using Virus Evolution. J. Virol., 83(1):368-383, Jan 2009. PubMed ID: 18922866. Show all entries for this paper.

Bontjer2010 Ilja Bontjer, Mark Melchers, Dirk Eggink, Kathryn David, John P. Moore, Ben Berkhout, and Rogier W. Sanders. Stabilized HIV-1 Envelope Glycoprotein Trimers Lacking the V1V2 Domain, Obtained by Virus Evolution. J. Biol. Chem, 285(47):36456-36470, 19 Nov 2010. PubMed ID: 20826824. Show all entries for this paper.

Borggren2011 Marie Borggren, Johanna Repits, Jasminka Sterjovski, Hannes Uchtenhagen, Melissa J. Churchill, Anders Karlsson, Jan Albert, Adnane Achour, Paul R. Gorry, Eva Maria Fenyö, and Marianne Jansson. Increased Sensitivity to Broadly Neutralizing Antibodies of End-Stage Disease R5 HIV-1 Correlates with Evolution in Env Glycosylation and Charge. PLoS One, 6(6):e20135, 2011. PubMed ID: 21698221. Show all entries for this paper.

Bouvin-Pley2014 M. Bouvin-Pley, M. Morgand, L. Meyer, C. Goujard, A. Moreau, H. Mouquet, M. Nussenzweig, C. Pace, D. Ho, P. J. Bjorkman, D. Baty, P. Chames, M. Pancera, P. D. Kwong, P. Poignard, F. Barin, and M. Braibant. Drift of the HIV-1 Envelope Glycoprotein gp120 Toward Increased Neutralization Resistance over the Course of the Epidemic: A Comprehensive Study Using the Most Potent and Broadly Neutralizing Monoclonal Antibodies. J. Virol., 88(23):13910-13917, Dec 2014. PubMed ID: 25231299. Show all entries for this paper.

Bowley2007 D. R. Bowley, A. F. Labrijn, M. B. Zwick, and D. R. Burton. Antigen Selection from an HIV-1 Immune Antibody Library Displayed on Yeast Yields Many Novel Antibodies Compared to Selection from the Same Library Displayed on Phage. Protein Eng. Des. Sel., 20(2):81-90, Feb 2007. PubMed ID: 17242026. Show all entries for this paper.

Braibant2006 Martine Braibant, Sylvie Brunet, Dominique Costagliola, Christine Rouzioux, Henri Agut, Hermann Katinger, Brigitte Autran, and Francis Barin. Antibodies to Conserved Epitopes of the HIV-1 Envelope in Sera from Long-Term Non-Progressors: Prevalence and Association with Neutralizing Activity. AIDS, 20(15):1923-30, 3 Oct 2006. PubMed ID: 16988513. Show all entries for this paper.

Braibant2013 Martine Braibant, Eun-Yeung Gong, Jean-Christophe Plantier, Thierry Moreau, Elodie Alessandri, François Simon, and Francis Barin. Cross-Group Neutralization of HIV-1 and Evidence for Conservation of the PG9/PG16 Epitopes within Divergent Groups. AIDS, 27(8):1239-1244, 15 May 2013. PubMed ID: 23343910. Show all entries for this paper.

Bricault2019 Christine A. Bricault, Karina Yusim, Michael S. Seaman, Hyejin Yoon, James Theiler, Elena E. Giorgi, Kshitij Wagh, Maxwell Theiler, Peter Hraber, Jennifer P. Macke, Edward F. Kreider, Gerald H. Learn, Beatrice H. Hahn, Johannes F. Scheid, James M. Kovacs, Jennifer L. Shields, Christy L. Lavine, Fadi Ghantous, Michael Rist, Madeleine G. Bayne, George H. Neubauer, Katherine McMahan, Hanqin Peng, Coraline Chéneau, Jennifer J. Jones, Jie Zeng, Christina Ochsenbauer, Joseph P. Nkolola, Kathryn E. Stephenson, Bing Chen, S. Gnanakaran, Mattia Bonsignori, LaTonya D. Williams, Barton F. Haynes, Nicole Doria-Rose, John R. Mascola, David C. Montefiori, Dan H. Barouch, and Bette Korber. HIV-1 Neutralizing Antibody Signatures and Application to Epitope-Targeted Vaccine Design. Cell Host Microbe, 25(1):59-72.e8, 9 Jan 2019. PubMed ID: 30629920. Show all entries for this paper.

Brown2005a Bruce K. Brown, Janice M. Darden, Sodsai Tovanabutra, Tamara Oblander, Julie Frost, Eric Sanders-Buell, Mark S. de Souza, Deborah L. Birx, Francine E. McCutchan, and Victoria R. Polonis. Biologic and Genetic Characterization of a Panel of 60 Human Immunodeficiency Virus Type 1 Isolates, Representing Clades A, B, C, D, CRF01\_AE, and CRF02\_AG, for the Development and Assessment of Candidate Vaccines. J. Virol., 79(10):6089-6101, May 2005. PubMed ID: 15857994. Show all entries for this paper.

Brown2012 Bruce K. Brown, Lindsay Wieczorek, Gustavo Kijak, Kara Lombardi, Jeffrey Currier, Maggie Wesberry, John C. Kappes, Viseth Ngauy, Mary Marovich, Nelson Michael, Christina Ochsenbauer, David C Montefiori, and Victoria R. Polonis. The Role of Natural Killer (NK) Cells and NK Cell Receptor Polymorphisms in the Assessment of HIV-1 Neutralization. PLoS One, 7(4):e29454, 2012. PubMed ID: 22509241. Show all entries for this paper.

Bunnik2007 Evelien M Bunnik, Esther D Quakkelaar, Ad C. van Nuenen, Brigitte Boeser-Nunnink, and Hanneke Schuitemaker. Increased Neutralization Sensitivity of Recently Emerged CXCR4-Using Human Immunodeficiency Virus Type 1 Strains Compared to Coexisting CCR5-Using Variants from the Same Patient. J. Virol., 81(2):525-531, Jan 2007. PubMed ID: 17079299. Show all entries for this paper.

Bunnik2009 Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Ad C. van Nuenen, and Hanneke Schuitemaker. Changing Sensitivity to Broadly Neutralizing Antibodies b12, 2G12, 2F5, and 4E10 of Primary Subtype B Human Immunodeficiency Virus Type 1 Variants in the Natural Course of Infection. Virology, 390(2):348-355, 1 Aug 2009. PubMed ID: 19539340. Show all entries for this paper.

Bunnik2010 Evelien M. Bunnik, Marit J. van Gils, Marilie S. D. Lobbrecht, Linaida Pisas, Nening M. Nanlohy, Debbie van Baarle, Ad C. van Nuenen, Ann J. Hessell, and Hanneke Schuitemaker. Emergence of Monoclonal Antibody b12-Resistant Human Immunodeficiency Virus Type 1 Variants during Natural Infection in the Absence of Humoral Or Cellular Immune Pressure. J. Gen. Virol., 91(5):1354-1364, May 2010. PubMed ID: 20053822. Show all entries for this paper.

Bunnik2010a Evelien M. Bunnik, Zelda Euler, Matthijs R. A. Welkers, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Adaptation of HIV-1 Envelope gp120 to Humoral Immunity at a Population Level. Nat. Med., 16(9):995-997, Sep 2010. PubMed ID: 20802498. Show all entries for this paper.

Bures2002 Renata Bures, Lynn Morris, Carolyn Williamson, Gita Ramjee, Mark Deers, Susan A Fiscus, Salim Abdool-Karim, and David C. Montefiori. Regional Clustering of Shared Neutralization Determinants on Primary Isolates of Clade C Human Immunodeficiency Virus Type 1 from South Africa. J. Virol., 76(5):2233-2244, Mar 2002. PubMed ID: 11836401. Show all entries for this paper.

Burrer2005 Renaud Burrer, Sandrine Haessig-Einius, Anne-Marie Aubertin, and Christiane Moog. Neutralizing as Well as Non-Neutralizing Polyclonal Immunoglobulin (Ig)G from Infected Patients Capture HIV-1 via Antibodies Directed against the Principal Immunodominant Domain of gp41. Virology, 333(1):102-113, 1 Mar 2005. PubMed ID: 15708596. Show all entries for this paper.

Burton1997 D. R. Burton and D. C. Montefiori. The antibody response in HIV-1 infection. AIDS, 11 Suppl A:S87-S98, 1997. An excellent review of Ab epitopes and the implications for Envelope structure, neutralization of HIV, the distinction between primary and TCLA strains, ADCC and its role in clearance, and the Ab response during the course of infection. PubMed ID: 9451972. Show all entries for this paper.

Burton2005 Dennis R. Burton, Robyn L. Stanfield, and Ian A. Wilson. Antibody vs. HIV in a Clash of Evolutionary Titans. Proc. Natl. Acad. Sci. U.S.A., 102(42):14943-14948, 18 Oct 2005. PubMed ID: 16219699. Show all entries for this paper.

Burton2012 Dennis R. Burton, Pascal Poignard, Robyn L. Stanfield, and Ian A. Wilson. Broadly Neutralizing Antibodies Present New Prospects to Counter Highly Antigenically Diverse Viruses. Science, 337(6091):183-186, 13 Jul 2012. PubMed ID: 22798606. Show all entries for this paper.

Burton2016 Dennis R. Burton and Lars Hangartner. Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design. Annu. Rev. Immunol., 34:635-659, 20 May 2016. PubMed ID: 27168247. Show all entries for this paper.

Cai2017 Yongfei Cai, Selen Karaca-Griffin, Jia Chen, Sai Tian, Nicholas Fredette, Christine E. Linton, Sophia Rits-Volloch, Jianming Lu, Kshitij Wagh, James Theiler, Bette Korber, Michael S. Seaman, Stephen C. Harrison, Andrea Carfi, and Bing Chen. Antigenicity-Defined Conformations of an Extremely Neutralization-Resistant HIV-1 Envelope Spike. Proc. Natl. Acad. Sci. U.S.A., 114(17):4477-4482, 25 Apr 2017. PubMed ID: 28396421. Show all entries for this paper.

Calarese2003 Daniel A. Calarese, Christopher N. Scanlan, Michael B. Zwick, Songpon Deechongkit, Yusuke Mimura, Renate Kunert, Ping Zhu, Mark R. Wormald, Robyn L. Stanfield, Kenneth H. Roux, Jeffery W. Kelly, Pauline M. Rudd, Raymond A. Dwek, Hermann Katinger, Dennis R. Burton, and Ian A. Wilson. Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition. Science, 300(5628):2065-2071, 27 Jun 2003. PubMed ID: 12829775. Show all entries for this paper.

Calarese2005 Daniel A. Calarese, Hing-Ken Lee, Cheng-Yuan Huang, Michael D. Best, Rena D. Astronomo, Robyn L. Stanfield, Hermann Katinger, Dennis R. Burton, Chi-Huey Wong, and Ian A. Wilson. Dissection of the Carbohydrate Specificity of the Broadly Neutralizing Anti-HIV-1 Antibody 2G12. Proc. Natl. Acad. Sci. U.S.A., 102(38):13372-13377, 20 Sep 2005. PubMed ID: 16174734. Show all entries for this paper.

Canducci2009 Filippo Canducci, Maria Chiara Marinozzi, Michela Sampaolo, Stefano Berrè, Patrizia Bagnarelli, Massimo Degano, Giulia Gallotta, Benedetta Mazzi, Philippe Lemey, Roberto Burioni, and Massimo Clementi. Dynamic Features of the Selective Pressure on the Human Immunodeficiency Virus Type 1 (HIV-1) gp120 CD4-Binding Site in a Group of Long Term Non Progressor (LTNP) Subjects. Retrovirology, 6:4, 2009. PubMed ID: 19146663. Show all entries for this paper.

Carbonetti2014 Sara Carbonetti, Brian G. Oliver, Jolene Glenn, Leonidas Stamatatos, and D. Noah Sather. Soluble HIV-1 Envelope Immunogens Derived from an Elite Neutralizer Elicit Cross-Reactive V1V2 Antibodies and Low Potency Neutralizing Antibodies. PLoS One, 9(1):e86905, 2014. PubMed ID: 24466285. Show all entries for this paper.

Castillo-Menendez2019 Luis R. Castillo-Menendez, Hanh T. Nguyen, and Joseph Sodroski. Conformational Differences between Functional Human Immunodeficiency Virus Envelope Glycoprotein Trimers and Stabilized Soluble Trimers. J. Virol., 93(3), 1 Feb 2019. PubMed ID: 30429345. Show all entries for this paper.

Cavacini2002 Lisa A. Cavacini, Mark Duval, James Robinson, and Marshall R. Posner. Interactions of Human Antibodies, Epitope Exposure, Antibody Binding and Neutralization of Primary Isolate HIV-1 Virions. AIDS, 16(18):2409-2417, 6 Dec 2002. Erratum in AIDS. 2003 Aug 15;17(12):1863. PubMed ID: 12461414. Show all entries for this paper.

Cavacini2003 Lisa Cavacini, Mark Duval, Leslie Song, Rebecca Sangster, Shi-hua Xiang, Joseph Sodroski, and Marshall Posner. Conformational Changes in env Oligomer Induced by an Antibody Dependent on the V3 Loop Base. AIDS, 17(5):685-689, 28 Mar 2003. PubMed ID: 12646791. Show all entries for this paper.

Chaillon2011 Antoine Chaillon, Martine Braibant, Thierry Moreau, Suzie Thenin, Alain Moreau, Brigitte Autran, and Francis Barin. The V1V2 Domain and an N-Linked Glycosylation Site in the V3 Loop of the HIV-1 Envelope Glycoprotein Modulate Neutralization Sensitivity to the Human Broadly Neutralizing Antibody 2G12. J. Virol., 85(7):3642-3648, Apr 2011. PubMed ID: 21248038. Show all entries for this paper.

Chakrabarti2002 Bimal K. Chakrabarti, Wing-pui Kong, Bei-yue Wu, Zhi-Yong Yang, Jacques Friborg, Xu Ling, Steven R. King, David C. Montefiori, and Gary J. Nabel. Modifications of the Human Immunodeficiency Virus Envelope Glycoprotein Enhance Immunogenicity for Genetic Immunization. J. Virol., 76(11):5357-5368, Jun 2002. PubMed ID: 11991964. Show all entries for this paper.

Cham2006 Fatim Cham, Peng Fei Zhang, Leo Heyndrickx, Peter Bouma, Ping Zhong, Herman Katinger, James Robinson, Guido van der Groen, and Gerald V. Quinnan, Jr. Neutralization and Infectivity Characteristics of Envelope Glycoproteins from Human Immunodeficiency Virus Type 1 Infected Donors Whose Sera Exhibit Broadly Cross-Reactive Neutralizing Activity. Virology, 347(1):36-51, 30 Mar 2006. PubMed ID: 16378633. Show all entries for this paper.

Cheeseman2017 Hannah M. Cheeseman, Natalia J. Olejniczak, Paul M. Rogers, Abbey B. Evans, Deborah F. L. King, Paul Ziprin, Hua-Xin Liao, Barton F. Haynes, and Robin J. Shattock. Broadly Neutralizing Antibodies Display Potential for Prevention of HIV-1 Infection of Mucosal Tissue Superior to That of Nonneutralizing Antibodies. J. Virol., 91(1), 1 Jan 2017. PubMed ID: 27795431. Show all entries for this paper.

Chen2005 Hongying Chen, Xiaodong Xu, Alexandra Bishop, and Ian M. Jones. Reintroduction of the 2G12 Epitope in an HIV-1 Clade C gp120. AIDS, 19(8):833-835, 20 May 2005. PubMed ID: 15867500. Show all entries for this paper.

Chen2007a Hongying Chen, Xiaodong Xu, and Ian M Jones. Immunogenicity of the Outer Domain of a HIV-1 Clade C gp120. Retrovirology, 4:33, 2007. PubMed ID: 17509143. Show all entries for this paper.

Chen2008a Hongying Chen, Xiaodong Xu, Hsin-Hui Lin, Ssu-Hsien Chen, Anna Forsman, Marlen Aasa-Chapman, and Ian M. Jones. Mapping the Immune Response to the Outer Domain of a Human Immunodeficiency Virus-1 Clade C gp120. J. Gen. Virol., 89(10):2597-2604, Oct 2008. PubMed ID: 18796729. Show all entries for this paper.

Chen2009b Weizao Chen and Dimiter S. Dimitrov. Human Monoclonal Antibodies and Engineered Antibody Domains as HIV-1 Entry Inhibitors. Curr. Opin. HIV AIDS, 4(2):112-117, Mar 2009. PubMed ID: 19339949. Show all entries for this paper.

Chen2015 Jia Chen, James M. Kovacs, Hanqin Peng, Sophia Rits-Volloch, Jianming Lu, Donghyun Park, Elise Zablowsky, Michael S. Seaman, and Bing Chen. Effect of the Cytoplasmic Domain on Antigenic Characteristics of HIV-1 Envelope Glycoprotein. Science, 349(6244):191-195, 10 Jul 2015. PubMed ID: 26113642. Show all entries for this paper.

Chen2016 Danying Chen, Xiaozhou He, Jingrong Ye, Pengxiang Zhao, Yi Zeng, and Xia Feng. Genetic and Phenotypic Analysis of CRF01\_AE HIV-1 env Clones from Patients Residing in Beijing, China. AIDS Res. Hum. Retroviruses, 32(10-11):1113-1124, Nov 2016. PubMed ID: 27066910. Show all entries for this paper.

Chen2016b Yajing Chen, Richard Wilson, Sijy O'Dell, Javier Guenaga, Yu Feng, Karen Tran, Chi-I Chiang, Heather E. Arendt, Joanne DeStefano, John R. Mascola, Richard T. Wyatt, and Yuxing Li. An HIV-1 Env-Antibody Complex Focuses Antibody Responses to Conserved Neutralizing Epitopes. J. Immunol., 197(10):3982-3998, 15 Nov 2016. PubMed ID: 27815444. Show all entries for this paper.

Chenine2018 Agnes-Laurence Chenine, Melanie Merbah, Lindsay Wieczorek, Sebastian Molnar, Brendan Mann, Jenica Lee, Anne-Marie O'Sullivan, Meera Bose, Eric Sanders-Buell, Gustavo H. Kijak, Carolina Herrera, Robert McLinden, Robert J. O'Connell, Nelson L. Michael, Merlin L. Robb, Jerome H. Kim, Victoria R. Polonis, and Sodsai Tovanabutra. Neutralization Sensitivity of a Novel HIV-1 CRF01\_AE Panel of Infectious Molecular Clones. J. Acquir. Immune Defic. Syndr., 78(3):348-355, 1 Jul 2018. PubMed ID: 29528942. Show all entries for this paper.

Ching2008 Lance K. Ching, Giorgos Vlachogiannis, Katherine A. Bosch, and Leonidas Stamatatos. The First Hypervariable Region of the gp120 Env Glycoprotein Defines the Neutralizing Susceptibility of Heterologous Human Immunodeficiency Virus Type 1 Isolates to Neutralizing Antibodies Elicited by the SF162gp140 Immunogen. J. Virol., 82(2):949-956, Jan 2008. PubMed ID: 18003732. Show all entries for this paper.

Ching2010 Lance Ching and Leonidas Stamatatos. Alterations in the Immunogenic Properties of Soluble Trimeric Human Immunodeficiency Virus Type 1 Envelope Proteins Induced by Deletion or Heterologous Substitutions of the V1 Loop. J. Virol., 84(19):9932-9946, Oct 2010. PubMed ID: 20660181. Show all entries for this paper.

Choe2003 Hyeryun Choe, Wenhui Li, Paulette L. Wright, Natalya Vasilieva, Miro Venturi, Chih-Chin Huang, Christoph Grundner, Tatyana Dorfman, Michael B. Zwick, Liping Wang, Eric S. Rosenberg, Peter D. Kwong, Dennis R. Burton, James E. Robinson, Joseph G. Sodroski, and Michael Farzan. Tyrosine Sulfation of Human Antibodies Contributes to Recognition of the CCR5 Binding Region of HIV-1 gp120. Cell, 114(2):161-170, 25 Jul 2003. PubMed ID: 12887918. Show all entries for this paper.

Chomont2008 Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650. Show all entries for this paper.

Chong2008 Huihui Chong, Kunxue Hong, Chuntao Zhang, Jianhui Nie, Aijing Song, Wei Kong, and Youchun Wang. Genetic and Neutralization Properties of HIV-1 env Clones from Subtype B/BC/AE Infections in China. J. Acquir. Immune Defic. Syndr., 47(5):535-543, 15 Apr 2008. PubMed ID: 18209676. Show all entries for this paper.

Chuang2017 Gwo-Yu Chuang, Hui Geng, Marie Pancera, Kai Xu, Cheng Cheng, Priyamvada Acharya, Michael Chambers, Aliaksandr Druz, Yaroslav Tsybovsky, Timothy G. Wanninger, Yongping Yang, Nicole A. Doria-Rose, Ivelin S. Georgiev, Jason Gorman, M. Gordon Joyce, Sijy O'Dell, Tongqing Zhou, Adrian B. McDermott, John R. Mascola, and Peter D. Kwong. Structure-Based Design of a Soluble Prefusion-Closed HIV-1 Env Trimer with Reduced CD4 Affinity and Improved Immunogenicity. J. Virol., 91(10), 15 May 2017. PubMed ID: 28275193. Show all entries for this paper.

Chuang2019 Gwo-Yu Chuang, Jing Zhou, Priyamvada Acharya, Reda Rawi, Chen-Hsiang Shen, Zizhang Sheng, Baoshan Zhang, Tongqing Zhou, Robert T. Bailer, Venkata P. Dandey, Nicole A. Doria-Rose, Mark K. Louder, Krisha McKee, John R. Mascola, Lawrence Shapiro, and Peter D. Kwong. Structural Survey of Broadly Neutralizing Antibodies Targeting the HIV-1 Env Trimer Delineates Epitope Categories and Characteristics of Recognition. Structure, 27(1):196-206.e6, 2 Jan 2019. PubMed ID: 30471922. Show all entries for this paper.

Chun2014 Tae-Wook Chun, Danielle Murray, Jesse S. Justement, Jana Blazkova, Claire W. Hallahan, Olivia Fankuchen, Kathleen Gittens, Erika Benko, Colin Kovacs, Susan Moir, and Anthony S. Fauci. Broadly Neutralizing Antibodies Suppress HIV in the Persistent Viral Reservoir. Proc. Natl. Acad. Sci. U.S.A., 111(36):13151-13156, 9 Sep 2014. PubMed ID: 25157148. Show all entries for this paper.

Connor1998 R. I. Connor, B. T. Korber, B. S. Graham, B. H. Hahn, D. D. Ho, B. D. Walker, A. U. Neumann, S. H. Vermund, J. Mestecky, S. Jackson, E. Fenamore, Y. Cao, F. Gao, S. Kalams, K. J. Kunstman, D. McDonald, N. McWilliams, A. Trkola, J. P. Moore, and S. M. Wolinsky. Immunological and virological analyses of persons infected by human immunodeficiency virus type 1 while participating in trials of recombinant gp120 subunit vaccines. J. Virol., 72:1552-76, 1998. No gp120-vaccine induced antibodies in a human trial of gp120 MN and SF2 could neutralize the primary viruses that infected the vaccinees. The primary isolates from the infected vaccinees were shown not to be particularly refractive to neutralization by their susceptibility to a panel of neutralizing MAbs. PubMed ID: 9445059. Show all entries for this paper.

Corti2010 Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712. Show all entries for this paper.

Crawford1999 John M.. Crawford, Patricia L. Earl, Bernard Moss, Kieth A. Reimann, Michael S. Wyand, Kelledy H. Manson, Miroslawa Bilska, Jin Tao Zhou, C. David Pauza, Paul W. H. I. Parren, Dennis R. Burton, Joseph G. Sodroski, Norman L. Letvin, and David C. Montefiori. Characterization of Primary Isolate-Like Variants of Simian-Human Immunodeficiency Virus. J. Virol., 73(12):10199-10207, Dec 1999. PubMed ID: 10559336. Show all entries for this paper.

Crooks2005 Emma T. Crooks, Penny L. Moore, Douglas Richman, James Robinson, Jeffrey A. Crooks, Michael Franti, Norbert Schülke, and James M. Binley. Characterizing Anti-HIV Monoclonal Antibodies and Immune Sera by Defining the Mechanism of Neutralization. Hum Antibodies, 14(3-4):101-113, 2005. PubMed ID: 16720980. Show all entries for this paper.

Crooks2007 Emma T. Crooks, Penny L. Moore, Michael Franti, Charmagne S. Cayanan, Ping Zhu, Pengfei Jiang, Robbert P. de Vries, Cheryl Wiley, Irina Zharkikh, Norbert Schülke, Kenneth H. Roux, David C. Montefiori, Dennis R. Burton, and James M. Binley. A Comparative Immunogenicity Study of HIV-1 Virus-Like Particles Bearing Various Forms of Envelope Proteins, Particles Bearing no Envelope and Soluble Monomeric gp120. Virology, 366(2):245-262, 30 Sep 2007. PubMed ID: 17580087. Show all entries for this paper.

Crooks2008 Emma T. Crooks, Pengfei Jiang, Michael Franti, Sharon Wong, Michael B. Zwick, James A. Hoxie, James E. Robinson, Penny L. Moore, and James M. Binley. Relationship of HIV-1 and SIV Envelope Glycoprotein Trimer Occupation and Neutralization. Virology, 377(2):364-378, 1 Aug 2008. PubMed ID: 18539308. Show all entries for this paper.

Crooks2011 Ema T. Crooks, Tommy Tong, Keiko Osawa, and James M. Binley. Enzyme Digests Eliminate Nonfunctional Env from HIV-1 Particle Surfaces, Leaving Native Env Trimers Intact and Viral Infectivity Unaffected. J. Virol., 85(12):5825-5839, Jun 2011. PubMed ID: 21471242. Show all entries for this paper.

Crooks2015 Ema T. Crooks, Tommy Tong, Bimal Chakrabarti, Kristin Narayan, Ivelin S. Georgiev, Sergey Menis, Xiaoxing Huang, Daniel Kulp, Keiko Osawa, Janelle Muranaka, Guillaume Stewart-Jones, Joanne Destefano, Sijy O'Dell, Celia LaBranche, James E. Robinson, David C. Montefiori, Krisha McKee, Sean X. Du, Nicole Doria-Rose, Peter D. Kwong, John R. Mascola, Ping Zhu, William R. Schief, Richard T. Wyatt, Robert G. Whalen, and James M. Binley. Vaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding Site. PLoS Pathog, 11(5):e1004932, May 2015. PubMed ID: 26023780. Show all entries for this paper.

Dacheux2004 Laurent Dacheux, Alain Moreau, Yasemin Ataman-Önal, François Biron, Bernard Verrier, and Francis Barin. Evolutionary Dynamics of the Glycan Shield of the Human Immunodeficiency Virus Envelope during Natural Infection and Implications for Exposure of the 2G12 Epitope. J. Virol., 78(22):12625-12637, Nov 2004. PubMed ID: 15507649. Show all entries for this paper.

Davis2006 David Davis, Helen Donners, Betty Willems, Michel Ntemgwa, Tine Vermoesen, Guido van der Groen, and Wouter Janssens. Neutralization Kinetics of Sensitive and Resistant Subtype B Primary Human Immunodeficiency Virus Type 1 Isolates. J. Med. Virol., 78(7):864-786, Jul 2006. PubMed ID: 16721864. Show all entries for this paper.

Decamp2014 Allan deCamp, Peter Hraber, Robert T. Bailer, Michael S. Seaman, Christina Ochsenbauer, John Kappes, Raphael Gottardo, Paul Edlefsen, Steve Self, Haili Tang, Kelli Greene, Hongmei Gao, Xiaoju Daniell, Marcella Sarzotti-Kelsoe, Miroslaw K. Gorny, Susan Zolla-Pazner, Celia C. LaBranche, John R. Mascola, Bette T. Korber, and David C. Montefiori. Global Panel of HIV-1 Env Reference Strains for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 88(5):2489-2507, Mar 2014. PubMed ID: 24352443. Show all entries for this paper.

Dennison2014 S. Moses Dennison, Kara M. Anasti, Frederick H. Jaeger, Shelley M. Stewart, Justin Pollara, Pinghuang Liu, Erika L. Kunz, Ruijun Zhang, Nathan Vandergrift, Sallie Permar, Guido Ferrari, Georgia D. Tomaras, Mattia Bonsignori, Nelson L. Michael, Jerome H Kim, Jaranit Kaewkungwal, Sorachai Nitayaphan, Punnee Pitisuttithum, Supachai Rerks-Ngarm, Hua-Xin Liao, Barton F. Haynes, and S. Munir Alam. Vaccine-Induced HIV-1 Envelope gp120 Constant Region 1-Specific Antibodies Expose a CD4-Inducible Epitope and Block the Interaction of HIV-1 gp140 with Galactosylceramide. J. Virol., 88(16):9406-9417, Aug 2014. PubMed ID: 24920809. Show all entries for this paper.

Depetris2012 Rafael S Depetris, Jean-Philippe Julien, Reza Khayat, Jeong Hyun Lee, Robert Pejchal, Umesh Katpally, Nicolette Cocco, Milind Kachare, Evan Massi, Kathryn B. David, Albert Cupo, Andre J. Marozsan, William C. Olson, Andrew B. Ward, Ian A. Wilson, Rogier W. Sanders, and John P Moore. Partial Enzymatic Deglycosylation Preserves the Structure of Cleaved Recombinant HIV-1 Envelope Glycoprotein Trimers. J. Biol. Chem., 287(29):24239-24254, 13 Jul 2012. PubMed ID: 22645128. Show all entries for this paper.

Derby2006 Nina R. Derby, Zane Kraft, Elaine Kan, Emma T. Crooks, Susan W. Barnett, Indresh K. Srivastava, James M. Binley, and Leonidas Stamatatos. Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection. J. Virol., 80(17):8745-8762, Sep 2006. PubMed ID: 16912322. Show all entries for this paper.

Derking2015 Ronald Derking, Gabriel Ozorowski, Kwinten Sliepen, Anila Yasmeen, Albert Cupo, Jonathan L. Torres, Jean-Philippe Julien, Jeong Hyun Lee, Thijs van Montfort, Steven W. de Taeye, Mark Connors, Dennis R. Burton, Ian A. Wilson, Per-Johan Klasse, Andrew B. Ward, John P. Moore, and Rogier W. Sanders. Comprehensive Antigenic Map of a Cleaved Soluble HIV-1 Envelope Trimer. PLoS Pathog, 11(3):e1004767, Mar 2015. PubMed ID: 25807248. Show all entries for this paper.

deTaeye2015 Steven W. de Taeye, Gabriel Ozorowski, Alba Torrents de la Peña, Miklos Guttman, Jean-Philippe Julien, Tom L. G. M. van den Kerkhof, Judith A. Burger, Laura K. Pritchard, Pavel Pugach, Anila Yasmeen, Jordan Crampton, Joyce Hu, Ilja Bontjer, Jonathan L. Torres, Heather Arendt, Joanne DeStefano, Wayne C. Koff, Hanneke Schuitemaker, Dirk Eggink, Ben Berkhout, Hansi Dean, Celia LaBranche, Shane Crotty, Max Crispin, David C. Montefiori, P. J. Klasse, Kelly K. Lee, John P. Moore, Ian A. Wilson, Andrew B. Ward, and Rogier W. Sanders. Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-Neutralizing Epitopes. Cell, 163(7):1702-1715, 17 Dec 2015. PubMed ID: 26687358. Show all entries for this paper.

deTaeye2018 Steven W. de Taeye, Alba Torrents de la Peña, Andrea Vecchione, Enzo Scutigliani, Kwinten Sliepen, Judith A. Burger, Patricia van der Woude, Anna Schorcht, Edith E. Schermer, Marit J. van Gils, Celia C. LaBranche, David C. Montefiori, Ian A. Wilson, John P. Moore, Andrew B. Ward, and Rogier W. Sanders. Stabilization of the gp120 V3 Loop through Hydrophobic Interactions Reduces the Immunodominant V3-Directed Non-Neutralizing Response to HIV-1 Envelope Trimers. J. Biol. Chem., 293(5):1688-1701, 2 Feb 2018. PubMed ID: 29222332. Show all entries for this paper.

deTaeye2019 Steven W. de Taeye, Eden P. Go, Kwinten Sliepen, Alba Torrents de la Peña, Kimberly Badal, Max Medina-Ramírez, Wen-Hsin Lee, Heather Desaire, Ian A. Wilson, John P. Moore, Andrew B. Ward, and Rogier W. Sanders. Stabilization of the V2 Loop Improves the Presentation of V2 Loop-Associated Broadly Neutralizing Antibody Epitopes on HIV-1 Envelope Trimers. J. Biol. Chem., 294(14):5616-5631, 5 Apr 2019. PubMed ID: 30728245. Show all entries for this paper.

DeVico2007 Anthony DeVico, Timothy Fouts, George K. Lewis, Robert C. Gallo, Karla Godfrey, Manhattan Charurat, Ilia Harris, Lindsey Galmin, and Ranajit Pal. Antibodies to CD4-Induced Sites in HIV gp120 Correlate with the Control of SHIV Challenge in Macaques Vaccinated with Subunit Immunogens. Proc. Natl. Acad. Sci. U.S.A., 104(44):17477-17482, 30 Oct 2007. PubMed ID: 17956985. Show all entries for this paper.

Dey2003 Barna Dey, Christie S. Del Castillo, and Edward A. Berger. Neutralization of Human Immunodeficiency Virus Type 1 by sCD4-17b, a Single-Chain Chimeric Protein, Based on Sequential Interaction of gp120 with CD4 and Coreceptor. J. Virol., 77(5):2859-2865, Mar 2003. PubMed ID: 12584309. Show all entries for this paper.

Dey2007 Antu K. Dey, Kathryn B. David, Per J. Klasse, and John P. Moore. Specific Amino Acids in the N-Terminus of the gp41 Ectodomain Contribute to the Stabilization of a Soluble, Cleaved gp140 Envelope Glycoprotein from Human Immunodeficiency Virus Type 1. Virology, 360(1):199-208, 30 Mar 2007. PubMed ID: 17092531. Show all entries for this paper.

Dey2007a Barna Dey, Marie Pancera, Krisha Svehla, Yuuei Shu, Shi-Hua Xiang, Jeffrey Vainshtein, Yuxing Li, Joseph Sodroski, Peter D Kwong, John R Mascola, and Richard Wyatt. Characterization of Human Immunodeficiency Virus Type 1 Monomeric and Trimeric gp120 Glycoproteins Stabilized in the CD4-Bound State: Antigenicity, Biophysics, and Immunogenicity. J Virol, 81(11):5579-5593, Jun 2007. PubMed ID: 17360741. Show all entries for this paper.

Dey2008 Antu K. Dey, Kathryn B. David, Neelanjana Ray, Thomas J. Ketas, Per J. Klasse, Robert W. Doms, and John P. Moore. N-Terminal Substitutions in HIV-1 gp41 Reduce the Expression of Non-Trimeric Envelope Glycoproteins on the Virus. Virology, 372(1):187-200, 1 Mar 2008. PubMed ID: 18031785. Show all entries for this paper.

Dey2009 Barna Dey, Krisha Svehla, Ling Xu, Dianne Wycuff, Tongqing Zhou, Gerald Voss, Adhuna Phogat, Bimal K. Chakrabarti, Yuxing Li, George Shaw, Peter D. Kwong, Gary J. Nabel, John R. Mascola, and Richard T. Wyatt. Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site. PLoS Pathog, 5(5):e1000445, May 2009. PubMed ID: 19478876. Show all entries for this paper.

Dhillon2007 Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160. Show all entries for this paper.

Dieltjens2009 Tessa Dieltjens, Leo Heyndrickx, Betty Willems, Elin Gray, Lies Van Nieuwenhove, Katrijn Grupping, Guido Vanham, and Wouter Janssens. Evolution of Antibody Landscape and Viral Envelope Escape in an HIV-1 CRF02\_AG Infected Patient with 4E10-Like Antibodies. Retrovirology, 6:113, 2009. PubMed ID: 20003438. Show all entries for this paper.

Ding2015 Shilei Ding, Maxime Veillette, Mathieu Coutu, Jérémie Prévost, Louise Scharf, Pamela J. Bjorkman, Guido Ferrari, James E. Robinson, Christina Stürzel, Beatrice H. Hahn, Daniel Sauter, Frank Kirchhoff, George K. Lewis, Marzena Pazgier, and Andrés Finzi. A Highly Conserved Residue of the HIV-1 gp120 Inner Domain Is Important for Antibody-Dependent Cellular Cytotoxicity Responses Mediated by Anti-cluster A Antibodies. J. Virol., 90(4):2127-2134, Feb 2016. PubMed ID: 26637462. Show all entries for this paper.

Diomede2012 L. Diomede, S. Nyoka, C. Pastori, L. Scotti, A. Zambon, G. Sherman, C. M. Gray, M. Sarzotti-Kelsoe, and L. Lopalco. Passively Transmitted gp41 Antibodies in Babies Born from HIV-1 Subtype C-Seropositive Women: Correlation between Fine Specificity and Protection. J. Virol., 86(8):4129-4138, Apr 2012. PubMed ID: 22301151. Show all entries for this paper.

Doores2010 Katie J. Doores and Dennis R. Burton. Variable Loop Glycan Dependency of the Broad and Potent HIV-1-Neutralizing Antibodies PG9 and PG16. J. Virol., 84(20):10510-10521, Oct 2010. PubMed ID: 20686044. Show all entries for this paper.

Doores2010a Katie J. Doores, Zara Fulton, Michael Huber, Ian A. Wilson, and Dennis R. Burton. Antibody 2G12 Recognizes Di-Mannose Equivalently in Domain- and Nondomain-Exchanged Forms but Only Binds the HIV-1 Glycan Shield if Domain Exchanged. J. Virol., 84(20):10690-10699, Oct 2010. PubMed ID: 20702629. Show all entries for this paper.

Doores2010b Katie J. Doores, Camille Bonomelli, David J. Harvey, Snezana Vasiljevic, Raymond A. Dwek, Dennis R. Burton, Max Crispin, and Christopher N. Scanlan. Envelope Glycans of Immunodeficiency Virions Are Almost Entirely Oligomannose Antigens. Proc. Natl. Acad. Sci. U.S.A., 107(31):13800-13805, 3 Aug 2010. PubMed ID: 20643940. Show all entries for this paper.

Doores2010c Katie J Doores, Zara Fulton, Vu Hong, Mitul K. Patel, Christopher N. Scanlan, Mark R. Wormald, M. G. Finn, Dennis R. Burton, Ian A. Wilson, and Benjamin G. Davis. A Nonself Sugar Mimic of the HIV Glycan Shield Shows Enhanced Antigenicity. Proc. Natl. Acad. Sci. U.S.A., 107(40):17107-17112, 5 Oct 2010. PubMed ID: 20852065. Show all entries for this paper.

Doores2013 Katie J. Doores, Michael Huber, Khoa M. Le, Sheng-Kai Wang, Colleen Doyle-Cooper, Anthony Cooper, Ralph Pantophlet, Chi-Huey Wong, David Nemazee, and Dennis R. Burton. 2G12-Expressing B Cell Lines May Aid in HIV Carbohydrate Vaccine Design Strategies. J. Virol., 87(4):2234-2241, Feb 2013. PubMed ID: 23221565. Show all entries for this paper.

Doria-Rose2010 Nicole A. Doria-Rose, Rachel M. Klein, Marcus G. Daniels, Sijy O'Dell, Martha Nason, Alan Lapedes, Tanmoy Bhattacharya, Stephen A. Migueles, Richard T. Wyatt, Bette T. Korber, John R. Mascola, and Mark Connors. Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables. J. Virol., 84(3):1631-1636, Feb 2010. PubMed ID: 19923174. Show all entries for this paper.

Drummer2013 Heidi E. Drummer, Melissa K. Hill, Anne L. Maerz, Stephanie Wood, Paul A. Ramsland, Johnson Mak, and Pantelis Poumbourios. Allosteric Modulation of the HIV-1 gp120-gp41 Association Site by Adjacent gp120 Variable Region 1 (V1) N-Glycans Linked to Neutralization Sensitivity. PLoS Pathog., 9(4):e1003218, 2013. PubMed ID: 23592978. Show all entries for this paper.

DSouza1997 M. P. D'Souza, D. Livnat, J. A. Bradac, S. H. Bridges, the AIDS Clinical Trials Group Antibody Selection Working Group, and Collaborating Investigators. Evaluation of monoclonal antibodies to human immunodeficiency virus type 1 primary isolates by neutralization assays: performance criteria for selecting candidate antibodies for clinical trials. J. Infect. Dis., 175:1056-1062, 1997. Five laboratories evaluated neutralization of nine primary B clade isolates by a coded panel of seven human MAbs to HIV-1 subtype B envelope. IgG1b12, 2G12, 2F5 showed potent and broadly cross-reactive neutralizing ability; F105, 447/52-D, 729-D, 19b did not neutralize the primary isolates. PubMed ID: 9129066. Show all entries for this paper.

Du2009 Sean X. Du, Rebecca J. Idiart, Ellaine B. Mariano, Helen Chen, Peifeng Jiang, Li Xu, Kristin M. Ostrow, Terri Wrin, Pham Phung, James M. Binley, Christos J. Petropoulos, John A. Ballantyne, and Robert G. Whalen. Effect of Trimerization Motifs on Quaternary Structure, Antigenicity, and Immunogenicity of a Noncleavable HIV-1 gp140 Envelope Glycoprotein. Virology, 395(1):33-44, 5 Dec 2009. PubMed ID: 19815247. Show all entries for this paper.

Duenas-Decamp2010 Maria J. Duenas-Decamp and Paul R. Clapham. HIV-1 gp120 Determinants Proximal to the CD4 Binding Site Shift Protective Glycans That Are Targeted by Monoclonal Antibody 2G12. J. Virol., 84(18):9608-9612, Sep 2010. PubMed ID: 20610714. Show all entries for this paper.

Dunfee2007 Rebecca L. Dunfee, Elaine R. Thomas, Jianbin Wang, Kevin Kunstman, Steven M. Wolinsky, and Dana Gabuzda. Loss of the N-Linked Glycosylation Site at Position 386 in the HIV Envelope V4 Region Enhances Macrophage Tropism and Is Associated with Dementia. Virology, 367(1):222-234, 10 Oct 2007. PubMed ID: 17599380. Show all entries for this paper.

Dunlop2010 D. Cameron Dunlop, Camille Bonomelli, Fatma Mansab, Snezana Vasiljevic, Katie J. Doores, Mark R. Wormald, Angelina S. Palma, Ten Feizi, David J. Harvey, Raymond A. Dwek, Max Crispin, and Christopher N. Scanlan. Polysaccharide Mimicry of the Epitope of the Broadly Neutralizing Anti-HIV Antibody, 2G12, Induces Enhanced Antibody Responses to Self Oligomannose Glycans. Glycobiology, 20(7):812-823, Jul 2010. PubMed ID: 20181792. Show all entries for this paper.

Edmonds2010 Tara G. Edmonds, Haitao Ding, Xing Yuan, Qing Wei, Kendra S. Smith, Joan A. Conway, Lindsay Wieczorek, Bruce Brown, Victoria Polonis, John T. West, David C. Montefiori, John C. Kappes, and Christina Ochsenbauer. Replication Competent Molecular Clones of HIV-1 Expressing Renilla Luciferase Facilitate the Analysis of Antibody Inhibition in PBMC. Virology, 408(1):1-13, 5 Dec 2010. PubMed ID: 20863545. Show all entries for this paper.

EdwardsBH2002 Bradley H. Edwards, Anju Bansal, Steffanie Sabbaj, Janna Bakari, Mark J. Mulligan, and Paul A. Goepfert. Magnitude of Functional CD8+ T-Cell Responses to the Gag Protein of Human Immunodeficiency Virus Type 1 Correlates Inversely with Viral Load in Plasma. J. Virol., 76(5):2298-2305, Mar 2002. PubMed ID: 11836408. Show all entries for this paper.

Enriquez-Navas2011 Pedro M. Enríquez-Navas, Marco Marradi, Daniel Padro, Jesús Angulo, and Soledad Penadés. A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands. Chemistry, 17(5):1547-1560, 1 Feb 2011. PubMed ID: 21268157. Show all entries for this paper.

Euler2011 Zelda Euler, Evelien M. Bunnik, Judith A. Burger, Brigitte D. M. Boeser-Nunnink, Marlous L. Grijsen, Jan M. Prins, and Hanneke Schuitemaker. Activity of Broadly Neutralizing Antibodies, Including PG9, PG16, and VRC01, against Recently Transmitted Subtype B HIV-1 Variants from Early and Late in the Epidemic. J. Virol., 85(14):7236-7245, Jul 2011. PubMed ID: 21561918. Show all entries for this paper.

Falkowska2012 Emilia Falkowska, Alejandra Ramos, Yu Feng, Tongqing Zhou, Stephanie Moquin, Laura M. Walker, Xueling Wu, Michael S. Seaman, Terri Wrin, Peter D. Kwong, Richard T. Wyatt, John R. Mascola, Pascal Poignard, and Dennis R. Burton. PGV04, an HIV-1 gp120 CD4 Binding Site Antibody, Is Broad and Potent in Neutralization but Does Not Induce Conformational Changes Characteristic of CD4. J. Virol., 86(8):4394-4403, Apr 2012. PubMed ID: 22345481. Show all entries for this paper.

Feng2012 Yu Feng, Krisha McKee, Karen Tran, Sijy O'Dell, Stephen D. Schmidt, Adhuna Phogat, Mattias N. Forsell, Gunilla B. Karlsson Hedestam, John R. Mascola, and Richard T. Wyatt. Biochemically Defined HIV-1 Envelope Glycoprotein Variant Immunogens Display Differential Binding and Neutralizing Specificities to the CD4-Binding Site. J. Biol. Chem., 287(8):5673-5686, 17 Feb 2012. PubMed ID: 22167180. Show all entries for this paper.

Fenyo2009 Eva Maria Fenyö, Alan Heath, Stefania Dispinseri, Harvey Holmes, Paolo Lusso, Susan Zolla-Pazner, Helen Donners, Leo Heyndrickx, Jose Alcami, Vera Bongertz, Christian Jassoy, Mauro Malnati, David Montefiori, Christiane Moog, Lynn Morris, Saladin Osmanov, Victoria Polonis, Quentin Sattentau, Hanneke Schuitemaker, Ruengpung Sutthent, Terri Wrin, and Gabriella Scarlatti. International Network for Comparison of HIV Neutralization Assays: The NeutNet Report. PLoS One, 4(2):e4505, 2009. PubMed ID: 19229336. Show all entries for this paper.

Ferrantelli2002 Flavia Ferrantelli and Ruth M. Ruprecht. Neutralizing Antibodies Against HIV --- Back in the Major Leagues? Curr. Opin. Immunol., 14(4):495-502, Aug 2002. PubMed ID: 12088685. Show all entries for this paper.

Ferrantelli2003 Flavia Ferrantelli, Regina Hofmann-Lehmann, Robert A. Rasmussen, Tao Wang, Weidong Xu, Pei-Lin Li, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Post-Exposure Prophylaxis with Human Monoclonal Antibodies Prevented SHIV89.6P Infection or Disease in Neonatal Macaques. AIDS, 17(3):301-309, 14 Feb 2003. PubMed ID: 12556683. Show all entries for this paper.

Ferrantelli2004 Flavia Ferrantelli, Robert A. Rasmussen, Kathleen A. Buckley, Pei-Lin Li, Tao Wang, David C. Montefiori, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Complete Protection of Neonatal Rhesus Macaques against Oral Exposure to Pathogenic Simian-Human Immunodeficiency Virus by Human Anti-HIV Monoclonal Antibodies. J. Infect. Dis., 189(12):2167-2173, 15 Jun 2004. PubMed ID: 15181562. Show all entries for this paper.

Ferrantelli2004a Flavia Ferrantelli, Moiz Kitabwalla, Robert A. Rasmussen, Chuanhai Cao, Ting-Chao Chou, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Yun Bai, Joseph Cotropia, Kenneth E. Ugen, and Ruth M. Ruprecht. Potent Cross-Group Neutralization of Primary Human Immunodeficiency Virus Isolates with Monoclonal Antibodies--Implications for Acquired Immunodeficiency Syndrome Vaccine. J. Infect. Dis., 189(1):71-74, 1 Jan 2004. PubMed ID: 14702155. Show all entries for this paper.

Ferrantelli2007 Flavia Ferrantelli, Kathleen A. Buckley, Robert A. Rasmussen, Alistair Chalmers, Tao Wang, Pei-Lin Li, Alison L. Williams, Regina Hofmann-Lehmann, David C. Montefiori, Lisa A. Cavacini, Hermann Katinger, Gabriela Stiegler, Daniel C. Anderson, Harold M. McClure, and Ruth M. Ruprecht. Time Dependence of Protective Post-Exposure Prophylaxis with Human Monoclonal Antibodies Against Pathogenic SHIV Challenge in Newborn Macaques. Virology, 358(1):69-78, 5 Feb 2007. PubMed ID: 16996554. Show all entries for this paper.

Ferrari2011a Guido Ferrari, Justin Pollara, Daniel Kozink, Tiara Harms, Mark Drinker, Stephanie Freel, M. Anthony Moody, S. Munir Alam, Georgia D. Tomaras, Christina Ochsenbauer, John C. Kappes, George M. Shaw, James A. Hoxie, James E. Robinson, and Barton F. Haynes. An HIV-1 gp120 Envelope Human Monoclonal Antibody That Recognizes a C1 Conformational Epitope Mediates Potent Antibody-Dependent Cellular Cytotoxicity (ADCC) Activity and Defines a Common ADCC Epitope in Human HIV-1 Serum. J. Virol., 85(14):7029-7036, Jul 2011. PubMed ID: 21543485. Show all entries for this paper.

Floss2009 Doreen M. Floss, Markus Sack, Elsa Arcalis, Johannes Stadlmann, Heribert Quendler, Thomas Rademacher, Eva Stoger, Jürgen Scheller, Rainer Fischer, and Udo Conrad. Influence of Elastin-Like Peptide Fusions on the Quantity and Quality of a Tobacco-Derived Human Immunodeficiency Virus-Neutralizing Antibody. Plant Biotechnol. J., 7(9):899-913, Dec 2009. PubMed ID: 19843249. Show all entries for this paper.

Forsell2005 Mattias N. E. Forsell, Yuxing Li, Maria Sundbäck, Krisha Svehla, Peter Liljeström, John R. Mascola, Richard Wyatt, and Gunilla B. Karlsson Hedestam. Biochemical and Immunogenic Characterization of Soluble Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers Expressed by Semliki Forest Virus. J Virol, 79(17):10902-10914, Sep 2005. PubMed ID: 16103142. Show all entries for this paper.

Forsman2008 Anna Forsman, Els Beirnaert, Marlén M. I. Aasa-Chapman, Bart Hoorelbeke, Karolin Hijazi, Willie Koh, Vanessa Tack, Agnieszka Szynol, Charles Kelly, Áine McKnight, Theo Verrips, Hans de Haard, and Robin A Weiss. Llama Antibody Fragments with Cross-Subtype Human Immunodeficiency Virus Type 1 (HIV-1)-Neutralizing Properties and High Affinity for HIV-1 gp120. J. Virol., 82(24):12069-12081, Dec 2008. PubMed ID: 18842738. Show all entries for this paper.

Forthal2009 Donald N. Forthal and Christiane Moog. Fc Receptor-Mediated Antiviral Antibodies. Curr. Opin. HIV AIDS, 4(5):388-393, Sep 2009. PubMed ID: 20048702. Show all entries for this paper.

Forthal2010 Donald N. Forthal, Johannes S. Gach, Gary Landucci, Jakub Jez, Richard Strasser, Renate Kunert, and Herta Steinkellner. Fc-Glycosylation Influences Fc-gamma Receptor Binding and Cell-Mediated Anti-HIV Activity of Monoclonal Antibody 2G12. J Immunol, 185(11):6876-6882, 1 Dec 2010. PubMed ID: 21041724. Show all entries for this paper.

Fouts1997 T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632. Show all entries for this paper.

Fouts1998 T. R. Fouts, A. Trkola, M. S. Fung, and J. P. Moore. Interactions of Polyclonal and Monoclonal Anti-Glycoprotein 120 Antibodies with Oligomeric Glycoprotein 120-Glycoprotein 41 Complexes of a Primary HIV Type 1 Isolate: Relationship to Neutralization. AIDS Res. Hum. Retroviruses, 14:591-597, 1998. Ab reactivity to oligomeric forms of gp120 were compared to neutralization of the macrophage tropic primary virus JRFL, and did not always correlate. This builds upon studies which have shown that oligomer binding while required for neutralization, is not always sufficient. MAb 205-46-9 and 2G6 bind oligomer with high affinity, comparable to IgG1b12, but unlike IgG1b12, cannot neutralize JRFL. Furthermore, neutralizing and non-neutralizing sera from HIV-1 infected people are similar in their reactivities to oligomeric JRFL Envelope. PubMed ID: 9591713. Show all entries for this paper.

Frankel1998 S. S. Frankel, R. M. Steinman, N. L. Michael, S. R. Kim, N. Bhardwaj, M. Pope, M. K. Louder, P. K. Ehrenberg, P. W. Parren, D. R. Burton, H. Katinger, T. C. VanCott, M. L. Robb, D. L. Birx, and J. R. Mascola. Neutralizing Monoclonal Antibodies Block Human Immunodeficiency Virus Type 1 Infection of Dendritic Cells and Transmission to T Cells. J. Virol., 72:9788-9794, 1998. Investigation of three human MAbs to elicit a neutralizing effect and block HIV-1 infection in human dendritic cells. Preincubation with NAbs IgG1b12 or a combination of 2F5/2G12 prevented infection of purified DC and transmission in DC/T-cell cultures. PubMed ID: 9811714. Show all entries for this paper.

Frey2008 Gary Frey, Hanqin Peng, Sophia Rits-Volloch, Marco Morelli, Yifan Cheng, and Bing Chen. A Fusion-Intermediate State of HIV-1 gp41 Targeted by Broadly Neutralizing Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(10):3739-3744, 11 Mar 2008. PubMed ID: 18322015. Show all entries for this paper.

Gach2010 Johannes S. Gach, Paul G. Furtmüller, Heribert Quendler, Paul Messner, Ralf Wagner, Hermann Katinger, and Renate Kunert. Proline Is Not Uniquely Capable of Providing the Pivot Point for Domain Swapping in 2G12, a Broadly Neutralizing Antibody against HIV-1. J. Biol. Chem., 285(2):1122-1127, 8 Jan 2010. PubMed ID: 19903812. Show all entries for this paper.

Gach2013 Johannes S. Gach, Heribert Quendler, Tommy Tong, Kristin M. Narayan, Sean X. Du, Robert G. Whalen, James M. Binley, Donald N. Forthal, Pascal Poignard, and Michael B. Zwick. A Human Antibody to the CD4 Binding Site of gp120 Capable of Highly Potent but Sporadic Cross Clade Neutralization of Primary HIV-1. PLoS One, 8(8):e72054, 2013. PubMed ID: 23991039. Show all entries for this paper.

Gach2014 Johannes S. Gach, Chad J. Achenbach, Veronika Chromikova, Baiba Berzins, Nina Lambert, Gary Landucci, Donald N. Forthal, Christine Katlama, Barbara H. Jung, and Robert L. Murphy. HIV-1 Specific Antibody Titers and Neutralization among Chronically Infected Patients on Long-Term Suppressive Antiretroviral Therapy (ART): A Cross-Sectional Study. PLoS One, 9(1):e85371, 2014. PubMed ID: 24454852. Show all entries for this paper.

Gao2005a Feng Gao, Eric A. Weaver, Zhongjing Lu, Yingying Li, Hua-Xin Liao, Benjiang Ma, S Munir Alam, Richard M. Scearce, Laura L. Sutherland, Jae-Sung Yu, Julie M. Decker, George M. Shaw, David C. Montefiori, Bette T. Korber, Beatrice H. Hahn, and Barton F. Haynes. Antigenicity and Immunogenicity of a Synthetic Human Immunodeficiency Virus Type 1 Group M Consensus Envelope Glycoprotein. J. Virol., 79(2):1154-1163, Jan 2005. PubMed ID: 15613343. Show all entries for this paper.

Gao2007 Feng Gao, Hua-Xin Liao, Beatrice H. Hahn, Norman L. Letvin, Bette T. Korber, and Barton F. Haynes. Centralized HIV-1 Envelope Immunogens and Neutralizing Antibodies. Curr. HIV Res., 5(6):572-577, Nov 2007. PubMed ID: 18045113. Show all entries for this paper.

Gao2009 Feng Gao, Richard M. Scearce, S. Munir Alam, Bhavna Hora, Shimao Xia, Julie E. Hohm, Robert J. Parks, Damon F. Ogburn, Georgia D. Tomaras, Emily Park, Woodrow E. Lomas, Vernon C. Maino, Susan A. Fiscus, Myron S. Cohen, M. Anthony Moody, Beatrice H. Hahn, Bette T. Korber, Hua-Xin Liao, and Barton F. Haynes. Cross-reactive Monoclonal Antibodies to Multiple HIV-1 Subtype and SIVcpz Envelope Glycoproteins. Virology, 394(1):91-98, 10 Nov 2009. PubMed ID: 19744690. Show all entries for this paper.

Gavrilyuk2013 Julia Gavrilyuk, Hitoshi Ban, Hisatoshi Uehara, Shannon J. Sirk, Karen Saye-Francisco, Angelica Cuevas, Elise Zablowsky, Avinash Oza, Michael S. Seaman, Dennis R. Burton, and Carlos F. Barbas, 3rd. Antibody Conjugation Approach Enhances Breadth and Potency of Neutralization of Anti-HIV-1 Antibodies and CD4-IgG. J. Virol., 87(9):4985-4993, May 2013. PubMed ID: 23427154. Show all entries for this paper.

Geonnotti2010 Anthony R. Geonnotti, Miroslawa Bilska, Xing Yuan, Christina Ochsenbauer, Tara G. Edmonds, John C. Kappes, Hua-Xin Liao, Barton F. Haynes, and David C. Montefiori. Differential Inhibition of Human Immunodeficiency Virus Type 1 in Peripheral Blood Mononuclear Cells and TZM-bl Cells by Endotoxin-Mediated Chemokine and Gamma Interferon Production. AIDS Res. Hum. Retroviruses, 26(3):279-291, Mar 2010. PubMed ID: 20218881. Show all entries for this paper.

Georgiev2013 Ivelin S. Georgiev, Nicole A. Doria-Rose, Tongqing Zhou, Young Do Kwon, Ryan P. Staupe, Stephanie Moquin, Gwo-Yu Chuang, Mark K. Louder, Stephen D. Schmidt, Han R. Altae-Tran, Robert T. Bailer, Krisha McKee, Martha Nason, Sijy O'Dell, Gilad Ofek, Marie Pancera, Sanjay Srivatsan, Lawrence Shapiro, Mark Connors, Stephen A. Migueles, Lynn Morris, Yoshiaki Nishimura, Malcolm A. Martin, John R. Mascola, and Peter D. Kwong. Delineating Antibody Recognition in Polyclonal Sera from Patterns of HIV-1 Isolate Neutralization. Science, 340(6133):751-756, 10 May 2013. PubMed ID: 23661761. Show all entries for this paper.

GoldingH2002 Hana Golding, Marina Zaitseva, Eve de Rosny, Lisa R. King, Jody Manischewitz, Igor Sidorov, Miroslaw K. Gorny, Susan Zolla-Pazner, Dimiter S. Dimitrov, and Carol D. Weiss. Dissection of Human Immunodeficiency Virus Type 1 Entry with Neutralizing Antibodies to gp41 Fusion Intermediates. J. Virol., 76(13):6780-6790, Jul 2002. PubMed ID: 12050391. Show all entries for this paper.

Gonzalez2010 Nuria Gonzalez, Amparo Alvarez, and Jose Alcami. Broadly Neutralizing Antibodies and their Significance for HIV-1 Vaccines. Curr. HIV Res., 8(8):602-612, Dec 2010. PubMed ID: 21054253. Show all entries for this paper.

Gopi2008 Hosahudya Gopi, M. Umashankara, Vanessa Pirrone, Judith LaLonde, Navid Madani, Ferit Tuzer, Sabine Baxter, Isaac Zentner, Simon Cocklin, Navneet Jawanda, Shendra R. Miller, Arne Schön, Jeffrey C. Klein, Ernesto Freire, Fred C. Krebs, Amos B. Smith, Joseph Sodroski, and Irwin Chaiken. Structural Determinants for Affinity Enhancement of a Dual Antagonist Peptide Entry Inhibitor of Human Immunodeficiency Virus Type-1. J. Med. Chem., 51(9):2638-2647, 8 May 2008. PubMed ID: 18402432. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Gorny2005 Miroslaw K. Gorny, Leonidas Stamatatos, Barbara Volsky, Kathy Revesz, Constance Williams, Xiao-Hong Wang, Sandra Cohen, Robert Staudinger, and Susan Zolla-Pazner. Identification of a New Quaternary Neutralizing Epitope on Human Immunodeficiency Virus Type 1 Virus Particles. J. Virol., 79(8):5232-5237, Apr 2005. PubMed ID: 15795308. Show all entries for this paper.

Gorry2002 Paul R. Gorry, Joann Taylor, Geoffrey H. Holm, Andrew Mehle, Tom Morgan, Mark Cayabyab, Michael Farzan, Hui Wang, Jeanne E. Bell, Kevin Kunstman, John P. Moore, Steven M. Wolinsky, and Dana Gabuzda. Increased CCR5 Affinity and Reduced CCR5/CD4 Dependence of a Neurovirulent Primary Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 76(12):6277-6292, Jun 2002. PubMed ID: 12021361. Show all entries for this paper.

Gray2006 Elin Solomonovna Gray, Tammy Meyers, Glenda Gray, David Charles Montefiori, and Lynn Morris. Insensitivity of Paediatric HIV-1 Subtype C Viruses to Broadly Neutralising Monoclonal Antibodies Raised against Subtype B. PLoS Med., 3(7):e255, Jul 2006. PubMed ID: 16834457. Show all entries for this paper.

Gray2007a Elin S. Gray, Penny L. Moore, Ralph A. Pantophlet, and Lynn Morris. N-Linked Glycan Modifications in gp120 of Human Immunodeficiency Virus Type 1 Subtype C Render Partial Sensitivity to 2G12 Antibody Neutralization. J. Virol., 81(19):10769-10776, Oct 2007. PubMed ID: 17634239. Show all entries for this paper.

Grovit-Ferbas2000 K. Grovit-Ferbas, J. F. Hsu, J. Ferbas, V. Gudeman, and I. S. Chen. Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1. J. Virol., 74(13):5802-9, Jul 2000. URL: http://jvi.asm.org/cgi/content/full/74/13/5802. PubMed ID: 10846059. Show all entries for this paper.

Grundner2002 Christoph Grundner, Tajib Mirzabekov, Joseph Sodroski, and Richard Wyatt. Solid-Phase Proteoliposomes Containing Human Immunodeficiency Virus Envelope Glycoproteins. J. Virol., 76(7):3511-3521, Apr 2002. PubMed ID: 11884575. Show all entries for this paper.

Grundner2005 Christoph Grundner, Yuxing Li, Mark Louder, John Mascola, Xinzhen Yang, Joseph Sodroski, and Richard Wyatt. Analysis of the Neutralizing Antibody Response Elicited in Rabbits by Repeated Inoculation with Trimeric HIV-1 Envelope Glycoproteins. Virology, 331(1):33-46, 5 Jan 2005. PubMed ID: 15582651. Show all entries for this paper.

Gunn2016 B. M. Gunn, J. R. Schneider, M. Shansab, A. R. Bastian, K. M. Fahrbach, A. D. Smith, A. E. Mahan, M. M. Karim, A. F. Licht, I. Zvonar, J. Tedesco, M. R. Anderson, A. Chapel, T. J. Suscovich, D. C. Malaspina, H. Streeck, B. D. Walker, A. Kim, G. Lauer, M. Altfeld, S. Pillai, I. Szleifer, N. L. Kelleher, P. F. Kiser, T. J. Hope, and G. Alter. Enhanced Binding of Antibodies Generated During Chronic HIV Infection to Mucus Component MUC16. Mucosal. Immunol., 9(6):1549-1558, Nov 2016. PubMed ID: 26960182. Show all entries for this paper.

Gupta2013 Sandeep Gupta, Johannes S. Gach, Juan C. Becerra, Tran B. Phan, Jeffrey Pudney, Zina Moldoveanu, Sarah B. Joseph, Gary Landucci, Medalyn Jude Supnet, Li-Hua Ping, Davide Corti, Brian Moldt, Zdenek Hel, Antonio Lanzavecchia, Ruth M. Ruprecht, Dennis R. Burton, Jiri Mestecky, Deborah J. Anderson, and Donald N. Forthal. The Neonatal Fc Receptor (FcRn) Enhances Human Immunodeficiency Virus Type 1 (HIV-1) Transcytosis across Epithelial Cells. PLoS Pathog., 9(11):e1003776, Nov 2013. PubMed ID: 24278022. Show all entries for this paper.

Gustchina2008 Elena Gustchina, Carole A. Bewley, and G. Marius Clore. Sequestering of the Prehairpin Intermediate of gp41 by Peptide N36Mut(e,g) Potentiates the Human Immunodeficiency Virus Type 1 Neutralizing Activity of Monoclonal Antibodies Directed against the N-Terminal Helical Repeat of gp41. J. Virol., 82(20):10032-10041, Oct 2008. PubMed ID: 18667502. Show all entries for this paper.

Guzzo2018 Christina Guzzo, Peng Zhang, Qingbo Liu, Alice L. Kwon, Ferzan Uddin, Alexandra I. Wells, Hana Schmeisser, Raffaello Cimbro, Jinghe Huang, Nicole Doria-Rose, Stephen D. Schmidt, Michael A. Dolan, Mark Connors, John R. Mascola, and Paolo Lusso. Structural Constraints at the Trimer Apex Stabilize the HIV-1 Envelope in a Closed, Antibody-Protected Conformation. mBio, 9(6), 11 Dec 2018. PubMed ID: 30538178. Show all entries for this paper.

Haigwood2009 Nancy L. Haigwood and Vanessa M. Hirsch. Blocking and Tackling HIV. Nat. Med., 15(8):841-842, Aug 2009. PubMed ID: 19661984. Show all entries for this paper.

Haim2007 Hillel Haim, Israel Steiner, and Amos Panet. Time Frames for Neutralization during the Human Immunodeficiency Virus Type 1 Entry Phase, as Monitored in Synchronously Infected Cell Cultures. J. Virol., 81(7):3525-3534, Apr 2007. PubMed ID: 17251303. Show all entries for this paper.

Haim2011 Hillel Haim, Bettina Strack, Aemro Kassa, Navid Madani, Liping Wang, Joel R. Courter, Amy Princiotto, Kathleen McGee, Beatriz Pacheco, Michael S. Seaman, Amos B. Smith, 3rd., and Joseph Sodroski. Contribution of Intrinsic Reactivity of the HIV-1 Envelope Glycoproteins to CD4-Independent Infection and Global Inhibitor Sensitivity. PLoS Pathog., 7(6):e1002101, Jun 2011. PubMed ID: 21731494. Show all entries for this paper.

Haldar2011 Bijayesh Haldar, Sherri Burda, Constance Williams, Leo Heyndrickx, Guido Vanham, Miroslaw K. Gorny, and Phillipe Nyambi. Longitudinal Study of Primary HIV-1 Isolates in Drug-Naïve Individuals Reveals the Emergence of Variants Sensitive to Anti-HIV-1 Monoclonal Antibodies. PLoS One, 6(2):e17253, 2011. PubMed ID: 21383841. Show all entries for this paper.

Hart2003 Melanie L. Hart, Mohammed Saifuddin, and Gregory T. Spear. Glycosylation Inhibitors and Neuraminidase Enhance Human Immunodeficiency Virus Type 1 Binding and Neutralization by Mannose-Binding Lectin. J. Gen. Virol., 84(Pt 2):353-360, Feb 2003. PubMed ID: 12560567. Show all entries for this paper.

Haynes2005 Barton F. Haynes, Judith Fleming, E. William St. Clair, Herman Katinger, Gabriela Stiegler, Renate Kunert, James Robinson, Richard M. Scearce, Kelly Plonk, Herman F. Staats, Thomas L. Ortel, Hua-Xin Liao, and S. Munir Alam. Cardiolipin Polyspecific Autoreactivity in Two Broadly Neutralizing HIV-1 Antibodies. Science, 308(5730):1906-1908, 24 Jun 2005. Comment in Science 2005 Jun 24;308(5730):1878-9. PubMed ID: 15860590. Show all entries for this paper.

Haynes2005a Barton F. Haynes, M. Anthony Moody, Laurent Verkoczy, Garnett Kelsoe, and S. Munir Alam. Antibody Polyspecificity and Neutralization of HIV-1: A Hypothesis. Hum. Antibodies, 14(3-4):59-67, 2005. PubMed ID: 16720975. Show all entries for this paper.

Haynes2006a Barton F. Haynes and David C. Montefiori. Aiming to Induce Broadly Reactive Neutralizing Antibody Responses with HIV-1 Vaccine Candidates. Expert Rev. Vaccines, 5(4):579-595, Aug 2006. PubMed ID: 16989638. Show all entries for this paper.

Haynes2008 Barton F. Haynes and Robin J. Shattock. Critical Issues in Mucosal Immunity for HIV-1 Vaccine Development. J. Allergy Clin. Immunol., 122(1):3-9, Jul 2008. PubMed ID: 18468671. Show all entries for this paper.

Haynes2012 Barton F. Haynes, Garnett Kelsoe, Stephen C. Harrison, and Thomas B. Kepler. B-Cell-Lineage Immunogen Design in Vaccine Development with HIV-1 as a Case Study. Nat. Biotechnol., 30(5):423-433, May 2012. PubMed ID: 22565972. Show all entries for this paper.

He2018 Linling He, Sonu Kumar, Joel D. Allen, Deli Huang, Xiaohe Lin, Colin J. Mann, Karen L. Saye-Francisco, Jeffrey Copps, Anita Sarkar, Gabrielle S. Blizard, Gabriel Ozorowski, Devin Sok, Max Crispin, Andrew B. Ward, David Nemazee, Dennis R. Burton, Ian A. Wilson, and Jiang Zhu. HIV-1 Vaccine Design through Minimizing Envelope Metastability. Sci. Adv., 4(11):eaau6769, Nov 2018. PubMed ID: 30474059. Show all entries for this paper.

Henderson2019 Rory Henderson, Brian E. Watts, Hieu N. Ergin, Kara Anasti, Robert Parks, Shi-Mao Xia, Ashley Trama, Hua-Xin Liao, Kevin O. Saunders, Mattia Bonsignori, Kevin Wiehe, Barton F. Haynes, and S. Munir Alam. Selection of Immunoglobulin Elbow Region Mutations Impacts Interdomain Conformational Flexibility in HIV-1 Broadly Neutralizing Antibodies. Nat. Commun., 10(1):654, 8 Feb 2019. PubMed ID: 30737386. Show all entries for this paper.

Herrera2003 Carolina Herrera, Catherine Spenlehauer, Michael S. Fung, Dennis R. Burton, Simon Beddows, and John P. Moore. Nonneutralizing Antibodies to the CD4-Binding Site on the gp120 Subunit of Human Immunodeficiency Virus Type 1 Do Not Interfere with the Activity of a Neutralizing Antibody against the Same Site. J. Virol., 77(2):1084-1091, Jan 2003. PubMed ID: 12502824. Show all entries for this paper.

Herrera2005 Carolina Herrera, Per Johan Klasse, Elizabeth Michael, Shivani Kake, Kelly Barnes, Christopher W. Kibler, Lila. Campbell-Gardener, Zhihai Si, Joseph Sodroski, John P. Moore, and Simon Beddows. The Impact of Envelope Glycoprotein Cleavage on the Antigenicity, Infectivity, and Neutralization Sensitivity of Env-Pseudotyped Human Immunodeficiency Virus Type 1 Particles. Virology, 338(1):154-172, 20 Jul 2005. PubMed ID: 15932765. Show all entries for this paper.

Herrera2006 Carolina Herrera, Per Johan Klasse, Christopher W. Kibler, Elizabeth Michael, John P. Moore, and Simon Beddows. Dominant-Negative Effect of Hetero-Oligomerization on the Function of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex. Virology, 351(1):121-132, 20 Jul 2006. PubMed ID: 16616288. Show all entries for this paper.

Hessell2009 Ann J. Hessell, Eva G. Rakasz, Pascal Poignard, Lars Hangartner, Gary Landucci, Donald N. Forthal, Wayne C. Koff, David I. Watkins, and Dennis R. Burton. Broadly Neutralizing Human Anti-HIV Antibody 2G12 Is Effective in Protection against Mucosal SHIV Challenge Even at Low Serum Neutralizing Titers. PLoS Pathog., 5(5):e1000433, May 2009. PubMed ID: 19436712. Show all entries for this paper.

Hildgartner2009 Alexander Hildgartner, Doris Wilflingseder, Christoph Gassner, Manfred P. Dierich, Heribert Stoiber, and Zoltán Bánki. Induction of Complement-Mediated Lysis of HIV-1 by a Combination of HIV-Specific and HLA Allotype-Specific Antibodies. Immunol. Lett., 126(1-2):85-90, 22 Sep 2009. PubMed ID: 19698750. Show all entries for this paper.

Hoffenberg2013 Simon Hoffenberg, Rebecca Powell, Alexei Carpov, Denise Wagner, Aaron Wilson, Sergei Kosakovsky Pond, Ross Lindsay, Heather Arendt, Joanne DeStefano, Sanjay Phogat, Pascal Poignard, Steven P. Fling, Melissa Simek, Celia LaBranche, David Montefiori, Terri Wrin, Pham Phung, Dennis Burton, Wayne Koff, C. Richter King, Christopher L. Parks, and Michael J. Caulfield. Identification of an HIV-1 Clade A Envelope That Exhibits Broad Antigenicity and Neutralization Sensitivity and Elicits Antibodies Targeting Three Distinct Epitopes. J. Virol., 87(10):5372-5383, May 2013. PubMed ID: 23468492. Show all entries for this paper.

HofmannLehmann2001 R. Hofmann-Lehmann, J. Vlasak, R. A. Rasmussen, B. A. Smith, T. W. Baba, V. Liska, F. Ferrantelli, D. C. Montefiori, H. M. McClure, D. C. Anderson, B. J. Bernacky, T. A. Rizvi, R. Schmidt, L. R. Hill, M. E. Keeling, H. Katinger, G. Stiegler, L. A. Cavacini, M. R. Posner, T. C. Chou, J. Andersen, and R. M. Ruprecht. Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge. J. Virol., 75(16):7470--80, Aug 2001. URL: http://jvi.asm.org/cgi/content/full/75/16/7470. PubMed ID: 11462019. Show all entries for this paper.

Hogan2018 Michael J. Hogan, Angela Conde-Motter, Andrea P. O. Jordan, Lifei Yang, Brad Cleveland, Wenjin Guo, Josephine Romano, Houping Ni, Norbert Pardi, Celia C. LaBranche, David C. Montefiori, Shiu-Lok Hu, James A. Hoxie, and Drew Weissman. Increased Surface Expression of HIV-1 Envelope Is Associated with Improved Antibody Response in Vaccinia Prime/Protein Boost Immunization. Virology, 514:106-117, 15 Jan 2018. PubMed ID: 29175625. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Holl2006a Vincent Holl, Maryse Peressin, Sylvie Schmidt, Thomas Decoville, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Efficient Inhibition of HIV-1 Replication in Human Immature Monocyte-Derived Dendritic Cells by Purified Anti-HIV-1 IgG without Induction of Maturation. Blood, 107(11):4466-4474, 1 Jun 2006. PubMed ID: 16469871. Show all entries for this paper.

Hong2007 Patrick W.-P. Hong, Sandra Nguyen, Sophia Young, Stephen V. Su, and Benhur Lee. Identification of the Optimal DC-SIGN Binding Site on Human Immunodeficiency Virus Type 1 gp120. J. Virol., 81(15):8325-8336, Aug 2007. PubMed ID: 17522223. Show all entries for this paper.

Honnen2007 W. J. Honnen, C. Krachmarov, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and A. Pinter. Type-Specific Epitopes Targeted by Monoclonal Antibodies with Exceptionally Potent Neutralizing Activities for Selected Strains of Human Immunodeficiency Virus Type 1 Map to a Common Region of the V2 Domain of gp120 and Differ Only at Single Positions from the Clade B Consensus Sequence. J. Virol., 81(3):1424-1432, Feb 2007. PubMed ID: 17121806. Show all entries for this paper.

Hoxie2010 James A. Hoxie. Toward an Antibody-Based HIV-1 Vaccine. Annu. Rev. Med., 61:135-52, 2010. PubMed ID: 19824826. Show all entries for this paper.

Hraber2014 Peter Hraber, Michael S. Seaman, Robert T. Bailer, John R. Mascola, David C. Montefiori, and Bette T. Korber. Prevalence of Broadly Neutralizing Antibody Responses during Chronic HIV-1 Infection. AIDS, 28(2):163-169, 14 Jan 2014. PubMed ID: 24361678. Show all entries for this paper.

Hrin2008 Renee Hrin, Donna L. Montgomery, Fubao Wang, Jon H. Condra, Zhiqiang An, William R. Strohl, Elisabetta Bianchi, Antonello Pessi, Joseph G. Joyce, and Ying-Jie Wang. Short Communication: In Vitro Synergy between Peptides or Neutralizing Antibodies Targeting the N- and C-Terminal Heptad Repeats of HIV Type 1 gp41. AIDS Res. Hum. Retroviruses, 24(12):1537-1544, Dec 2008. PubMed ID: 19102685. Show all entries for this paper.

Hu2007 Qinxue Hu, Naheed Mahmood, and Robin J. Shattock. High-Mannose-Specific Deglycosylation of HIV-1 gp120 Induced by Resistance to Cyanovirin-N and the Impact on Antibody Neutralization. Virology, 368(1):145-154, 10 Nov 2007. PubMed ID: 17658575. Show all entries for this paper.

Hu2017 Xintao Hu, Yuanyuan Hu, Chunhong Zhao, Hongmei Gao, Kelli M. Greene, Li Ren, Liying Ma, Yuhua Ruan, Marcella Sarzotti-Kelsoe, David C. Montefiori, Kunxue Hong, and Yiming Shao. Profiling the Neutralizing Antibody Response in Chronically HIV-1 CRF07\_BC-Infected Intravenous Drug Users Naive to Antiretroviral Therapy. Sci. Rep., 7:46308, 7 Apr 2017. PubMed ID: 28387330. Show all entries for this paper.

Huang2007 Li Huang, Weihong Lai, Phong Ho, and Chin Ho Chen. Induction of a Nonproductive Conformational Change in gp120 by a Small Molecule HIV Type 1 Entry Inhibitor. AIDS Res. Hum. Retroviruses, 23(1):28-32, Jan 2007. PubMed ID: 17263629. Show all entries for this paper.

Huang2010 Kuan-Hsiang G. Huang, David Bonsall, Aris Katzourakis, Emma C. Thomson, Sarah J. Fidler, Janice Main, David Muir, Jonathan N. Weber, Alexander J. Frater, Rodney E. Phillips, Oliver G. Pybus, Philip J. R. Goulder, Myra O. McClure, Graham S. Cooke, and Paul Klenerman. B-Cell Depletion Reveals a Role for Antibodies in the Control of Chronic HIV-1 Infection. Nat. Commun., 1:102, 2010. PubMed ID: 20981030. Show all entries for this paper.

Huang2012 Xin Huang, Wei Jin, Kai Hu, Sukun Luo, Tao Du, George E. Griffin, Robin J. Shattock, and Qinxue Hu. Highly Conserved HIV-1 gp120 Glycans Proximal to CD4-Binding Region Affect Viral Infectivity and Neutralizing Antibody Induction. Virology, 423(1):97-106, 5 Feb 2012. PubMed ID: 22192629. Show all entries for this paper.

Huang2017a Xun Huang, Qianqian Zhu, Xiaoxing Huang, Lifei Yang, Yufeng Song, Ping Zhu, and Paul Zhou. In Vivo Electroporation in DNA-VLP Prime-Boost Preferentially Enhances HIV-1 Envelope-Specific IgG2a, Neutralizing Antibody and CD8 T Cell Responses. Vaccine, 35(16):2042-2051, 11 Apr 2017. PubMed ID: 28318765. Show all entries for this paper.

Huber2007 M. Huber and A. Trkola. Humoral Immunity to HIV-1: Neutralization and Beyond. J. Intern. Med., 262(1):5-25, Jul 2007. PubMed ID: 17598812. Show all entries for this paper.

Huber2010 Michael Huber, Khoa M. Le, Katie J. Doores, Zara Fulton, Robyn L. Stanfield, Ian A. Wilson, and Dennis R. Burton. Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain Exchange. J. Virol., 84(20):10700-10707, Oct 2010. PubMed ID: 20702640. Show all entries for this paper.

Huskens2007 Dana Huskens, Kristel Van Laethem, Kurt Vermeire, Jan Balzarini, and Dominique Schols. Resistance of HIV-1 to the Broadly HIV-1-Neutralizing, Anti-Carbohydrate Antibody 2G12. Virology, 360(2):294-304, 10 Apr 2007. PubMed ID: 17123566. Show all entries for this paper.

Jeffs2004 S. A. Jeffs, S. Goriup, B. Kebble, D. Crane, B. Bolgiano, Q. Sattentau, S. Jones, and H. Holmes. Expression and Characterisation of Recombinant Oligomeric Envelope Glycoproteins Derived from Primary Isolates of HIV-1. Vaccine, 22(8):1032-1046, 25 Feb 2004. PubMed ID: 15161081. Show all entries for this paper.

Jenabian2010 Mohammad-Ali Jenabian, Héla Saïdi, Charlotte Charpentier, Hicham Bouhlal, Dominique Schols, Jan Balzarini, Thomas W. Bell, Guido Vanham, and Laurent Bélec. Differential Activity of Candidate Microbicides against Early Steps of HIV-1 Infection upon Complement Virus Opsonization. AIDS Res. Ther., 7:16, 2010. PubMed ID: 20546571. Show all entries for this paper.

Johnson2017 Jacklyn Johnson, Yinjie Zhai, Hamid Salimi, Nicole Espy, Noah Eichelberger, Orlando DeLeon, Yunxia O'Malley, Joel Courter, Amos B. Smith, III, Navid Madani, Joseph Sodroski, and Hillel Haim. Induction of a Tier-1-Like Phenotype in Diverse Tier-2 Isolates by Agents That Guide HIV-1 Env to Perturbation-Sensitive, Nonnative States. J. Virol., 91(15), 1 Aug 2017. PubMed ID: 28490588. Show all entries for this paper.

Joos2006 Beda Joos, Alexandra Trkola, Herbert Kuster, Leonardo Aceto, Marek Fischer, Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Hermann Katinger, and Huldrych F. Günthard. Long-Term Multiple-Dose Pharmacokinetics of Human Monoclonal Antibodies (MAbs) against Human Immunodeficiency Virus Type 1 Envelope gp120 (MAb 2G12) and gp41 (MAbs 4E10 and 2F5). Antimicrob. Agents Chemother., 50(5):1773-1779, May 2006. PubMed ID: 16641449. Show all entries for this paper.

Joseph2010 Aviva Joseph, Jian Hua Zheng, Ken Chen, Monica Dutta, Cindy Chen, Gabriela Stiegler, Renate Kunert, Antonia Follenzi, and Harris Goldstein. Inhibition of In Vivo HIV Infection in Humanized Mice by Gene Therapy of Human Hematopoietic Stem Cells with a Lentiviral Vector Encoding a Broadly Neutralizing Anti-HIV Antibody. J. Virol., 84(13):6645-6653, Jul 2010. PubMed ID: 20410262. Show all entries for this paper.

Joubert2010 Marisa K. Joubert, Nichole Kinsley, Alexio Capovilla, B. Trevor Sewell, Mohamed A. Jaffer, and Makobetsa Khati. A Modeled Structure of an Aptamer-gp120 Complex Provides Insight into the Mechanism of HIV-1 Neutralization. Biochemistry, 49(28):5880-5890, 20 Jul 2010. PubMed ID: 20527993. Show all entries for this paper.

Joyce2008 Joseph G. Joyce, Isaac J. Krauss, Hong C. Song, David W. Opalka, Karen M. Grimm, Deborah D. Nahas, Mark T. Esser, Renee Hrin, Meizhen Feng, Vadim Y. Dudkin, Michael Chastain, John W. Shiver, and Samuel J. Danishefsky. An Oligosaccharide-Based HIV-1 2G12 Mimotope Vaccine Induces Carbohydrate-Specific Antibodies That Fail To Neutralize HIV-1 Virions. Proc. Natl. Acad. Sci. U.S.A., 105(41):15684-15689, 14 Oct 2008. PubMed ID: 18838688. Show all entries for this paper.

Joyner2011 Amanda S. Joyner, Jordan R. Willis, James E.. Crowe, Jr., and Christopher Aiken. Maturation-Induced Cloaking of Neutralization Epitopes on HIV-1 Particles. PLoS Pathog., 7(9):e1002234, Sep 2011. PubMed ID: 21931551. Show all entries for this paper.

Julg2005 B. Jülg and F. D. Goebel. What's New in HIV/AIDS? Neutralizing HIV Antibodies: Do They Really Protect? Infection, 33(5-6):405-407, Oct 2005. PubMed ID: 16258878. Show all entries for this paper.

Julien2015 Jean-Philippe Julien, Jeong Hyun Lee, Gabriel Ozorowski, Yuanzi Hua, Alba Torrents de la Peña, Steven W. de Taeye, Travis Nieusma, Albert Cupo, Anila Yasmeen, Michael Golabek, Pavel Pugach, P. J. Klasse, John P. Moore, Rogier W. Sanders, Andrew B. Ward, and Ian A. Wilson. Design and Structure of Two HIV-1 Clade C SOSIP.664 Trimers That Increase the Arsenal of Native-Like Env Immunogens. Proc. Natl. Acad. Sci. U.S.A., 112(38):11947-11952, 22 Sep 2015. PubMed ID: 26372963. Show all entries for this paper.

Kabanova2010 Anna Kabanova, Roberto Adamo, Daniela Proietti, Francesco Berti, Marta Tontini, Rino Rappuoli, and Paolo Costantino. Preparation, Characterization and Immunogenicity of HIV-1 Related High-Mannose Oligosaccharides-CRM197 Glycoconjugates. Glycoconj. J., 27(5):501-513, Jul 2010. PubMed ID: 20524062. Show all entries for this paper.

Kalia2005 Vandana Kalia, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41. J. Virol., 79(4):2097-2107, Feb 2005. PubMed ID: 15681412. Show all entries for this paper.

Kang2005 Sang-Moo Kang, Fu Shi Quan, Chunzi Huang, Lizheng Guo, Ling Ye, Chinglai Yang, and Richard W. Compans. Modified HIV Envelope Proteins with Enhanced Binding to Neutralizing Monoclonal Antibodies. Virology, 331(1):20-32, 5 Jan 2005. PubMed ID: 15582650. Show all entries for this paper.

Kang2009 Yun Kenneth Kang, Sofija Andjelic, James M. Binley, Emma T. Crooks, Michael Franti, Sai Prasad N. Iyer, Gerald P. Donovan, Antu K. Dey, Ping Zhu, Kenneth H. Roux, Robert J. Durso, Thomas F. Parsons, Paul J. Maddon, John P. Moore, and William C. Olson. Structural and Immunogenicity Studies of a Cleaved, Stabilized Envelope Trimer Derived from Subtype A HIV-1. Vaccine, 27(37):5120-5132, 13 Aug 2009. PubMed ID: 19567243. Show all entries for this paper.

Karpenko2012 Larisa I. Karpenko, Nadezhda S. Scherbakova, Anton N. Chikaev, Olga Yu. Tumanova, Leonid R. Lebedev, Lyudmila A. Shalamova, Olga G. Pyankova, Alexander B. Ryzhikov, and Alexander A. Ilyichev. Polyepitope Protein Incorporated the HIV-1 Mimotope Recognized by Monoclonal Antibody 2G12. Mol. Immunol., 50(4):193-199, Apr 2012. PubMed ID: 22341130. Show all entries for this paper.

Keele2008 Brandon F. Keele, Elena E. Giorgi, Jesus F. Salazar-Gonzalez, Julie M. Decker, Kimmy T. Pham, Maria G. Salazar, Chuanxi Sun, Truman Grayson, Shuyi Wang, Hui Li, Xiping Wei, Chunlai Jiang, Jennifer L. Kirchherr, Feng Gao, Jeffery A. Anderson, Li-Hua Ping, Ronald Swanstrom, Georgia D. Tomaras, William A. Blattner, Paul A. Goepfert, J. Michael Kilby, Michael S. Saag, Eric L. Delwart, Michael P. Busch, Myron S. Cohen, David C. Montefiori, Barton F. Haynes, Brian Gaschen, Gayathri S. Athreya, Ha Y. Lee, Natasha Wood, Cathal Seoighe, Alan S. Perelson, Tanmoy Bhattacharya, Bette T. Korber, Beatrice H. Hahn, and George M. Shaw. Identification and Characterization of Transmitted and Early Founder Virus Envelopes in Primary HIV-1 Infection. Proc. Natl. Acad. Sci. U.S.A., 105(21):7552-7557, 27 May 2008. PubMed ID: 18490657. Show all entries for this paper.

Kirchherr2007 Jennifer L. Kirchherr, Xiaozhi Lu, Webster Kasongo, Victor Chalwe, Lawrence Mwananyanda, Rosemary M. Musonda, Shi-Mao Xia, Richard M. Scearce, Hua-Xin Liao, David C. Montefiori, Barton F. Haynes, and Feng Gao. High Throughput Functional Analysis of HIV-1 env Genes Without Cloning. J. Virol. Methods, 143(1):104-111, Jul 2007. PubMed ID: 17416428. Show all entries for this paper.

Kishko2011 Michael Kishko, Mohan Somasundaran, Frank Brewster, John L. Sullivan, Paul R. Clapham, and Katherine Luzuriaga. Genotypic and Functional Properties of Early Infant HIV-1 Envelopes. Retrovirology, 8:67, 2011. PubMed ID: 21843318. Show all entries for this paper.

Kitabwalla2003 Moiz Kitabwalla, Flavia Ferrantelli, Tao Wang, Alistair Chalmers, Hermann Katinger, Gabriela Stiegler, Lisa A. Cavacini, Ting-Chao Chou, and Ruth M. Ruprecht. Primary African HIV Clade A and D Isolates: Effective Cross-Clade Neutralization with a Quadruple Combination of Human Monoclonal Antibodies Raised against Clade B. AIDS Res. Hum. Retroviruses, 19(2):125-131, Feb 2003. PubMed ID: 12639248. Show all entries for this paper.

Klein2010 Joshua S. Klein and Pamela J. Bjorkman. Few and Far Between: How HIV May Be Evading Antibody Avidity. PLoS Pathog., 6(5):e1000908, May 2010. PubMed ID: 20523901. Show all entries for this paper.

Klein2010a Joshua S. Klein, Alexandre Webster, Priyanthi N. P. Gnanapragasam, Rachel P. Galimidi, and Pamela J. Bjorkman. A Dimeric Form of the HIV-1 Antibody 2G12 Elicits Potent Antibody-Dependent Cellular Cytotoxicity. AIDS, 24(11):1633-1640, 17 Jul 2010. PubMed ID: 20597163. Show all entries for this paper.

Klein2012 Florian Klein, Christian Gaebler, Hugo Mouquet, D. Noah Sather, Clara Lehmann, Johannes F. Scheid, Zane Kraft, Yan Liu, John Pietzsch, Arlene Hurley, Pascal Poignard, Ten Feizi, Lynn Morris, Bruce D. Walker, Gerd Fätkenheuer, Michael S. Seaman, Leonidas Stamatatos, and Michel C. Nussenzweig. Broad Neutralization by a Combination of Antibodies Recognizing the CD4 Binding Site and a New Conformational Epitope on the HIV-1 Envelope Protein. J. Exp. Med., 209(8):1469-1479, 30 Jul 2012. PubMed ID: 22826297. Show all entries for this paper.

Klein2013 Florian Klein, Ron Diskin, Johannes F. Scheid, Christian Gaebler, Hugo Mouquet, Ivelin S. Georgiev, Marie Pancera, Tongqing Zhou, Reha-Baris Incesu, Brooks Zhongzheng Fu, Priyanthi N. P. Gnanapragasam, Thiago Y. Oliveira, Michael S. Seaman, Peter D. Kwong, Pamela J. Bjorkman, and Michel C. Nussenzweig. Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization. Cell, 153(1):126-138, 28 Mar 2013. PubMed ID: 23540694. Show all entries for this paper.

Koh2010a Willie W. L. Koh, Anna Forsman, Stéphane Hué, Gisela J. van der Velden, David L. Yirrell, Áine McKnight, Robin A. Weiss, and Marlén M. I. Aasa-Chapman. Novel Subtype C Human Immunodeficiency Virus Type 1 Envelopes Cloned Directly from Plasma: Coreceptor Usage and Neutralization Phenotypes. J. Gen. Virol., 91(9):2374-2380, Sep 2010. PubMed ID: 20484560. Show all entries for this paper.

Kong2013 Leopold Kong, Jeong Hyun Lee, Katie J. Doores, Charles D. Murin, Jean-Philippe Julien, Ryan McBride, Yan Liu, Andre Marozsan, Albert Cupo, Per-Johan Klasse, Simon Hoffenberg, Michael Caulfield, C. Richter King, Yuanzi Hua, Khoa M. Le, Reza Khayat, Marc C. Deller, Thomas Clayton, Henry Tien, Ten Feizi, Rogier W. Sanders, James C. Paulson, John P. Moore, Robyn L. Stanfield, Dennis R. Burton, Andrew B. Ward, and Ian A. Wilson. Supersite of Immune Vulnerability on the Glycosylated Face of HIV-1 Envelope Glycoprotein gp120. Nat. Struct. Mol. Biol., 20(7):796-803, Jul 2013. PubMed ID: 23708606. Show all entries for this paper.

Korber2009 Bette Korber and S. Gnanakaran. The Implications of Patterns in HIV Diversity for Neutralizing Antibody Induction and Susceptibility. Curr. Opin. HIV AIDS, 4(5):408-417, Sep 2009. PubMed ID: 20048705. Show all entries for this paper.

Kothe2007 Denise L. Kothe, Julie M Decker, Yingying Li, Zhiping Weng, Frederic Bibollet-Ruche, Kenneth P. Zammit, Maria G. Salazar, Yalu Chen, Jesus F. Salazar-Gonzalez, Zina Moldoveanu, Jiri Mestecky, Feng Gao, Barton F. Haynes, George M. Shaw, Mark Muldoon, Bette T. M. Korber, and Beatrice H. Hahn. Antigenicity and Immunogenicity of HIV-1 Consensus Subtype B Envelope Glycoproteins. Virology, 360(1):218-234, 30 Mar 2007. PubMed ID: 17097711. Show all entries for this paper.

Kovacs2012 James M. Kovacs, Joseph P. Nkolola, Hanqin Peng, Ann Cheung, James Perry, Caroline A. Miller, Michael S. Seaman, Dan H. Barouch, and Bing Chen. HIV-1 Envelope Trimer Elicits More Potent Neutralizing Antibody Responses than Monomeric gp120. Proc. Natl. Acad. Sci. U.S.A., 109(30):12111-12116, 24 Jul 2012. PubMed ID: 22773820. Show all entries for this paper.

Koyama2014 Yuka Koyama, Kaori Ueno-Noto, and Keiko Takano. Affinity of HIV-1 Antibody 2G12 with Monosaccharides: A Theoretical Study Based on Explicit and Implicit Water Models. Comput. Biol. Chem., 49:36-44, Apr 2014. PubMed ID: 24583603. Show all entries for this paper.

Krachmarov2005 Chavdar Krachmarov, Abraham Pinter, William J. Honnen, Miroslaw K. Gorny, Phillipe N. Nyambi, Susan Zolla-Pazner, and Samuel C. Kayman. Antibodies That Are Cross-Reactive for Human Immunodeficiency Virus Type 1 Clade A and Clade B V3 Domains Are Common in Patient Sera from Cameroon, but Their Neutralization Activity Is Usually Restricted by Epitope Masking. J. Virol., 79(2):780-790, Jan 2005. PubMed ID: 15613306. Show all entries for this paper.

Krachmarov2006 C. P. Krachmarov, W. J. Honnen, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and Abraham Pinter. Factors Determining the Breadth and Potency of Neutralization by V3-Specific Human Monoclonal Antibodies Derived from Subjects Infected with Clade A or Clade B Strains of Human Immunodeficiency Virus Type 1. J. Virol., 80(14):7127-7135, Jul 2006. PubMed ID: 16809318. Show all entries for this paper.

Kramer2007 Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119. Show all entries for this paper.

Kulkarni2009 Smita S. Kulkarni, Alan Lapedes, Haili Tang, S. Gnanakaran, Marcus G. Daniels, Ming Zhang, Tanmoy Bhattacharya, Ming Li, Victoria R. Polonis, Francine E. McCutchan, Lynn Morris, Dennis Ellenberger, Salvatore T. Butera, Robert C. Bollinger, Bette T. Korber, Ramesh S. Paranjape, and David C. Montefiori. Highly Complex Neutralization Determinants on a Monophyletic Lineage of Newly Transmitted Subtype C HIV-1 Env Clones from India. Virology, 385(2):505-520, 15 Mar 2009. PubMed ID: 19167740. Show all entries for this paper.

Kunert1998 R. Kunert, F. Ruker, and H. Katinger. Molecular Characterization of Five Neutralizing Anti-HIV Type 1 Antibodies: Identification of Nonconventional D Segments in the Human Monoclonal Antibodies 2G12 and 2F5. AIDS Res. Hum. Retroviruses, 14:1115-1128, 1998. Study identifies five human MAbs which were able to neutralize primary isolates of different clades in vitro and reports the nucleotide and amino acid sequences of the heavy and light chain V segments of the antibodies. PubMed ID: 9737583. Show all entries for this paper.

Kwong2002 Peter D. Kwong, Michael L. Doyle, David J. Casper, Claudia Cicala, Stephanie A. Leavitt, Shahzad Majeed, Tavis D. Steenbeke, Miro Venturi, Irwin Chaiken, Michael Fung, Hermann Katinger, Paul W. I. H. Parren, James Robinson, Donald Van Ryk, Liping Wang, Dennis R. Burton, Ernesto Freire, Richard Wyatt, Joseph Sodroski, Wayne A. Hendrickson, and James Arthos. HIV-1 Evades Antibody-Mediated Neutralization through Conformational Masking of Receptor-Binding Sites. Nature, 420(6916):678-682, 12 Dec 2002. Comment in Nature. 2002 Dec 12;420(6916):623-4. PubMed ID: 12478295. Show all entries for this paper.

Kwong2009a Peter D. Kwong and Ian A. Wilson. HIV-1 and Influenza Antibodies: Seeing Antigens in New Ways. Nat. Immunol., 10(6):573-578, Jun 2009. PubMed ID: 19448659. Show all entries for this paper.

Kwong2011 Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Rational Design of Vaccines to Elicit Broadly Neutralizing Antibodies to HIV-1. Cold Spring Harb. Perspect. Med., 1(1):a007278, Sep 2011. PubMed ID: 22229123. Show all entries for this paper.

Kwong2012 Peter D. Kwong and John R. Mascola. Human Antibodies that Neutralize HIV-1: Identification, Structures, and B Cell Ontogenies. Immunity, 37(3):412-425, 21 Sep 2012. PubMed ID: 22999947. Show all entries for this paper.

Kwong2013 Peter D. Kwong, John R. Mascola, and Gary J. Nabel. Broadly Neutralizing Antibodies and the Search for an HIV-1 Vaccine: The End of the Beginning. Nat. Rev. Immunol., 13(9):693-701, Sep 2013. PubMed ID: 23969737. Show all entries for this paper.

Lagenaur2010 Laurel A. Lagenaur, Vadim A. Villarroel, Virgilio Bundoc, Barna Dey, and Edward A. Berger. sCD4-17b Bifunctional Protein: Extremely Broad and Potent Neutralization of HIV-1 Env Pseudotyped Viruses from Genetically Diverse Primary Isolates. Retrovirology, 7:11, 2010. PubMed ID: 20158904. Show all entries for this paper.

Lambotte2009 Olivier Lambotte, Guido Ferrari, Christiane Moog, Nicole L. Yates, Hua-Xin Liao, Robert J. Parks, Charles B. Hicks, Kouros Owzar, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, and Jean-François Delfraissy. Heterogeneous Neutralizing Antibody and Antibody-Dependent Cell Cytotoxicity Responses in HIV-1 Elite Controllers. AIDS, 23(8):897-906, 15 May 2009. PubMed ID: 19414990. Show all entries for this paper.

Lavine2012 Christy L. Lavine, Socheata Lao, David C. Montefiori, Barton F. Haynes, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology (CHAVI). High-Mannose Glycan-Dependent Epitopes Are Frequently Targeted in Broad Neutralizing Antibody Responses during Human Immunodeficiency Virus Type 1 Infection. J. Virol., 86(4):2153-2164, Feb 2012. PubMed ID: 22156525. Show all entries for this paper.

Law2007 Mansun Law, Rosa M. F. Cardoso, Ian A. Wilson, and Dennis R. Burton. Antigenic and Immunogenic Study of Membrane-Proximal External Region-Grafted gp120 Antigens by a DNA Prime-Protein Boost Immunization Strategy. J. Virol., 81(8):4272-4285, Apr 2007. PubMed ID: 17267498. Show all entries for this paper.

Leaman2010 Daniel P. Leaman, Heather Kinkead, and Michael B. Zwick. In-Solution Virus Capture Assay Helps Deconstruct Heterogeneous Antibody Recognition of Human Immunodeficiency Virus Type 1. J. Virol., 84(7):3382-3395, Apr 2010. PubMed ID: 20089658. Show all entries for this paper.

Li1997 A. Li, T. W. Baba, J. Sodroski, S. Zolla-Pazner, M. K. Gorny, J. Robinson, M. R. Posner, H. Katinger, C. F. Barbas III, D. R. Burton, T.-C. Chou, and R. M Ruprecht. Synergistic Neutralization of a Chimeric SIV/HIV Type 1 Virus with Combinations of Human Anti-HIV Type 1 Envelope Monoclonal Antibodies or Hyperimmune Globulins. AIDS Res. Hum. Retroviruses, 13:647-656, 1997. Multiple combinations of MAbs were tested for their ability to synergize neutralization of a SHIV construct containing HIV IIIB env. All of the MAb combinations tried were synergistic, suggesting such combinations may be useful for passive immunotherapy or immunoprophylaxis. Because SHIV can replicate in rhesus macaques, such approaches can potentially be studied in an it in vivo monkey model. PubMed ID: 9168233. Show all entries for this paper.

Li1998 A. Li, H. Katinger, M. R. Posner, L. Cavacini, S. Zolla-Pazner, M. K. Gorny, J. Sodroski, T. C. Chou, T. W. Baba, and R. M. Ruprecht. Synergistic Neutralization of Simian-Human Immunodeficiency Virus SHIV-vpu+ by Triple and Quadruple Combinations of Human Monoclonal Antibodies and High-Titer Anti-Human Immunodeficiency Virus Type 1 Immunoglobulins. J. Virol., 72:3235-3240, 1998. PubMed ID: 9525650. Show all entries for this paper.

Li2005a Ming Li, Feng Gao, John R. Mascola, Leonidas Stamatatos, Victoria R. Polonis, Marguerite Koutsoukos, Gerald Voss, Paul Goepfert, Peter Gilbert, Kelli M. Greene, Miroslawa Bilska, Denise L Kothe, Jesus F. Salazar-Gonzalez, Xiping Wei, Julie M. Decker, Beatrice H. Hahn, and David C. Montefiori. Human Immunodeficiency Virus Type 1 env Clones from Acute and Early Subtype B Infections for Standardized Assessments of Vaccine-Elicited Neutralizing Antibodies. J. Virol., 79(16):10108-10125, Aug 2005. PubMed ID: 16051804. Show all entries for this paper.

Li2006a Ming Li, Jesus F. Salazar-Gonzalez, Cynthia A. Derdeyn, Lynn Morris, Carolyn Williamson, James E. Robinson, Julie M. Decker, Yingying Li, Maria G. Salazar, Victoria R. Polonis, Koleka Mlisana, Salim Abdool Karim, Kunxue Hong, Kelli M. Greene, Miroslawa Bilska, Jintao Zhou, Susan Allen, Elwyn Chomba, Joseph Mulenga, Cheswa Vwalika, Feng Gao, Ming Zhang, Bette T. M. Korber, Eric Hunter, Beatrice H. Hahn, and David C. Montefiori. Genetic and Neutralization Properties of Subtype C Human Immunodeficiency Virus Type 1 Molecular env Clones from Acute and Early Heterosexually Acquired Infections in Southern Africa. J. Virol., 80(23):11776-11790, Dec 2006. PubMed ID: 16971434. Show all entries for this paper.

Li2007a Yuxing Li, Stephen A. Migueles, Brent Welcher, Krisha Svehla, Adhuna Phogat, Mark K. Louder, Xueling Wu, George M. Shaw, Mark Connors, Richard T. Wyatt, and John R. Mascola. Broad HIV-1 Neutralization Mediated by CD4-Binding Site Antibodies. Nat. Med., 13(9):1032-1034, Sep 2007. PubMed ID: 17721546. Show all entries for this paper.

Li2009c Yuxing Li, Krisha Svehla, Mark K. Louder, Diane Wycuff, Sanjay Phogat, Min Tang, Stephen A. Migueles, Xueling Wu, Adhuna Phogat, George M. Shaw, Mark Connors, James Hoxie, John R. Mascola, and Richard Wyatt. Analysis of Neutralization Specificities in Polyclonal Sera Derived from Human Immunodeficiency Virus Type 1-Infected Individuals. J Virol, 83(2):1045-1059, Jan 2009. PubMed ID: 19004942. Show all entries for this paper.

Li2012 Yuxing Li, Sijy O'Dell, Richard Wilson, Xueling Wu, Stephen D. Schmidt, Carl-Magnus Hogerkorp, Mark K. Louder, Nancy S. Longo, Christian Poulsen, Javier Guenaga, Bimal K. Chakrabarti, Nicole Doria-Rose, Mario Roederer, Mark Connors, John R. Mascola, and Richard T. Wyatt. HIV-1 Neutralizing Antibodies Display Dual Recognition of the Primary and Coreceptor Binding Sites and Preferential Binding to Fully Cleaved Envelope Glycoproteins. J. Virol., 86(20):11231-11241, Oct 2012. PubMed ID: 22875963. Show all entries for this paper.

Li2017 Hongru Li, Chati Zony, Ping Chen, and Benjamin K. Chen. Reduced Potency and Incomplete Neutralization of Broadly Neutralizing Antibodies against Cell-to-Cell Transmission of HIV-1 with Transmitted Founder Envs. J. Virol., 91(9), 1 May 2017. PubMed ID: 28148796. Show all entries for this paper.

Liang2016 Yu Liang, Miklos Guttman, James A. Williams, Hans Verkerke, Daniel Alvarado, Shiu-Lok Hu, and Kelly K. Lee. Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan. J. Virol., 90(20):9224-9236, 15 Oct 2016. PubMed ID: 27489265. Show all entries for this paper.

Liao2004 Hua-Xin Liao, S Munir Alam, John R. Mascola, James Robinson, Benjiang Ma, David C. Montefiori, Maria Rhein, Laura L. Sutherland, Richard Scearce, and Barton F. Haynes. Immunogenicity of Constrained Monoclonal Antibody A32-Human Immunodeficiency Virus (HIV) Env gp120 Complexes Compared to That of Recombinant HIV Type 1 gp120 Envelope Glycoproteins. J. Virol., 78(10):5270-5278, May 2004. PubMed ID: 15113908. Show all entries for this paper.

Liao2006 Hua-Xin Liao, Laura L. Sutherland, Shi-Mao Xia, Mary E. Brock, Richard M. Scearce, Stacie Vanleeuwen, S. Munir Alam, Mildred McAdams, Eric A. Weaver, Zenaido Camacho, Ben-Jiang Ma, Yingying Li, Julie M. Decker, Gary J. Nabel, David C. Montefiori, Beatrice H. Hahn, Bette T. Korber, Feng Gao, and Barton F. Haynes. A Group M Consensus Envelope Glycoprotein Induces Antibodies That Neutralize Subsets of Subtype B and C HIV-1 Primary Viruses. Virology, 353(2):268-282, 30 Sep 2006. PubMed ID: 17039602. Show all entries for this paper.

Liao2013c Hua-Xin Liao, Chun-Yen Tsao, S. Munir Alam, Mark Muldoon, Nathan Vandergrift, Ben-Jiang Ma, Xiaozhi Lu, Laura L. Sutherland, Richard M. Scearce, Cindy Bowman, Robert Parks, Haiyan Chen, Julie H. Blinn, Alan Lapedes, Sydeaka Watson, Shi-Mao Xia, Andrew Foulger, Beatrice H. Hahn, George M. Shaw, Ron Swanstrom, David C. Montefiori, Feng Gao, Barton F. Haynes, and Bette Korber. Antigenicity and Immunogenicity of Transmitted/Founder, Consensus, and Chronic Envelope Glycoproteins of Human Immunodeficiency Virus Type 1. J. Virol., 87(8):4185-4201, Apr 2013. PubMed ID: 23365441. Show all entries for this paper.

Lin2007 George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109. Show all entries for this paper.

Liu2002 Xiao Song Liu, Wen Jun Liu, Kong Nan Zhao, Yue Hua Liu, Graham Leggatt, and Ian H. Frazer. Route of Administration of Chimeric BPV1 VLP Determines the Character of the Induced Immune Responses. Immunol. Cell Biol., 80(1):21-9, Feb 2002. PubMed ID: 11869359. Show all entries for this paper.

Liu2011c Pinghuang Liu, R. Glenn Overman, Nicole L. Yates, S. Munir Alam, Nathan Vandergrift, Yue Chen, Frederik Graw, Stephanie A. Freel, John C. Kappes, Christina Ochsenbauer, David C. Montefiori, Feng Gao, Alan S. Perelson, Myron S. Cohen, Barton F. Haynes, and Georgia D. Tomaras. Dynamic Antibody Specificities and Virion Concentrations in Circulating Immune Complexes in Acute to Chronic HIV-1 Infection. J. Virol., 85(21):11196-11207, Nov 2011. PubMed ID: 21865397. Show all entries for this paper.

Liu2014 Pinghuang Liu, Latonya D. Williams, Xiaoying Shen, Mattia Bonsignori, Nathan A. Vandergrift, R. Glenn Overman, M. Anthony Moody, Hua-Xin Liao, Daniel J. Stieh, Kerrie L. McCotter, Audrey L. French, Thomas J. Hope, Robin Shattock, Barton F. Haynes, and Georgia D. Tomaras. Capacity for Infectious HIV-1 Virion Capture Differs by Envelope Antibody Specificity. J. Virol., 88(9):5165-5170, May 2014. PubMed ID: 24554654. Show all entries for this paper.

Liu2015a Mengfei Liu, Guang Yang, Kevin Wiehe, Nathan I. Nicely, Nathan A. Vandergrift, Wes Rountree, Mattia Bonsignori, S. Munir Alam, Jingyun Gao, Barton F. Haynes, and Garnett Kelsoe. Polyreactivity and Autoreactivity among HIV-1 Antibodies. J. Virol., 89(1):784-798, Jan 2015. PubMed ID: 25355869. Show all entries for this paper.

Lorin2004 Clarisse Lorin, Lucile Mollet, Frédéric Delebecque, Chantal Combredet, Bruno Hurtrel, Pierre Charneau, Michel Brahic, and Frédéric Tangy. A Single Injection of Recombinant Measles Virus Vaccines Expressing Human Immunodeficiency Virus (HIV) Type 1 Clade B Envelope Glycoproteins Induces Neutralizing Antibodies and Cellular Immune Responses to HIV. J. Virol., 78(1):146-157, Jan 2004. PubMed ID: 14671096. Show all entries for this paper.

Louder2005 Mark K. Louder, Anna Sambor, Elena Chertova, Tai Hunte, Sarah Barrett, Fallon Ojong, Eric Sanders-Buell, Susan Zolla-Pazner, Francine E. McCutchan, James D. Roser, Dana Gabuzda, Jeffrey D. Lifson, and John R. Mascola. HIV-1 Envelope Pseudotyped Viral Vectors and Infectious Molecular Clones Expressing the Same Envelope Glycoprotein Have a Similar Neutralization Phenotype, but Culture in Peripheral Blood Mononuclear Cells Is Associated with Decreased Neutralization Sensitivity. Virology, 339(2):226-238, 1 Sep 2005. PubMed ID: 16005039. Show all entries for this paper.

Louis2003 John M. Louis, Issa Nesheiwat, LengChee Chang, G. Marius Clore, and Carole A. Bewley. Covalent Trimers of the Internal N-Terminal Trimeric Coiled-Coil of gp41 and Antibodies Directed against Them Are Potent Inhibitors of HIV Envelope-Mediated Cell Fusion. J. Biol. Chem., 278(22):20278-20285, 30 May 2003. PubMed ID: 12654905. Show all entries for this paper.

Louis2005 John M. Louis, Carole A. Bewley, Elena Gustchina, Annie Aniana, and G. Marius Clore. Characterization and HIV-1 Fusion Inhibitory Properties of Monoclonal Fabs Obtained from a Human Non-Immune Phage Library Selected against Diverse Epitopes of the Ectodomain of HIV-1 gp41. J. Mol. Biol., 353(5):945-951, 11 Nov 2005. PubMed ID: 16216270. Show all entries for this paper.

Luallen2008 Robert J. Luallen, Jianqiao Lin, Hu Fu, Karen K. Cai, Caroline Agrawal, Innocent Mboudjeka, Fang-Hua Lee, David Montefiori, David F. Smith, Robert W. Doms, and Yu Geng. An Engineered Saccharomyces cerevisiae Strain Binds the Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody 2G12 and Elicits Mannose-Specific gp120-Binding Antibodies. J. Virol., 82(13):6447-6457, Jul 2008. PubMed ID: 18434410. Show all entries for this paper.

Luallen2009 Robert J. Luallen, Hu Fu, Caroline Agrawal-Gamse, Innocent Mboudjeka, Wei Huang, Fang-Hua Lee, Lai-Xi Wang, Robert W. Doms, and Yu Geng. A Yeast Glycoprotein Shows High-Affinity Binding to the Broadly Neutralizing Human Immunodeficiency Virus Antibody 2G12 and Inhibits gp120 Interactions with 2G12 and DC-SIGN. J. Virol., 83(10):4861-4870, May 2009. PubMed ID: 19264785. Show all entries for this paper.

Luallen2010 Robert J Luallen, Caroline Agrawal-Gamse, Hu Fu, David F. Smith, Robert W. Doms, and Yu Geng. Antibodies against Man-alpha1,2-Man-alpha1,2-Man Oligosaccharide Structures Recognize Envelope Glycoproteins from HIV-1 and SIV Strains. Glycobiology, 20(3):280-286, Mar 2010. PubMed ID: 19920089. Show all entries for this paper.

Luo2010 Xin M. Luo, Margarida Y. Y. Lei, Rana A. Feidi, Anthony P. West, Jr., Alejandro Benjamin Balazs, Pamela J. Bjorkman, Lili Yang, and David Baltimore. Dimeric 2G12 as a Potent Protection against HIV-1. PLoS Pathog., 6(12):e1001225, 2010. PubMed ID: 21187894. Show all entries for this paper.

Lusso2005 Paolo Lusso, Patricia L. Earl, Francesca Sironi, Fabio Santoro, Chiara Ripamonti, Gabriella Scarlatti, Renato Longhi, Edward A. Berger, and Samuele E. Burastero. Cryptic Nature of a Conserved, CD4-Inducible V3 Loop Neutralization Epitope in the Native Envelope Glycoprotein Oligomer of CCR5-Restricted, but not CXCR4-Using, Primary Human Immunodeficiency Virus Type 1 Strains. J. Virol., 79(11):6957-6968, Jun 2005. PubMed ID: 15890935. Show all entries for this paper.

Lynch2011a Rebecca M. Lynch, Rong Rong, Saikat Boliar, Anurag Sethi, Bing Li, Joseph Mulenga, Susan Allen, James E. Robinson, S. Gnanakaran, and Cynthia A. Derdeyn. The B Cell Response Is Redundant and Highly Focused on V1V2 During Early Subtype C Infection in a Zambian Seroconverter. J. Virol., 85(2):905-915, Jan 2011. PubMed ID: 20980495. Show all entries for this paper.

Lynch2012 Rebecca M. Lynch, Lillian Tran, Mark K. Louder, Stephen D. Schmidt, Myron Cohen, CHAVI 001 Clinical Team Members, Rebecca DerSimonian, Zelda Euler, Elin S. Gray, Salim Abdool Karim, Jennifer Kirchherr, David C. Montefiori, Sengeziwe Sibeko, Kelly Soderberg, Georgia Tomaras, Zhi-Yong Yang, Gary J. Nabel, Hanneke Schuitemaker, Lynn Morris, Barton F. Haynes, and John R. Mascola. The Development of CD4 Binding Site Antibodies during HIV-1 Infection. J. Virol., 86(14):7588-7595, Jul 2012. PubMed ID: 22573869. Show all entries for this paper.

Ma2011 Ben-Jiang Ma, S. Munir Alam, Eden P. Go, Xiaozhi Lu, Heather Desaire, Georgia D. Tomaras, Cindy Bowman, Laura L. Sutherland, Richard M. Scearce, Sampa Santra, Norman L. Letvin, Thomas B. Kepler, Hua-Xin Liao, and Barton F. Haynes. Envelope Deglycosylation Enhances Antigenicity of HIV-1 gp41 Epitopes for Both Broad Neutralizing Antibodies and Their Unmutated Ancestor Antibodies. PLoS Pathog., 7(9):e1002200, Sep 2011. PubMed ID: 21909262. Show all entries for this paper.

Magnus2010 Carsten Magnus and Roland R. Regoes. Estimating the Stoichiometry of HIV Neutralization. PLoS Comput. Biol., 6(3):e1000713, Mar 2010. PubMed ID: 20333245. Show all entries for this paper.

Magnus2016 Carsten Magnus, Lucia Reh, and Alexandra Trkola. HIV-1 Resistance to Neutralizing Antibodies: Determination of Antibody Concentrations Leading to Escape Mutant Evolution. Virus Res., 218:57-70, 15 Jun 2016. PubMed ID: 26494166. Show all entries for this paper.

Mann2009 Axel M. Mann, Peter Rusert, Livia Berlinger, Herbert Kuster, Huldrych F. Günthard, and Alexandra Trkola. HIV Sensitivity to Neutralization Is Determined by Target and Virus Producer Cell Properties. AIDS, 23(13):1659-1667, 24 Aug 2009. PubMed ID: 19581791. Show all entries for this paper.

Mao2012 Youdong Mao, Liping Wang, Christopher Gu, Alon Herschhorn, Shi-Hua Xiang, Hillel Haim, Xinzhen Yang, and Joseph Sodroski. Subunit Organization of the Membrane-Bound HIV-1 Envelope Glycoprotein Trimer. Nat. Struct. Mol. Biol., 19(9):893-899, Sep 2012. PubMed ID: 22864288. Show all entries for this paper.

Marradi2011 Marco Marradi, Paolo Di Gianvincenzo, Pedro M. Enríquez-Navas, Olga M. Martínez-Ávila, Fabrizio Chiodo, Eloísa Yuste, Jesús Angulo, and Soledad Penadé. Gold Nanoparticles Coated with Oligomannosides of HIV-1 Glycoprotein gp120 Mimic the Carbohydrate Epitope of Antibody 2G12. J. Mol. Biol., 410(5):798-810, 29 Jul 2011. PubMed ID: 21440555. Show all entries for this paper.

Martin2008 Grégoire Martin, Yide Sun, Bernadette Heyd, Olivier Combes, Jeffrey B Ulmer, Anne Descours, Susan W Barnett, Indresh K Srivastava, and Loïc Martin. A Simple One-Step Method for the Preparation of HIV-1 Envelope Glycoprotein Immunogens Based on a CD4 Mimic Peptide. Virology, 381(2):241-250, 25 Nov 2008. PubMed ID: 18835005. Show all entries for this paper.

Martin2011 Grégoire Martin, Brian Burke, Robert Thaï, Antu K. Dey, Olivier Combes, Bernadette Heyd, Anthony R. Geonnotti, David C. Montefiori, Elaine Kan, Ying Lian, Yide Sun, Toufik Abache, Jeffrey B. Ulmer, Hocine Madaoui, Raphaël Guérois, Susan W. Barnett, Indresh K. Srivastava, Pascal Kessler, and Loïc Martin. Stabilization of HIV-1 Envelope in the CD4-Bound Conformation through Specific Cross-Linking of a CD4 Mimetic. J. Biol. Chem., 286(24):21706-21716, 17 Jun 2011. PubMed ID: 21487012. Show all entries for this paper.

Martines2012 Elena Martines, Isabel García, Marco Marradi, Daniel Padro, and Soledad Penadés. Dissecting the Carbohydrate Specificity of the Anti-HIV-1 2G12 Antibody by Single-Molecule Force Spectroscopy. Langmuir, 28(51):17726-17732, 21 Dec 2012. PubMed ID: 23198686. Show all entries for this paper.

Martinez2009 Valérie Martinez, Marie-Claude Diemert, Martine Braibant, Valérie Potard, Jean-Luc Charuel, Francis Barin, Dominique Costagliola, Eric Caumes, Jean-Pierre Clauvel, Brigitte Autran, Lucile Musset, and ALT ANRS CO15 Study Group. Anticardiolipin Antibodies in HIV Infection Are Independently Associated with Antibodies to the Membrane Proximal External Region of gp41 and with Cell-Associated HIV DNA and Immune Activation. Clin. Infect. Dis., 48(1):123-32, 1 Jan 2009. PubMed ID: 19035778. Show all entries for this paper.

Martin-Garcia2005 Julio Martín-García, Simon Cocklin, Irwin M. Chaiken, and Francisco González-Scarano. Interaction with CD4 and Antibodies to CD4-Induced Epitopes of the Envelope gp120 from a Microglial Cell-Adapted Human Immunodeficiency Virus Type 1 Isolate. J. Virol., 79(11):6703-6713, Jun 2005. PubMed ID: 15890908. Show all entries for this paper.

Marusic2009 Carla Marusic, Alessandro Vitale, Emanuela Pedrazzini, Marcello Donini, Lorenzo Frigerio, Ralph Bock, Philip J. Dix, Matthew S. McCabe, Michele Bellucci, and Eugenio Benvenuto. Plant-Based Strategies Aimed at Expressing HIV Antigens and Neutralizing Antibodies at High Levels. Nef as a Case Study. Transgenic Res., 18(4):499-512, Aug 2009. PubMed ID: 19169897. Show all entries for this paper.

Marzi2007 Andrea Marzi, Daniel A. Mitchell, Chawaree Chaipan, Tanja Fisch, Robert W. Doms, Mary Carrington, Ronald C. Desrosiers, and Stefan Pöhlmann. Modulation of HIV and SIV Neutralization Sensitivity by DC-SIGN and Mannose-Binding Lectin. Virology, 368(2):322-330, 25 Nov 2007. PubMed ID: 17659761. Show all entries for this paper.

Mascola1997 J. R. Mascola, M. K. Louder, T. C. VanCott, C. V. Sapan, J. S. Lambert, L. R. Muenz, B. Bunow, D. L. Birx, and M. L. Robb. Potent and Synergistic Neutralization of Human Immunodeficiency Virus (HIV) Type 1 Primary Isolates by Hyperimmune Anti-HIV Immunoglobulin Combined with Monoclonal Antibodies 2F5 and 2G12. J. Virol., 71:7198-7206, 1997. HIVIG derived from the plasma of HIV-1-infected donors, and MAbs 2F5 and 2G12 were tested against a panel of 15 clade B HIV-1 isolates, using a single concentration that is achievable in vivo (HIVIG, 2,500 microg/ml; MAbs, 25 microg/ml). While the three antibody reagents neutralized many of the viruses tested, potency varied. The virus neutralization achieved by double or triple combinations was generally equal to or greater than that predicted by the effect of individual antibodies, and the triple combination was shown to be synergistic and to have the greatest breadth and potency. Passive immunotherapy for treatment or prophylaxis of HIV-1 should consider mixtures of these potent neutralizing antibody reagents. PubMed ID: 9311792. Show all entries for this paper.

Mascola1999 J. R. Mascola, M. G. Lewis, G. Stiegler, D. Harris, T. C. VanCott, D. Hayes, M. K. Louder, C. R. Brown, C. V. Sapan, S. S. Frankel, Y. Lu, M. L. Robb, H. Katinger, and D. L. Birx. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J. Virol., 73(5):4009--18, May 1999. URL: http://jvi.asm.org/cgi/content/full/73/5/4009. PubMed ID: 10196297. Show all entries for this paper.

Mascola2000a John R. Mascola, Gabriela Stiegler, Thomas C. VanCott, Hermann Katinger, Calvin B. Carpenter, Chris E. Hanson, Holly Beary, Deborah Hayes, Sarah S. Frankel, Deborah L. Birx, and Mark G. Lewis. Protection of Macaques against Vaginal Transmission of a Pathogenic HIV-1/SIV Chimeric Virus by Passive Infusion of Neutralizing Antibodies. Nat. Med., 6(2):207-210, Feb 2000. PubMed ID: 10655111. Show all entries for this paper.

Mascola2001 J. R. Mascola and G. J. Nabel. Vaccines for the prevention of HIV-1 disease. Curr. Opin. Immunol., 13(4):489--95, Aug 2001. PubMed ID: 11498307. Show all entries for this paper.

Mascola2002 John R. Mascola. Passive Transfer Studies to Elucidate the Role of Antibody-Mediated Protection against HIV-1. Vaccine, 20(15):1922-1925, 6 May 2002. PubMed ID: 11983246. Show all entries for this paper.

Mascola2003 John R. Mascola, Mark G. Lewis, Thomas C. VanCott, Gabriela Stiegler, Hermann Katinger, Michael Seaman, Kristin Beaudry, Dan H. Barouch, Birgit Korioth-Schmitz, Georgia Krivulka, Anna Sambor, Brent Welcher, Daniel C. Douek, David C. Montefiori, John W. Shiver, Pascal Poignard, Dennis R. Burton, and Norman L. Letvin. Cellular Immunity Elicited by Human Immunodeficiency Virus Type 1/Simian Immunodeficiency Virus DNA Vaccination Does Not Augment the Sterile Protection Afforded by Passive Infusion of Neutralizing Antibodies. J. Virol., 77(19):10348-10356, Oct 2003. PubMed ID: 12970419. Show all entries for this paper.

Mascola2003a John R. Mascola. Defining the Protective Antibody Response for HIV-1. Curr. Mol. Med., 3(3):209-216, May 2003. PubMed ID: 12699358. Show all entries for this paper.

Mascola2010 John R. Mascola and David C. Montefiori. The Role of Antibodies in HIV Vaccines. Annu. Rev. Immunol., 28:413-444, Mar 2010. PubMed ID: 20192810. Show all entries for this paper.

Matyas2009 Gary R. Matyas, Zoltan Beck, Nicos Karasavvas, and Carl R. Alving. Lipid Binding Properties of 4E10, 2F5, and WR304 Monoclonal Antibodies that Neutralize HIV-1. Biochim. Biophys. Acta, 1788(3):660-665, Mar 2009. PubMed ID: 19100711. Show all entries for this paper.

McCann2005 C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016. Show all entries for this paper.

McCoy2015 Laura E. McCoy, Emilia Falkowska, Katie J. Doores, Khoa Le, Devin Sok, Marit J. van Gils, Zelda Euler, Judith A. Burger, Michael S. Seaman, Rogier W. Sanders, Hanneke Schuitemaker, Pascal Poignard, Terri Wrin, and Dennis R. Burton. Incomplete Neutralization and Deviation from Sigmoidal Neutralization Curves for HIV Broadly Neutralizing Monoclonal Antibodies. PLoS Pathog., 11(8):e1005110, Aug 2015. PubMed ID: 26267277. Show all entries for this paper.

McFadden2007 Karyn McFadden, Simon Cocklin, Hosahudya Gopi, Sabine Baxter, Sandya Ajith, Naheed Mahmood, Robin Shattock, and Irwin Chaiken. A Recombinant Allosteric Lectin Antagonist of HIV-1 Envelope gp120 Interactions. Proteins, 67(3):617-629, 15 May 2007. PubMed ID: 17348010. Show all entries for this paper.

McKeating1996b J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395. Show all entries for this paper.

McKeating1996c J. A. McKeating. Biological Consequences of Human Immunodeficiency Virus Type 1 Envelope Polymorphism: Does Variation Matter? 1995 Fleming Lecture. J. Gen. Virol., 77:2905-2919, 1996. PubMed ID: 9000081. Show all entries for this paper.

McKnight2007 Aine McKnight and Marlen M. I. Aasa-Chapman. Clade Specific Neutralising Vaccines for HIV: An Appropriate Target? Curr. HIV Res., 5(6):554-560, Nov 2007. PubMed ID: 18045111. Show all entries for this paper.

McLinden2013 Robert J. McLinden, Celia C. LaBranche, Agnès-Laurence Chenine, Victoria R. Polonis, Michael A. Eller, Lindsay Wieczorek, Christina Ochsenbauer, John C. Kappes, Stephen Perfetto, David C. Montefiori, Nelson L. Michael, and Jerome H. Kim. Detection of HIV-1 Neutralizing Antibodies in a Human CD4+/CXCR4+/CCR5+ T-Lymphoblastoid Cell Assay System. PLoS One, 8(11):e77756, 2013. PubMed ID: 24312168. Show all entries for this paper.

Mehandru2007 Saurabh Mehandru, Brigitta Vcelar, Terri Wrin, Gabriela Stiegler, Beda Joos, Hiroshi Mohri, Daniel Boden, Justin Galovich, Klara Tenner-Racz, Paul Racz, Mary Carrington, Christos Petropoulos, Hermann Katinger, and Martin Markowitz. Adjunctive Passive Immunotherapy in Human Immunodeficiency Virus Type 1-Infected Individuals Treated with Antiviral Therapy during Acute and Early Infection. J. Virol., 81(20):11016-11031, Oct 2007. PubMed ID: 17686878. Show all entries for this paper.

Melchers2012 Mark Melchers, Ilja Bontjer, Tommy Tong, Nancy P. Y. Chung, Per Johan Klasse, Dirk Eggink, David C. Montefiori, Maurizio Gentile, Andrea Cerutti, William C. Olson, Ben Berkhout, James M. Binley, John P. Moore, and Rogier W. Sanders. Targeting HIV-1 Envelope Glycoprotein Trimers to B Cells by Using APRIL Improves Antibody Responses. J. Virol., 86(5):2488-2500, Mar 2012. PubMed ID: 22205734. Show all entries for this paper.

Menendez2008 Alfredo Menendez, Daniel A. Calarese, Robyn L. Stanfield, Keith C. Chow, Chris N. Scanlan, Renate Kunert, Herman Katinger, Dennis R. Burton, Ian A. Wilson, and Jamie K. Scott. A Peptide Inhibitor of HIV-1 Neutralizing Antibody 2G12 Is Not a Structural Mimic of the Natural Carbohydrate Epitope on gp120. FASEB J., 22(5):1380-1392, May 2008. PubMed ID: 18198210. Show all entries for this paper.

Miglietta2014 Riccardo Miglietta, Claudia Pastori, Assunta Venuti, Christina Ochsenbauer, and Lucia Lopalco. Synergy in Monoclonal Antibody Neutralization of HIV-1 Pseudoviruses and Infectious Molecular Clones. J. Transl. Med., 12:346, 2014. PubMed ID: 25496375. Show all entries for this paper.

Miller2005 Michael D. Miller, Romas Geleziunas, Elisabetta Bianchi, Simon Lennard, Renee Hrin, Hangchun Zhang, Meiqing Lu, Zhiqiang An, Paolo Ingallinella, Marco Finotto, Marco Mattu, Adam C. Finnefrock, David Bramhill, James Cook, Debra M. Eckert, Richard Hampton, Mayuri Patel, Stephen Jarantow, Joseph Joyce, Gennaro Ciliberto, Riccardo Cortese, Ping Lu, William Strohl, William Schleif, Michael McElhaugh, Steven Lane, Christopher Lloyd, David Lowe, Jane Osbourn, Tristan Vaughan, Emilio Emini, Gaetano Barbato, Peter S. Kim, Daria J. Hazuda, John W. Shiver, and Antonello Pessi. A Human Monoclonal Antibody Neutralizes Diverse HIV-1 Isolates By Binding a Critical gp41 Epitope. Proc. Natl. Acad. Sci. U.S.A., 102(41):14759-14764, 11 Oct 2005. PubMed ID: 16203977. Show all entries for this paper.

Mo1997 H. Mo, L. Stamatatos, J. E. Ip, C. F. Barbas, P. W. H. I. Parren, D. R. Burton, J. P. Moore, and D. D. Ho. Human Immunodeficiency Virus Type 1 Mutants That Escape Neutralization by Human Monoclonal Antibody IgG1b12. J. Virol., 71:6869-6874, 1997. A JRCSF resistant variant was selected by culturing in the presence of IgG1b12. The resistant virus remained sensitive to 2G12 and 2F5 and to CD4-IgG, encouraging for the possibility of combination therapy. PubMed ID: 9261412. Show all entries for this paper.

Mohr2010 Emma L. Mohr, Jinhua Xiang, James H. McLinden, Thomas M. Kaufman, Qing Chang, David C. Montefiori, Donna Klinzman, and Jack T. Stapleton. GB Virus Type C Envelope Protein E2 Elicits Antibodies That React with a Cellular Antigen on HIV-1 Particles and Neutralize Diverse HIV-1 Isolates. J. Immunol., 185(7):4496-4505, 1 Oct 2010. PubMed ID: 20826757. Show all entries for this paper.

Moldt2012a Brian Moldt, Eva G. Rakasz, Niccole Schultz, Po-Ying Chan-Hui, Kristine Swiderek, Kimberly L. Weisgrau, Shari M. Piaskowski, Zachary Bergman, David I. Watkins, Pascal Poignard, and Dennis R. Burton. Highly Potent HIV-Specific Antibody Neutralization In Vitro Translates into Effective Protection against Mucosal SHIV Challenge In Vivo. Proc. Natl. Acad. Sci. U.S.A., 109(46):18921-18925, 13 Nov 2012. PubMed ID: 23100539. Show all entries for this paper.

Mondor1998 I. Mondor, S. Ugolini, and Q. J. Sattentau. Human Immunodeficiency Virus Type 1 Attachment to HeLa CD4 Cells Is CD4 Independent and Gp120 Dependent and Requires Cell Surface Heparans. J. Virol., 72:3623-3634, 1998. PubMed ID: 9557643. Show all entries for this paper.

Montefiori1999 D. Montefiori and T. Evans. Toward an HIV Type 1 Vaccine That Generates Potent Broadly Cross-Reactive Neutralizing Antibodies. AIDS Res. Hum. Retroviruses, 15:689-698, 1999. PubMed ID: 10357464. Show all entries for this paper.

Montefiori2003 David C. Montefiori, Marcus Altfeld, Paul K. Lee, Miroslawa Bilska, Jintao Zhou, Mary N. Johnston, Feng Gao, Bruce D. Walker, and Eric S. Rosenberg. Viremia Control Despite Escape from a Rapid and Potent Autologous Neutralizing Antibody Response after Therapy Cessation in an HIV-1-Infected Individual. J. Immunol., 170(7):3906-3914, Apr 2003. PubMed ID: 12646660. Show all entries for this paper.

Montefiori2005 David C. Montefiori. Neutralizing Antibodies Take a Swipe at HIV In Vivo. Nat. Med., 11(6):593-594, Jun 2005. PubMed ID: 15937465. Show all entries for this paper.

Montefiori2009 David C. Montefiori and John R. Mascola. Neutralizing Antibodies against HIV-1: Can We Elicit Them with Vaccines and How Much Do We Need? Curr. Opin. HIV AIDS, 4(5):347-351, Sep 2009. PubMed ID: 20048696. Show all entries for this paper.

Moody2010 M. Anthony Moody, Hua-Xin Liao, S. Munir Alam, Richard M. Scearce, M. Kelly Plonk, Daniel M. Kozink, Mark S. Drinker, Ruijun Zhang, Shi-Mao Xia, Laura L. Sutherland, Georgia D. Tomaras, Ian P. Giles, John C. Kappes, Christina Ochsenbauer-Jambor, Tara G. Edmonds, Melina Soares, Gustavo Barbero, Donald N. Forthal, Gary Landucci, Connie Chang, Steven W. King, Anita Kavlie, Thomas N. Denny, Kwan-Ki Hwang, Pojen P. Chen, Philip E. Thorpe, David C. Montefiori, and Barton F. Haynes. Anti-Phospholipid Human Monoclonal Antibodies Inhibit CCR5-Tropic HIV-1 and Induce beta-Chemokines. J. Exp. Med., 207(4):763-776, 12 Apr 2010. PubMed ID: 20368576. Show all entries for this paper.

Moog2014 C. Moog, N. Dereuddre-Bosquet, J.-L. Teillaud, M. E. Biedma, V. Holl, G. Van Ham, L. Heyndrickx, A. Van Dorsselaer, D. Katinger, B. Vcelar, S. Zolla-Pazner, I. Mangeot, C. Kelly, R. J. Shattock, and R. Le Grand. Protective Effect of Vaginal Application of Neutralizing and Nonneutralizing Inhibitory Antibodies Against Vaginal SHIV Challenge in Macaques. Mucosal Immunol., 7(1):46-56, Jan 2014. PubMed ID: 23591718. Show all entries for this paper.

Moore1995c J. P. Moore and D. D. Ho. HIV-1 Neutralization: The Consequences of Adaptation to Growth on Transformed T-Cells. AIDS, 9(suppl A):S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579. Show all entries for this paper.

Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.

Moore1997 J. Moore and A. Trkola. HIV Type 1 Coreceptors, Neutralization Serotypes and Vaccine Development. AIDS Res. Hum. Retroviruses, 13:733-736, 1997. PubMed ID: 9171216. Show all entries for this paper.

Moore2001 J. P. Moore, P. W. Parren, and D. R. Burton. Genetic subtypes, humoral immunity, and human immunodeficiency virus type 1 vaccine development. J. Virol., 75(13):5721--9, Jul 2001. URL: http://jvi.asm.org/cgi/content/full/75/13/5721. PubMed ID: 11390574. Show all entries for this paper.

Moore2006 Penny L. Moore, Emma T. Crooks, Lauren Porter, Ping Zhu, Charmagne S. Cayanan, Henry Grise, Paul Corcoran, Michael B. Zwick, Michael Franti, Lynn Morris, Kenneth H. Roux, Dennis R. Burton, and James M. Binley. Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1. J. Virol., 80(5):2515-2528, Mar 2006. PubMed ID: 16474158. Show all entries for this paper.

Moore2009 Penny L. Moore, Elin S. Gray, and Lynn Morris. Specificity of the Autologous Neutralizing Antibody Response. Curr. Opin. HIV AIDS, 4(5):358-363, Sep 2009. PubMed ID: 20048698. Show all entries for this paper.

Moore2012 Penny L. Moore, Elin S. Gray, C. Kurt Wibmer, Jinal N. Bhiman, Molati Nonyane, Daniel J. Sheward, Tandile Hermanus, Shringkhala Bajimaya, Nancy L. Tumba, Melissa-Rose Abrahams, Bronwen E. Lambson, Nthabeleng Ranchobe, Lihua Ping, Nobubelo Ngandu, Quarraisha Abdool Karim, Salim S. Abdool Karim, Ronald I. Swanstrom, Michael S. Seaman, Carolyn Williamson, and Lynn Morris. Evolution of an HIV Glycan-Dependent Broadly Neutralizing Antibody Epitope through Immune Escape. Nat. Med., 18(11):1688-1692, Nov 2012. PubMed ID: 23086475. Show all entries for this paper.

Mouquet2011 Hugo Mouquet, Florian Klein, Johannes F. Scheid, Malte Warncke, John Pietzsch, Thiago Y. K. Oliveira, Klara Velinzon, Michael S. Seaman, and Michel C. Nussenzweig. Memory B Cell Antibodies to HIV-1 gp140 Cloned from Individuals Infected with Clade A and B Viruses. PLoS One, 6(9):e24078, 2011. PubMed ID: 21931643. Show all entries for this paper.

Mouquet2012a Hugo Mouquet, Louise Scharf, Zelda Euler, Yan Liu, Caroline Eden, Johannes F. Scheid, Ariel Halper-Stromberg, Priyanthi N. P. Gnanapragasam, Daniel I. R. Spencer, Michael S. Seaman, Hanneke Schuitemaker, Ten Feizi, Michel C. Nussenzweig, and Pamela J. Bjorkman. Complex-Type N-Glycan Recognition by Potent Broadly Neutralizing HIV Antibodies. Proc. Natl. Acad. Sci. U.S.A, 109(47):E3268-E3277, 20 Nov 2012. PubMed ID: 23115339. Show all entries for this paper.

Murin2014 Charles D. Murin, Jean-Philippe Julien, Devin Sok, Robyn L. Stanfield, Reza Khayat, Albert Cupo, John P. Moore, Dennis R. Burton, Ian A. Wilson, and Andrew B. Ward. Structure of 2G12 Fab2 in Complex with Soluble and Fully Glycosylated HIV-1 Env by Negative-Stain Single-Particle Electron Microscopy. J. Virol., 88(17):10177-10188, 1 Sep 2014. PubMed ID: 24965454. Show all entries for this paper.

Naarding2007 Marloes A. Naarding, Elly Baan, Georgios Pollakis, and William A. Paxton. Effect of Chloroquine on Reducing HIV-1 Replication In Vitro and the DC-SIGN Mediated Transfer of Virus to CD4+ T-Lymphocytes. Retrovirology, 4:6, 2007. PubMed ID: 17263871. Show all entries for this paper.

Nabatov2004 Alexey A. Nabatov, Georgios Pollakis, Thomas Linnemann, Aletta Kliphius, Moustapha I. M. Chalaby, and William A. Paxton. Intrapatient Alterations in the Human Immunodeficiency Virus Type 1 gp120 V1V2 and V3 Regions Differentially Modulate Coreceptor Usage, Virus Inhibition by CC/CXC Chemokines, Soluble CD4, and the b12 and 2G12 Monoclonal Antibodies. J. Virol., 78(1):524-530, Jan 2004. PubMed ID: 14671134. Show all entries for this paper.

Nabel2005 Gary J. Nabel. Close to the Edge: Neutralizing the HIV-1 Envelope. Science, 308(5730):1878-1879, 24 Jun 2005. PubMed ID: 15976295. Show all entries for this paper.

Nakowitsch2005 Sabine Nakowitsch, Heribert Quendler, Helga Fekete, Renate Kunert, Hermann Katinger, and Gabriela Stiegler. HIV-1 Mutants Escaping Neutralization by the Human Antibodies 2F5, 2G12, and 4E10: In Vitro Experiments Versus Clinical Studies. AIDS, 19(17):1957-1966, 18 Nov 2005. PubMed ID: 16260901. Show all entries for this paper.

Nandi2010 Avishek Nandi, Christine L. Lavine, Pengcheng Wang, Inna Lipchina, Paul A. Goepfert, George M. Shaw, Georgia D. Tomaras, David C. Montefiori, Barton F. Haynes, Philippa Easterbrook, James E. Robinson, Joseph G. Sodroski, Xinzhen Yang, and NIAID Center for HIV/AIDS Vaccine Immunology. Epitopes for Broad and Potent Neutralizing Antibody Responses during Chronic Infection with Human Immunodeficiency Virus Type 1. Virology, 396(2):339-348, 20 Jan 2010. PubMed ID: 19922969. Show all entries for this paper.

Narayan2013 Kristin M. Narayan, Nitish Agrawal, Sean X. Du, Janelle E. Muranaka, Katherine Bauer, Daniel P. Leaman, Pham Phung, Kay Limoli, Helen Chen, Rebecca I. Boenig, Terri Wrin, Michael B. Zwick, and Robert G. Whalen. Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate. PLoS One, 8(1):e52732 doi, 2013. PubMed ID: 23326351 Show all entries for this paper.

Nie2010 Jianhui Nie, Chuntao Zhang, Wei Liu, Xueling Wu, Feng Li, Suting Wang, Fuxiong Liang, Aijing Song, and Youchun Wang. Genotypic and Phenotypic Characterization of HIV-1 CRF01\_AE env Molecular Clones from Infections in China. J. Acquir. Immune Defic. Syndr., 53(4):440-450, 1 Apr 2010. PubMed ID: 20090544. Show all entries for this paper.

Nie2020 Jianhui Nie, Weijin Huang, Qiang Liu, and Youchun Wang. HIV-1 pseudoviruses constructed in China regulatory laboratory. Emerg Microbes Infect, 9(1):32-41 doi, 2020. PubMed ID: 31859609 Show all entries for this paper.

Nishiyama2009 Yasuhiro Nishiyama, Stephanie Planque, Yukie Mitsuda, Giovanni Nitti, Hiroaki Taguchi, Lei Jin, Jindrich Symersky, Stephane Boivin, Marcin Sienczyk, Maria Salas, Carl V. Hanson, and Sudhir Paul. Toward Effective HIV Vaccination: Induction of Binary Epitope Reactive Antibodies with Broad HIV Neutralizing Activity. J. Biol. Chem., 284(44):30627-30642, 30 Oct 2009. PubMed ID: 19726674. Show all entries for this paper.

Nolan2009 Katrina M. Nolan, Gregory Q. Del Prete, Andrea P. O. Jordan, Beth Haggarty, Josephine Romano, George J. Leslie, and James A. Hoxie. Characterization of a Human Immunodeficiency Virus Type 1 V3 Deletion Mutation That Confers Resistance to CCR5 Inhibitors and the Ability to Use Aplaviroc-Bound Receptor. J. Virol., 83(8):3798-3809, Apr 2009. PubMed ID: 19193800. Show all entries for this paper.

Nora2008 Tamara Nora, Francine Bouchonnet, Béatrice Labrosse, Charlotte Charpentier, Fabrizio Mammano, François Clavel, and Allan J. Hance. Functional Diversity of HIV-1 Envelope Proteins Expressed by Contemporaneous Plasma Viruses. Retrovirology, 5:23, 2008. PubMed ID: 18312646. Show all entries for this paper.

Ofek2004 Gilad Ofek, Min Tang, Anna Sambor, Hermann Katinger, John R. Mascola, Richard Wyatt, and Peter D. Kwong. Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope. J. Virol., 78(19):10724-10737, Oct 2004. PubMed ID: 15367639. Show all entries for this paper.

Ohagen2003 Asa Ohagen, Amy Devitt, Kevin J. Kunstman, Paul R. Gorry, Patrick P. Rose, Bette Korber, Joann Taylor, Robert Levy, Robert L. Murphy, Steven M. Wolinsky, and Dana Gabuzda. Genetic and Functional Analysis of Full-Length Human Immunodeficiency Virus Type 1 env Genes Derived from Brain and Blood of Patients with AIDS. J. Virol., 77(22):12336-12345, Nov 2003. PubMed ID: 14581570. Show all entries for this paper.

Opalka2004 David Opalka, Antonello Pessi, Elisabetta Bianchi, Gennaro Ciliberto, William Schleif, Michael McElhaugh, Renee Danzeisen, Romas Geleziunas, Michael Miller, Debra M. Eckert, David Bramhill, Joseph Joyce, James Cook, William Magilton, John Shiver, Emilio Emini, and Mark T. Esser. Analysis of the HIV-1 gp41 Specific Immune Response Using a Multiplexed Antibody Detection Assay. J. Immunol. Methods, 287(1-2):49-65, Apr 2004. PubMed ID: 15099755. Show all entries for this paper.

ORourke2009 Sara M. O'Rourke, Becky Schweighardt, William G. Scott, Terri Wrin, Dora P. A. J. Fonseca, Faruk Sinangil, and Phillip W. Berman. Novel Ring Structure in the gp41 Trimer of Human Immunodeficiency Virus Type 1 That Modulates Sensitivity and Resistance to Broadly Neutralizing Antibodies. J. Virol., 83(15):7728-7738, Aug 2009. PubMed ID: 19474108. Show all entries for this paper.

ORourke2010 Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Dora P. A. J. Fonseca, Karianne Terry, Terri Wrin, Faruk Sinangil, and Phillip W. Berman. Mutation at a Single Position in the V2 Domain of the HIV-1 Envelope Protein Confers Neutralization Sensitivity to a Highly Neutralization-Resistant Virus. J. Virol., 84(21):11200-11209, Nov 2010. PubMed ID: 20702624. Show all entries for this paper.

Overbaugh2012 Julie Overbaugh and Lynn Morris. The Antibody Response against HIV-1. Cold Spring Harb. Perspect. Med., 2(1):a007039, Jan 2012. PubMed ID: 22315717. Show all entries for this paper.

Pahar2006 Bapi Pahar, Mayra A. Cantu, Wei Zhao, Marcelo J. Kuroda, Ronald S. Veazey, David C. Montefiori, John D. Clements, Pyone P. Aye, Andrew A. Lackner, Karin Lovgren-Bengtsson, and Karol Sestak. Single Epitope Mucosal Vaccine Delivered via Immuno-Stimulating Complexes Induces Low Level of Immunity Against Simian-HIV. Vaccine, 24(47-48):6839-6849, 17 Nov 2006. PubMed ID: 17050045. Show all entries for this paper.

Pancera2005 Marie Pancera and Richard Wyatt. Selective Recognition of Oligomeric HIV-1 Primary Isolate Envelope Glycoproteins by Potently Neutralizing Ligands Requires Efficient Precursor Cleavage. Virology, 332(1):145-156, 5 Feb 2005. PubMed ID: 15661147. Show all entries for this paper.

Pantophlet2003 Ralph Pantophlet, Erica Ollmann Saphire, Pascal Poignard, Paul W. H. I. Parren, Ian A. Wilson, and Dennis R. Burton. Fine Mapping of the Interaction of Neutralizing and Nonneutralizing Monoclonal Antibodies with the CD4 Binding Site of Human Immunodeficiency Virus Type 1 gp120. J. Virol., 77(1):642-658, Jan 2003. PubMed ID: 12477867. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.

Pantophlet2006 Ralph Pantophlet and Dennis R. Burton. GP120: Target for Neutralizing HIV-1 Antibodies. Annu. Rev. Immunol., 24:739-769, 2006. PubMed ID: 16551265. Show all entries for this paper.

Pantophlet2009 Ralph Pantophlet, Meng Wang, Rowena O. Aguilar-Sino, and Dennis R. Burton. The Human Immunodeficiency Virus Type 1 Envelope Spike of Primary Viruses Can Suppress Antibody Access to Variable Regions. J. Virol., 83(4):1649-1659, Feb 2009. PubMed ID: 19036813. Show all entries for this paper.

Pantophlet2010 Ralph Pantophlet. Antibody Epitope Exposure and Neutralization of HIV-1. Curr. Pharm. Des., 16(33):3729-3743, 2010. PubMed ID: 21128886. Show all entries for this paper.

Park2000 E. J. Park, M. K. Gorny, S. Zolla-Pazner, and G. V. Quinnan. A global neutralization resistance phenotype of human immunodeficiency virus type 1 is determined by distinct mechanisms mediating enhanced infectivity and conformational change of the envelope complex. J. Virol., 74:4183-91, 2000. PubMed ID: 10756031. Show all entries for this paper.

Parren1997 P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324. Show all entries for this paper.

Parren1998 P. W. Parren, I. Mondor, D. Naniche, H. J. Ditzel, P. J. Klasse, D. R. Burton, and Q. J. Sattentau. Neutralization of human immunodeficiency virus type 1 by antibody to gp120 is determined primarily by occupancy of sites on the virion irrespective of epitope specificity. J. Virol., 72:3512-9, 1998. The authors propose that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Neutralization was assayed T-cell-line-adapted HIV-1 isolates. Binding of Fabs to monomeric rgp120 was not correlated with binding to functional oligomeric gp120 or neutralization, while binding to functional oligomeric gp120 was highly correlated with neutralization. The ratios of oligomer binding/neutralization were similar for antibodies to different neutralization epitopes, with a few exceptions. PubMed ID: 9557629. Show all entries for this paper.

Parren1998a P. W. Parren, M. Wang, A. Trkola, J. M. Binley, M. Purtscher, H. Katinger, J. P. Moore, and D. R. Burton. Antibody neutralization-resistant primary isolates of human immunodeficiency virus type 1. J. Virol., 72:10270-4, 1998. PubMed ID: 9811774. Show all entries for this paper.

Parren1999 P. W. Parren, J. P. Moore, D. R. Burton, and Q. J. Sattentau. The Neutralizing Antibody Response to HIV-1: Viral Evasion and Escape from Humoral Immunity. AIDS, 13(Suppl A):S137-162, 1999. PubMed ID: 10885772. Show all entries for this paper.

Pashov2005 Anastas Pashov, Stewart MacLeod, Rinku Saha, Marty Perry, Thomas C. VanCott, and Thomas Kieber-Emmons. Concanavalin A Binding to HIV Envelope Protein Is Less Sensitive to Mutations in Glycosylation Sites than Monoclonal Antibody 2G12. Glycobiology, 15(10):994-1001, Oct 2005. PubMed ID: 15917430. Show all entries for this paper.

Pashov2005a Anastas Pashov, Gabriela Canziani, Stewart Macleod, Jason Plaxco, Behjatolah Monzavi-Karbassi, and Thomas Kieber-Emmons. Targeting Carbohydrate Antigens in HIV Vaccine Development. Vaccine, 23(17-18):2168-2175, 18 Mar 2005. PubMed ID: 15755589. Show all entries for this paper.

Pashov2006 Anastas D. Pashov, Jason Plaxco, Srinivas V. Kaveri, Behjatolah Monzavi-Karbassi, Donald Harn, and Thomas Kieber-Emmons. Multiple Antigenic Mimotopes of HIV Carbohydrate Antigens: Relating Structure and Antigenicity. J. Biol. Chem., 281(40):29675-29683, 6 Oct 2006. PubMed ID: 16899462. Show all entries for this paper.

Patel2008 Milloni B Patel, Noah G. Hoffman, and Ronald Swanstrom. Subtype-Specific Conformational Differences within the V3 Region of Subtype B and Subtype C Human Immunodeficiency Virus Type 1 Env Proteins. J. Virol., 82(2):903-916, Jan 2008. PubMed ID: 18003735. Show all entries for this paper.

Peachman2010a Kristina K. Peachman, Lindsay Wieczorek, Victoria R. Polonis, Carl R. Alving, and Mangala Rao. The Effect of sCD4 on the Binding and Accessibility of HIV-1 gp41 MPER Epitopes to Human Monoclonal Antibodies. Virology, 408(2):213-223, 20 Dec 2010. PubMed ID: 20961591. Show all entries for this paper.

Pegu2017 Amarendra Pegu, Ann J. Hessell, John R. Mascola, and Nancy L. Haigwood. Use of Broadly Neutralizing Antibodies for HIV-1 Prevention. Immunol. Rev., 275(1):296-312, Jan 2017. PubMed ID: 28133803. Show all entries for this paper.

Pejchal2011 Robert Pejchal, Katie J. Doores, Laura M. Walker, Reza Khayat, Po-Ssu Huang, Sheng-Kai Wang, Robyn L. Stanfield, Jean-Philippe Julien, Alejandra Ramos, Max Crispin, Rafael Depetris, Umesh Katpally, Andre Marozsan, Albert Cupo, Sebastien Maloveste, Yan Liu, Ryan McBride, Yukishige Ito, Rogier W. Sanders, Cassandra Ogohara, James C. Paulson, Ten Feizi, Christopher N. Scanlan, Chi-Huey Wong, John P. Moore, William C. Olson, Andrew B. Ward, Pascal Poignard, William R. Schief, Dennis R. Burton, and Ian A. Wilson. A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield. Science, 334(6059):1097-1103, 25 Nov 2011. PubMed ID: 21998254. Show all entries for this paper.

Perdomo2008 Maria F. Perdomo, Michael Levi, Matti Sällberg, and Anders Vahlne. Neutralization of HIV-1 by Redirection of Natural Antibodies. Proc. Natl. Acad. Sci. U.S.A., 105(34):12515-12520, 26 Aug 2008. PubMed ID: 18719129. Show all entries for this paper.

Peressin2011 M. Peressin, V. Holl, S. Schmidt, T. Decoville, D. Mirisky, A. Lederle, M. Delaporte, K. Xu, A. M. Aubertin, and C. Moog. HIV-1 Replication in Langerhans and Interstitial Dendritic Cells Is Inhibited by Neutralizing and Fc-Mediated Inhibitory Antibodies. J. Virol., 85(2):1077-1085, Jan 2011. PubMed ID: 21084491. Show all entries for this paper.

Perez2009 Lautaro G. Perez, Matthew R. Costa, Christopher A. Todd, Barton F. Haynes, and David C. Montefiori. Utilization of Immunoglobulin G Fc Receptors by Human Immunodeficiency Virus Type 1: A Specific Role for Antibodies against the Membrane-Proximal External Region of gp41. J. Virol., 83(15):7397-7410, Aug 2009. PubMed ID: 19458010. Show all entries for this paper.

Peters2008a Paul J. Peters, Maria J. Duenas-Decamp, W. Matthew Sullivan, Richard Brown, Chiambah Ankghuambom, Katherine Luzuriaga, James Robinson, Dennis R. Burton, Jeanne Bell, Peter Simmonds, Jonathan Ball, and Paul R. Clapham. Variation in HIV-1 R5 Macrophage-Tropism Correlates with Sensitivity to Reagents that Block Envelope: CD4 Interactions But Not with Sensitivity to Other Entry Inhibitors. Retrovirology, 5:5, 2008. PubMed ID: 18205925. Show all entries for this paper.

Pham2014 Tram N. Q. Pham, Sabelo Lukhele, Fadi Hajjar, Jean-Pierre Routy, and Éric A. Cohen. HIV Nef and Vpu Protect HIV-Infected CD4+ T Cells from Antibody-Mediated Cell Lysis through Down-Modulation of CD4 and BST2. Retrovirology, 11:15, 2014. PubMed ID: 24498878. Show all entries for this paper.

Phogat2007 S. Phogat, R. T. Wyatt, and G. B. Karlsson Hedestam. Inhibition of HIV-1 Entry by Antibodies: Potential Viral and Cellular Targets. J. Intern. Med., 262(1):26-43, Jul 2007. PubMed ID: 17598813. Show all entries for this paper.

Pinter2004 Abraham Pinter, William J. Honnen, Yuxian He, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection. J. Virol., 78(10):5205-5215, May 2004. PubMed ID: 15113902. Show all entries for this paper.

Pinter2005 Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930. Show all entries for this paper.

Platis2009a Dimitris Platis and Nikolaos E. Labrou. Application of a PEG/Salt Aqueous Two-Phase Partition System for the Recovery of Monoclonal Antibodies from Unclarified Transgenic Tobacco Extract. Biotechnol. J., 4(9):1320-1327, Sep 2009. PubMed ID: 19557796. Show all entries for this paper.

Platt2012 Emily J. Platt, Michelle M. Gomes, and David Kabat. Kinetic Mechanism for HIV-1 Neutralization by Antibody 2G12 Entails Reversible Glycan Binding That Slows Cell Entry. Proc. Natl. Acad. Sci. U.S.A., 109(20):7829-7834, 15 May 2012. PubMed ID: 22547820. Show all entries for this paper.

Pluckthun2010 Andreas Plückthun. HIV: Antibodies with a Split Personality. Nature, 467(7315):537-538, 30 Sep 2010. PubMed ID: 20882002. Show all entries for this paper.

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Pollara2013 Justin Pollara, Mattia Bonsignori, M. Anthony Moody, Marzena Pazgier, Barton F. Haynes, and Guido Ferrari. Epitope Specificity of Human Immunodeficiency Virus-1 Antibody Dependent Cellular Cytotoxicity (ADCC) Responses. Curr. HIV Res., 11(5):378-387, Jul 2013. PubMed ID: 24191939. Show all entries for this paper.

Poon2005 B. Poon, J. F. Hsu, V. Gudeman, I. S. Y. Chen, and K. Grovit-Ferbas. Formaldehyde-Treated, Heat-Inactivated Virions with Increased Human Immunodeficiency Virus Type 1 Env Can Be Used To Induce High-Titer Neutralizing Antibody Responses. J. Virol., 79(16):10210-10217, Aug 2005. PubMed ID: 16051814. Show all entries for this paper.

Prevost2017 Jérémie Prévost, Daria Zoubchenok, Jonathan Richard, Maxime Veillette, Beatriz Pacheco, Mathieu Coutu, Nathalie Brassard, Matthew S. Parsons, Kiat Ruxrungtham, Torsak Bunupuradah, Sodsai Tovanabutra, Kwan-Ki Hwang, M. Anthony Moody, Barton F. Haynes, Mattia Bonsignori, Joseph Sodroski, Daniel E. Kaufmann, George M. Shaw, Agnes L. Chenine, and Andrés Finzi. Influence of the Envelope gp120 Phe 43 Cavity on HIV-1 Sensitivity to Antibody-Dependent Cell-Mediated Cytotoxicity Responses. J. Virol., 91(7), 1 Apr 2017. PubMed ID: 28100618. Show all entries for this paper.

Prevost2018 Jérémie Prévost, Jonathan Richard, Shilei Ding, Beatriz Pacheco, Roxanne Charlebois, Beatrice H Hahn, Daniel E Kaufmann, and Andrés Finzi. Envelope Glycoproteins Sampling States 2/3 Are Susceptible to ADCC by Sera from HIV-1-Infected Individuals. Virology, 515:38-45, Feb 2018. PubMed ID: 29248757. Show all entries for this paper.

Prigent2018 Julie Prigent, Annaëlle Jarossay, Cyril Planchais, Caroline Eden, Jérémy Dufloo, Ayrin Kök, Valérie Lorin, Oxana Vratskikh, Thérèse Couderc, Timothée Bruel, Olivier Schwartz, Michael S. Seaman, Ohlenschläger, Jordan D. Dimitrov, and Hugo Mouquet. Conformational Plasticity in Broadly Neutralizing HIV-1 Antibodies Triggers Polyreactivity. Cell Rep., 23(9):2568-2581, 29 May 2018. PubMed ID: 29847789. Show all entries for this paper.

Pugach2004 Pavel Pugach, Shawn E. Kuhmann, Joann Taylor, Andre J. Marozsan, Amy Snyder, Thomas Ketas, Steven M. Wolinsky, Bette T. Korber, and John P. Moore. The Prolonged Culture of Human Immunodeficiency Virus Type 1 in Primary Lymphocytes Increases its Sensitivity to Neutralization by Soluble CD4. Virology, 321(1):8-22, 30 Mar 2004. PubMed ID: 15033560. Show all entries for this paper.

Pugach2008 Pavel Pugach, Thomas J. Ketas, Elizabeth Michael, and John P. Moore. Neutralizing Antibody and Anti-Retroviral Drug Sensitivities of HIV-1 Isolates Resistant to Small Molecule CCR5 Inhibitors. Virology, 377(2):401-407, 1 Aug 2008. PubMed ID: 18519143. Show all entries for this paper.

Pugach2015 Pavel Pugach, Gabriel Ozorowski, Albert Cupo, Rajesh Ringe, Anila Yasmeen, Natalia de Val, Ronald Derking, Helen J. Kim, Jacob Korzun, Michael Golabek, Kevin de Los Reyes, Thomas J. Ketas, Jean-Philippe Julien, Dennis R. Burton, Ian A. Wilson, Rogier W. Sanders, P. J. Klasse, Andrew B. Ward, and John P. Moore. A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene. J. Virol., 89(6):3380-3395, Mar 2015. PubMed ID: 25589637. Show all entries for this paper.

Quakkelaar2007a Esther D. Quakkelaar, Floris P. J. van Alphen, Brigitte D. M. Boeser-Nunnink, Ad C. van Nuenen, Ralph Pantophlet, and Hanneke Schuitemaker. Susceptibility of Recently Transmitted Subtype B Human Immunodeficiency Virus Type 1 Variants to Broadly Neutralizing Antibodies. J. Virol., 81(16):8533-8542, Aug 2007. PubMed ID: 17522228. Show all entries for this paper.

Rademacher2008 Thomas Rademacher, Markus Sack, Elsa Arcalis, Johannes Stadlmann, Simone Balzer, Friedrich Altmann, Heribert Quendler, Gabriela Stiegler, Renate Kunert, Rainer Fischer, and Eva Stoger. Recombinant Antibody 2G12 Produced in Maize Endosperm Efficiently Neutralizes HIV-1 and Contains Predominantly Single-GlcNAc N-Glycans. Plant Biotechnol. J., 6(2):189-201, Feb 2008. PubMed ID: 17979949. Show all entries for this paper.

Rainwater2007 Stephanie M. J. Rainwater, Xueling Wu, Ruth Nduati, Rebecca Nedellec, Donald Mosier, Grace John-Stewart, Dorothy Mbori-Ngacha, and Julie Overbaugh. Cloning and Characterization of Functional Subtype A HIV-1 Envelope Variants Transmitted Through Breastfeeding. Curr. HIV Res., 5(2):189-197, Mar 2007. PubMed ID: 17346133. Show all entries for this paper.

Raja2003 Aarti Raja, Miro Venturi, Peter Kwong, and Joseph Sodroski. CD4 Binding Site Antibodies Inhibit Human Immunodeficiency Virus gp120 Envelope Glycoprotein Interaction with CCR5. J. Virol., 77(1):713-718, Jan 2003. PubMed ID: 12477875. Show all entries for this paper.

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Reeves2005 Jacqueline D. Reeves, Fang-Hua Lee, John L. Miamidian, Cassandra B. Jabara, Marisa M. Juntilla, and Robert W. Doms. Enfuvirtide Resistance Mutations: Impact on Human Immunodeficiency Virus Envelope Function, Entry Inhibitor Sensitivity, and Virus Neutralization. J. Virol., 79(8):4991-4999, Apr 2005. PubMed ID: 15795284. Show all entries for this paper.

Richard2014 Jonathan Richard, Maxime Veillette, Laurie-Anne Batraville, Mathieu Coutu, Jean-Philippe Chapleau, Mattia Bonsignori, Nicole Bernard, Cécile Tremblay, Michel Roger, Daniel E. Kaufmann, and Andrés Finzi. Flow Cytometry-Based Assay to Study HIV-1 gp120 Specific Antibody-Dependent Cellular Cytotoxicity Responses. J. Virol. Methods, 208:107-.14, Nov 2014. PubMed ID: 25125129. Show all entries for this paper.

Richman2003 Douglas D. Richman, Terri Wrin, Susan J. Little, and Christos J. Petropoulos. Rapid Evolution of the Neutralizing Antibody Response to HIV Type 1 Infection. Proc. Natl. Acad. Sci. U.S.A., 100(7):4144-4149, 1 Apr 2003. PubMed ID: 12644702. Show all entries for this paper.

Ringe2010 Rajesh Ringe, Madhuri Thakar, and Jayanta Bhattacharya. Variations in Autologous Neutralization and CD4 Dependence of b12 Resistant HIV-1 Clade C env Clones Obtained at Different Time Points from Antiretroviral Naïve Indian Patients with Recent Infection. Retrovirology, 7:76, 2010. PubMed ID: 20860805. Show all entries for this paper.

Rits-Volloch2006 Sophia Rits-Volloch, Gary Frey, Stephen C. Harrison, and Bing Chen. Restraining the Conformation of HIV-1 gp120 by Removing a Flexible Loop. EMBO J., 25(20):5026-5035, 18 Oct 2006. PubMed ID: 17006538. Show all entries for this paper.

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Ruprecht2011 Claudia R. Ruprecht, Anders Krarup, Lucy Reynell, Axel M. Mann, Oliver F. Brandenberg, Livia Berlinger, Irene A. Abela, Roland R. Regoes, Huldrych F. Günthard, Peter Rusert, and Alexandra Trkola. MPER-Specific Antibodies Induce gp120 Shedding and Irreversibly Neutralize HIV-1. J. Exp. Med., 208(3):439-454, 14 Mar 2011. PubMed ID: 21357743. Show all entries for this paper.

Rusert2005 Peter Rusert, Herbert Kuster, Beda Joos, Benjamin Misselwitz, Cornelia Gujer, Christine Leemann, Marek Fischer, Gabriela Stiegler, Hermann Katinger, William C Olson, Rainer Weber, Leonardo Aceto, Huldrych F Günthard, and Alexandra Trkola. Virus Isolates during Acute and Chronic Human Immunodeficiency Virus Type 1 Infection Show Distinct Patterns of Sensitivity to Entry Inhibitors. J. Virol., 79(13):8454-8469, Jul 2005. PubMed ID: 15956589. Show all entries for this paper.

Rusert2009 Peter Rusert, Axel Mann, Michael Huber, Viktor von Wyl, Huldrych F. Günthar, and Alexandra Trkola. Divergent Effects of Cell Environment on HIV Entry Inhibitor Activity. AIDS, 23(11):1319-1327, 17 Jul 2009. PubMed ID: 19579289. Show all entries for this paper.

Russell2011 Elizabeth S. Russell, Jesse J. Kwiek, Jessica Keys, Kirston Barton, Victor Mwapasa, David C. Montefiori, Steven R. Meshnick, and Ronald Swanstrom. The Genetic Bottleneck in Vertical Transmission of Subtype C HIV-1 Is Not Driven by Selection of Especially Neutralization-Resistant Virus from the Maternal Viral Population. J Virol, 85(16):8253-8262, Aug 2011. PubMed ID: 21593171. Show all entries for this paper.

Sabin2010 Charles Sabin, Davide Corti, Victor Buzon, Mike S. Seaman, David Lutje Hulsik, Andreas Hinz, Fabrizia Vanzetta, Gloria Agatic, Chiara Silacci, Lara Mainetti, Gabriella Scarlatti, Federica Sallusto, Robin Weiss, Antonio Lanzavecchia, and Winfried Weissenhorn. Crystal Structure and Size-Dependent Neutralization Properties of HK20, a Human Monoclonal Antibody Binding to the Highly Conserved Heptad Repeat 1 of gp41. PLoS Pathog., 6(11):e1001195, 2010. PubMed ID: 21124990. Show all entries for this paper.

Safrit2004 Jeffrey T. Safrit, Ruth Ruprecht, Flavia Ferrantelli, Weidong Xu, Moiz Kitabwalla, Koen Van Rompay, Marta Marthas, Nancy Haigwood, John R. Mascola, Katherine Luzuriaga, Samuel Adeniyi Jones, Bonnie J. Mathieson, Marie-Louise Newell, and Ghent IAS Working Group on HIV in Women Children. Immunoprophylaxis to Prevent Mother-to-Child Transmission of HIV-1. J. Acquir. Immune Defic. Syndr., 35(2):169-177, 1 Feb 2004. PubMed ID: 14722451. Show all entries for this paper.

Sagar2012 Manish Sagar, Hisashi Akiyama, Behzad Etemad, Nora Ramirez, Ines Freitas, and Suryaram Gummuluru. Transmembrane Domain Membrane Proximal External Region but Not Surface Unit-Directed Broadly Neutralizing HIV-1 Antibodies Can Restrict Dendritic Cell-Mediated HIV-1 Trans-Infection. J. Infect. Dis., 205(8):1248-1257, 15 Apr 2012. PubMed ID: 22396600. Show all entries for this paper.

Sainsbury2010 Frank Sainsbury, Markus Sack, Johannes Stadlmann, Heribert Quendler, Rainer Fischer, and George P. Lomonossoff. Rapid Transient Production in Plants by Replicating and Non-Replicating Vectors Yields High Quality Functional Anti-HIV Antibody. PLoS One, 5(11):e13976, 2010. PubMed ID: 21103044. Show all entries for this paper.

Sajadi2012 Mohammad M. Sajadi, George K. Lewis, Michael S. Seaman, Yongjun Guan, Robert R. Redfield, and Anthony L. DeVico. Signature Biochemical Properties of Broadly Cross-Reactive HIV-1 Neutralizing Antibodies in Human Plasma. J. Virol., 86(9):5014-5025, May 2012. PubMed ID: 22379105. Show all entries for this paper.

Sanchez-Merino2016 V. Sanchez-Merino, A. Fabra-Garcia, N. Gonzalez, D. Nicolas, A. Merino-Mansilla, C. Manzardo, J. Ambrosioni, A. Schultz, A. Meyerhans, J. R. Mascola, J. M. Gatell, J. Alcami, J. M. Miro, and E. Yuste. Detection of Broadly Neutralizing Activity within the First Months of HIV-1 Infection. J. Virol., 90(11):5231-5245, 1 Jun 2016. PubMed ID: 26984721. Show all entries for this paper.

Sanders2002 Rogier W. Sanders, Miro Venturi, Linnea Schiffner, Roopa Kalyanaraman, Hermann Katinger, Kenneth O. Lloyd, Peter D. Kwong, and John P. Moore. The Mannose-Dependent Epitope for Neutralizing Antibody 2G12 on Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Virol., 76(14):7293-7305, Jul 2002. PubMed ID: 12072528. Show all entries for this paper.

Sanders2013 Rogier W. Sanders, Ronald Derking, Albert Cupo, Jean-Philippe Julien, Anila Yasmeen, Natalia de Val, Helen J. Kim, Claudia Blattner, Alba Torrents de la Peña, Jacob Korzun, Michael Golabek, Kevin de los Reyes, Thomas J. Ketas, Marit J. van Gils, C. Richter King, Ian A. Wilson, Andrew B. Ward, P. J. Klasse, and John P. Moore. A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but not Non-Neutralizing Antibodies. PLoS Pathog., 9(9):e1003618, Sep 2013. PubMed ID: 24068931. Show all entries for this paper.

Sanders2015 Rogier W. Sanders, Marit J. van Gils, Ronald Derking, Devin Sok, Thomas J. Ketas, Judith A. Burger, Gabriel Ozorowski, Albert Cupo, Cassandra Simonich, Leslie Goo, Heather Arendt, Helen J. Kim, Jeong Hyun Lee, Pavel Pugach, Melissa Williams, Gargi Debnath, Brian Moldt, Mariëlle J. van Breemen, Gözde Isik, Max Medina-Ramírez, Jaap Willem Back, Wayne C. Koff, Jean-Philippe Julien, Eva G. Rakasz, Michael S. Seaman, Miklos Guttman, Kelly K. Lee, Per Johan Klasse, Celia LaBranche, William R. Schief, Ian A. Wilson, Julie Overbaugh, Dennis R. Burton, Andrew B. Ward, David C. Montefiori, Hansi Dean, and John P. Moore. HIV-1 Neutralizing Antibodies Induced by Native-Like Envelope Trimers. Science, 349(6244):aac4223, 10 Jul 2015. PubMed ID: 26089353. Show all entries for this paper.

Sather2014 D. Noah Sather, Sara Carbonetti, Delphine C. Malherbe, Franco Pissani, Andrew B. Stuart, Ann J. Hessell, Mathew D. Gray, Iliyana Mikell, Spyros A. Kalams, Nancy L. Haigwood, and Leonidas Stamatatos. Emergence of Broadly Neutralizing Antibodies and Viral Coevolution in Two Subjects during the Early Stages of Infection with Human Immunodeficiency Virus Type 1. J. Virol., 88(22):12968-12981, Nov 2014. PubMed ID: 25122781. Show all entries for this paper.

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Sattentau2010 Quentin J. Sattentau and Andrew J. McMichael. New Templates for HIV-1 Antibody-Based Vaccine Design. F1000 Biol. Rep., 2:60, 2010. PubMed ID: 21173880. Show all entries for this paper.

Saunders2017 Kevin O. Saunders, Nathan I. Nicely, Kevin Wiehe, Mattia Bonsignori, R. Ryan Meyerhoff, Robert Parks, William E. Walkowicz, Baptiste Aussedat, Nelson R. Wu, Fangping Cai, Yusuf Vohra, Peter K. Park, Amanda Eaton, Eden P. Go, Laura L. Sutherland, Richard M. Scearce, Dan H. Barouch, Ruijun Zhang, Tarra Von Holle, R. Glenn Overman, Kara Anasti, Rogier W. Sanders, M. Anthony Moody, Thomas B. Kepler, Bette Korber, Heather Desaire, Sampa Santra, Norman L. Letvin, Gary J. Nabel, David C. Montefiori, Georgia D. Tomaras, Hua-Xin Liao, S. Munir Alam, Samuel J. Danishefsky, and Barton F. Haynes. Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman Primates. Cell Rep., 18(9):2175-2188, 28 Feb 2017. PubMed ID: 28249163. Show all entries for this paper.

Savarino2001 A. Savarino, L. Gennero, H. C. Chen, D. Serrano, F. Malavasi, J. R. Boelaert, and K. Sperber. Anti-HIV effects of chloroquine: mechanisms of inhibition and spectrum of activity. AIDS, 15(17):2221--9, 23 Nov 2001. PubMed ID: 11698694. Show all entries for this paper.

Scanlan2002 Christopher N. Scanlan, Ralph Pantophlet, Mark R. Wormald, Erica Ollmann Saphire, Robyn Stanfield, Ian A. Wilson, Hermann Katinger, Raymond A. Dwek, Pauline M. Rudd, and Dennis R. Burton. The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2G12 Recognizes a Cluster of Alpha1→2 Mannose Residues on the Outer Face of gp120. J. Virol., 76(14):7306-7321, Jul 2002. PubMed ID: 12072529. Show all entries for this paper.

Scanlan2007 Christopher N. Scanlan, Gayle E. Ritchie, Kavitha Baruah, Max Crispin, David J. Harvey, Bernhard B. Singer, Lothar Lucka, Mark R. Wormald, Paul Wentworth, Jr., Nicole Zitzmann, Pauline M. Rudd, Dennis R Burton, and Raymond A. Dwek. Inhibition of Mammalian Glycan Biosynthesis Produces Non-Self Antigens for a Broadly Neutralising, HIV-1 Specific Antibody. J. Mol. Biol., 372(1):16-22, 7 Sep 2007. PubMed ID: 17631311. Show all entries for this paper.

Scheid2009 Johannes F. Scheid, Hugo Mouquet, Niklas Feldhahn, Michael S. Seaman, Klara Velinzon, John Pietzsch, Rene G. Ott, Robert M. Anthony, Henry Zebroski, Arlene Hurley, Adhuna Phogat, Bimal Chakrabarti, Yuxing Li, Mark Connors, Florencia Pereyra, Bruce D. Walker, Hedda Wardemann, David Ho, Richard T. Wyatt, John R. Mascola, Jeffrey V. Ravetch, and Michel C. Nussenzweig. Broad Diversity of Neutralizing Antibodies Isolated from Memory B Cells in HIV-Infected Individuals. Nature, 458(7238):636-640, 2 Apr 2009. PubMed ID: 19287373. Show all entries for this paper.

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Schiffner2016 Torben Schiffner, Natalia de Val, Rebecca A. Russell, Steven W. de Taeye, Alba Torrents de la Peña, Gabriel Ozorowski, Helen J. Kim, Travis Nieusma, Florian Brod, Albert Cupo, Rogier W. Sanders, John P. Moore, Andrew B. Ward, and Quentin J. Sattentau. Chemical Cross-Linking Stabilizes Native-Like HIV-1 Envelope Glycoprotein Trimer Antigens. J. Virol., 90(2):813-828, 28 Oct 2015. PubMed ID: 26512083. Show all entries for this paper.

Schiffner2018 Torben Schiffner, Jesper Pallesen, Rebecca A. Russell, Jonathan Dodd, Natalia de Val, Celia C. LaBranche, David Montefiori, Georgia D. Tomaras, Xiaoying Shen, Scarlett L. Harris, Amin E. Moghaddam, Oleksandr Kalyuzhniy, Rogier W. Sanders, Laura E. McCoy, John P. Moore, Andrew B. Ward, and Quentin J. Sattentau. Structural and Immunologic Correlates of Chemically Stabilized HIV-1 Envelope Glycoproteins. PLoS Pathog., 14(5):e1006986, May 2018. PubMed ID: 29746590. Show all entries for this paper.

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Schweighardt2007 Becky Schweighardt, Yang Liu, Wei Huang, Colombe Chappey, Yolanda S. Lie, Christos J. Petropoulos, and Terri Wrin. Development of an HIV-1 Reference Panel of Subtype B Envelope Clones Isolated from the Plasma of Recently Infected Individuals. J. Acquir. Immune Defic. Syndr., 46(1):1-11, 1 Sep 2007. PubMed ID: 17514017. Show all entries for this paper.

Sellhorn2012 George Sellhorn, Zane Kraft, Zachary Caldwell, Katharine Ellingson, Christine Mineart, Michael S. Seaman, David C. Montefiori, Eliza Lagerquist, and Leonidas Stamatatos. Engineering, Expression, Purification, and Characterization of Stable Clade A/B Recombinant Soluble Heterotrimeric gp140 Proteins. J. Virol., 86(1):128-142, Jan 2012. PubMed ID: 22031951. Show all entries for this paper.

Selvarajah2005 Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142. Show all entries for this paper.

Shan2007 Meimei Shan, Per Johan Klasse, Kaustuv Banerjee, Antu K Dey, Sai Prasad N. Iyer, Robert Dionisio, Dustin Charles, Lila Campbell-Gardener, William C. Olson, Rogier W. Sanders, and John P. Moore. HIV-1 gp120 Mannoses Induce Immunosuppressive Responses from Dendritic Cells. PLoS Pathog., 3(11):e169, Nov 2007. PubMed ID: 17983270. Show all entries for this paper.

Shang2011 Hong Shang, Xiaoxu Han, Xuanling Shi, Teng Zuo, Mark Goldin, Dan Chen, Bing Han, Wei Sun, Hao Wu, Xinquan Wang, and Linqi Zhang. Genetic and Neutralization Sensitivity of Diverse HIV-1 env Clones from Chronically Infected Patients in China. J. Biol. Chem., 286(16):14531-14541, 22 Apr 2011. PubMed ID: 21325278. Show all entries for this paper.

Shen2010 Xiaoying Shen, S. Moses Dennison, Pinghuang Liu, Feng Gao, Frederick Jaeger, David C. Montefiori, Laurent Verkoczy, Barton F. Haynes, S. Munir Alam, and Georgia D. Tomaras. Prolonged Exposure of the HIV-1 gp41 Membrane Proximal Region with L669S Substitution. Proc. Natl. Acad. Sci. U.S.A., 107(13):5972-5977, 30 Mar 2010. PubMed ID: 20231447. Show all entries for this paper.

Sheppard2007a Neil C. Sheppard, Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins. Clin. Vaccine Immunol., 14(2):157-167, Feb 2007. PubMed ID: 17167037. Show all entries for this paper.

Si2001 Zhihai Si, Mark Cayabyab, and Joseph Sodroski. Envelope Glycoprotein Determinants of nEutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys. J. Virol., 75(9):4208-4218, May 2001. PubMed ID: 11287570. Show all entries for this paper.

Siddappa2010 Nagadenahalli B. Siddappa, Jennifer D. Watkins, Klemens J. Wassermann, Ruijiang Song, Wendy Wang, Victor G. Kramer, Samir Lakhashe, Michael Santosuosso, Mark C. Poznansky, Francis J. Novembre, François Villinger, James G. Else, David C. Montefiori, Robert A. Rasmussen, and Ruth M. Ruprecht. R5 Clade C SHIV Strains with Tier 1 or 2 Neutralization Sensitivity: Tools to Dissect Env Evolution and to Develop AIDS Vaccines in Primate Models. PLoS One, 5(7):e11689, 2010. PubMed ID: 20657739. Show all entries for this paper.

Simek2009 Melissa D. Simek, Wasima Rida, Frances H. Priddy, Pham Pung, Emily Carrow, Dagna S. Laufer, Jennifer K. Lehrman, Mark Boaz, Tony Tarragona-Fiol, George Miiro, Josephine Birungi, Anton Pozniak, Dale A. McPhee, Olivier Manigart, Etienne Karita, André Inwoley, Walter Jaoko, Jack DeHovitz, Linda-Gail Bekker, Punnee Pitisuttithum, Robert Paris, Laura M. Walker, Pascal Poignard, Terri Wrin, Patricia E. Fast, Dennis R. Burton, and Wayne C. Koff. Human Immunodeficiency Virus Type 1 Elite Neutralizers: Individuals with Broad and Potent Neutralizing Activity Identified by Using a High-Throughput Neutralization Assay together with an Analytical Selection Algorithm. J. Virol., 83(14):7337-7348, Jul 2009. PubMed ID: 19439467. Show all entries for this paper.

Simonich2016 Cassandra A. Simonich, Katherine L. Williams, Hans P. Verkerke, James A. Williams, Ruth Nduati, Kelly K. Lee, and Julie Overbaugh. HIV-1 Neutralizing Antibodies with Limited Hypermutation from an Infant. Cell, 166(1):77-87, 30 Jun 2016. PubMed ID: 27345369. Show all entries for this paper.

Singh2003 Suddham Singh, Jiahong Ni, and Lai-Xi Wang. Chemoenzymatic Synthesis of High-Mannose Type HIV-1 gp120 Glycopeptides. Bioorg. Med. Chem. Lett., 13(3):327-330, 10 Feb 2003. PubMed ID: 12565922. Show all entries for this paper.

Singh2011 Harvir Singh, Kevin A. Henry, Sampson S. T. Wu, Andrzej Chruscinski, Paul J. Utz, and Jamie K. Scott. Reactivity Profiles of Broadly Neutralizing Anti-HIV-1 Antibodies Are Distinct from Those of Pathogenic Autoantibodies. AIDS, 25(10):1247-1257, 19 Jun 2011. PubMed ID: 21508803. Show all entries for this paper.

Sirois2007 Suzanne Sirois, Mohamed Touaibia, Kuo-Chen Chou, and Rene Roy. Glycosylation of HIV-1 gp120 V3 Loop: Towards the Rational Design of a Synthetic Carbohydrate Vaccine. Curr. Med. Chem., 14(30):3232-3242, 2007. PubMed ID: 18220757. Show all entries for this paper.

Smalls-Mantey2012 Adjoa Smalls-Mantey, Nicole Doria-Rose, Rachel Klein, Andy Patamawenu, Stephen A. Migueles, Sung-Youl Ko, Claire W. Hallahan, Hing Wong, Bai Liu, Lijing You, Johannes Scheid, John C. Kappes, Christina Ochsenbauer, Gary J. Nabel, John R. Mascola, and Mark Connors. Antibody-Dependent Cellular Cytotoxicity against Primary HIV-Infected CD4+ T Cells Is Directly Associated with the Magnitude of Surface IgG Binding. J. Virol., 86(16):8672-8680, Aug 2012. PubMed ID: 22674985. Show all entries for this paper.

Sok2014a Devin Sok, Katie J. Doores, Bryan Briney, Khoa M. Le, Karen L. Saye-Francisco, Alejandra Ramos, Daniel W. Kulp, Jean-Philippe Julien, Sergey Menis, Lalinda Wickramasinghe, Michael S. Seaman, William R. Schief, Ian A. Wilson, Pascal Poignard, and Dennis R. Burton. Promiscuous Glycan Site Recognition by Antibodies to the High-Mannose Patch of gp120 Broadens Neutralization of HIV. Sci. Transl. Med., 6(236):236ra63, 14 May 2014. PubMed ID: 24828077. Show all entries for this paper.

Sok2016 Devin Sok, Matthias Pauthner, Bryan Briney, Jeong Hyun Lee, Karen L. Saye-Francisco, Jessica Hsueh, Alejandra Ramos, Khoa M. Le, Meaghan Jones, Joseph G. Jardine, Raiza Bastidas, Anita Sarkar, Chi-Hui Liang, Sachin S. Shivatare, Chung-Yi Wu, William R. Schief, Chi-Huey Wong, Ian A. Wilson, Andrew B. Ward, Jiang Zhu, Pascal Poignard, and Dennis R. Burton. A Prominent Site of Antibody Vulnerability on HIV Envelope Incorporates a Motif Associated with CCR5 Binding and Its Camouflaging Glycans. Immunity, 45(1):31-45, 19 Jul 2016. PubMed ID: 27438765. Show all entries for this paper.

Spenlehauer2001 C. Spenlehauer, C. A. Gordon, A. Trkola, and J. P. Moore. A luciferase-reporter gene-expressing T-cell line facilitates neutralization and drug-sensitivity assays that use either R5 or X4 strains of human immunodeficiency virus type 1. Virology, 280(2):292--300, 15 Feb 2001. PubMed ID: 11162843. Show all entries for this paper.

Srivastava2005 Indresh K. Srivastava, Jeffrey B. Ulmer, and Susan W. Barnett. Role of Neutralizing Antibodies in Protective Immunity Against HIV. Hum. Vaccin., 1(2):45-60, Mar-Apr 2005. PubMed ID: 17038830. Show all entries for this paper.

Stamatatos2009 Leonidas Stamatatos, Lynn Morris, Dennis R. Burton, and John R. Mascola. Neutralizing Antibodies Generated during Natural HIV-1 Infection: Good News for an HIV-1 Vaccine? Nat. Med., 15(8):866-870, Aug 2009. PubMed ID: 19525964. Show all entries for this paper.

Stephenson2016 Kathryn E. Stephenson and Dan H. Barouch. Broadly Neutralizing Antibodies for HIV Eradication. Curr. HIV/AIDS Rep., 13(1):31-37, Feb 2016. PubMed ID: 26841901. Show all entries for this paper.

Stewart-Jones2016 Guillaume B. E. Stewart-Jones, Cinque Soto, Thomas Lemmin, Gwo-Yu Chuang, Aliaksandr Druz, Rui Kong, Paul V. Thomas, Kshitij Wagh, Tongqing Zhou, Anna-Janina Behrens, Tatsiana Bylund, Chang W. Choi, Jack R. Davison, Ivelin S. Georgiev, M. Gordon Joyce, Young Do Kwon, Marie Pancera, Justin Taft, Yongping Yang, Baoshan Zhang, Sachin S. Shivatare, Vidya S. Shivatare, Chang-Chun D. Lee, Chung-Yi Wu, Carole A. Bewley, Dennis R. Burton, Wayne C. Koff, Mark Connors, Max Crispin, Ulrich Baxa, Bette T. Korber, Chi-Huey Wong, John R. Mascola, and Peter D. Kwong. Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B, and G. Cell, 165(4):813-826, 5 May 2016. PubMed ID: 27114034. Show all entries for this paper.

Stiegler2001 G. Stiegler, R. Kunert, M. Purtscher, S. Wolbank, R. Voglauer, F. Steindl, and H. Katinger. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 17(18):1757--65, 10 Dec 2001. PubMed ID: 11788027. Show all entries for this paper.

Stiegler2002 Gabriela Stiegler, Christine Armbruster, Brigitta Vcelar, Heribert Stoiber, Renate Kunert, Nelson L. Michael, Linda L. Jagodzinski, Christoph Ammann, Walter Jäger, Jeffrey Jacobson, Norbert Vetter, and Hermann Katinger. Antiviral Activity of the Neutralizing Antibodies 2F5 and 2G12 in Asymptomatic HIV-1-Infected Humans: A Phase I Evaluation. AIDS, 16(15):2019-2025, 18 Oct 2002. PubMed ID: 12370500. Show all entries for this paper.

Strasser2009 Richard Strasser, Alexandra Castilho, Johannes Stadlmann, Renate Kunert, Heribert Quendler, Pia Gattinger, Jakub Jez, Thomas Rademacher, Friedrich Altmann, Lukas Mach, and Herta Steinkellner. Improved Virus Neutralization by Plant-Produced Anti-HIV Antibodies with a Homogeneous beta1,4-Galactosylated N-Glycan Profile. J. Biol. Chem., 284(31):20479-20485, 31 Jul 2009. PubMed ID: 19478090. Show all entries for this paper.

Sullivan1998 N. Sullivan, Y. Sun, Q. Sattentau, M. Thali, D. Wu, G. Denisova, J. Gershoni, J. Robinson, J. Moore, and J. Sodroski. CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization. J. Virol., 72:4694-4703, 1998. A study of the sCD4 inducible MAb 17bi, and the MAb CG10 that recognizes a gp120-CD4 complex. These epitopes are minimally accessible upon attachment of gp120 to the cell. The CD4-binding induced changes in gp120 were studied, exploring the sequestering of chemokine receptor binding sites from the humoral response. PubMed ID: 9573233. Show all entries for this paper.

Sundling2012 Christopher Sundling, Yuxing Li, Nick Huynh, Christian Poulsen, Richard Wilson, Sijy O'Dell, Yu Feng, John R. Mascola, Richard T. Wyatt, and Gunilla B. Karlsson Hedestam. High-Resolution Definition of Vaccine-Elicited B Cell Responses Against the HIV Primary Receptor Binding Site. Sci. Transl. Med., 4(142):142ra96, 11 Jul 2012. PubMed ID: 22786681. Show all entries for this paper.

Swanson2010 Michael D. Swanson, Harry C. Winter, Irwin J. Goldstein, and David M. Markovitz. A Lectin Isolated from Bananas Is a Potent Inhibitor of HIV Replication. J. Biol. Chem., 285(12):8646-55, 19 Mar 2010. PubMed ID: 20080975. Show all entries for this paper.

Takefman1998 D. M. Takefman, B. L. Sullivan, B. E. Sha, and G. T. Spear. Mechanisms of Resistance of HIV-1 Primary Isolates to Complement-Mediated Lysis. Virology, 246:370-378, 1998. PubMed ID: 9657955. Show all entries for this paper.

Tasca2008 Silvana Tasca, Siu-Hong Ho, and Cecilia Cheng-Mayer. R5X4 Viruses Are Evolutionary, Functional, and Antigenic Intermediates in the Pathway of a Simian-Human Immunodeficiency Virus Coreceptor Switch. J. Virol., 82(14):7089-7099, Jul 2008. PubMed ID: 18480460. Show all entries for this paper.

Taylor2008 Brian M. Taylor, J. Scott Foulke, Robin Flinko, Alonso Heredia, Anthony DeVico, and Marvin Reitz. An Alteration of Human Immunodeficiency Virus gp41 Leads to Reduced CCR5 Dependence and CD4 Independence. J. Virol., 82(11):5460-5471, Jun 2008. PubMed ID: 18353949. Show all entries for this paper.

Thenin2012a Suzie Thenin, Emmanuelle Roch, Tanawan Samleerat, Thierry Moreau, Antoine Chaillon, Alain Moreau, Francis Barin, and Martine Braibant. Naturally Occurring Substitutions of Conserved Residues in Human Immunodeficiency Virus Type 1 Variants of Different Clades Are Involved in PG9 and PG16 Resistance to Neutralization. J. Gen. Virol., 93(7):1495-1505, Jul 2012. PubMed ID: 22492917. Show all entries for this paper.

Thida2019 Win Thida, Takeo Kuwata, Yosuke Maeda, Tetsu Yamashiro, Giang Van Tran, Kinh Van Nguyen, Masafumi Takiguchi, Hiroyuki Gatanaga, Kazuki Tanaka, and Shuzo Matsushita. The role of conventional antibodies targeting the CD4 binding site and CD4-induced epitopes in the control of HIV-1 CRF01_AE viruses. Biochem Biophys Res Commun, 508(1):46-51 doi, Jan 2019. PubMed ID: 30470571 Show all entries for this paper.

Todd2012 Christopher A. Todd, Kelli M. Greene, Xuesong Yu, Daniel A. Ozaki, Hongmei Gao, Yunda Huang, Maggie Wang, Gary Li, Ronald Brown, Blake Wood, M. Patricia D'Souza, Peter Gilbert, David C. Montefiori, and Marcella Sarzotti-Kelsoe. Development and Implementation of an International Proficiency Testing Program for a Neutralizing Antibody Assay for HIV-1 in TZM-bl Cells. J. Immunol. Methods, 375(1-2):57-67, 31 Jan 2012. PubMed ID: 21968254. Show all entries for this paper.

Tokarev2015 Andrey Tokarev, Charlotte Stoneham, Mary K. Lewinski, Amey Mukim, Savitha Deshmukh, Thomas Vollbrecht, Celsa A. Spina, and John Guatelli. Pharmacologic Inhibition of Nedd8 Activation Enzyme Exposes CD4-Induced Epitopes within Env on Cells Expressing HIV-1. J. Virol., 90(5):2486-2502, 16 Dec 2015. PubMed ID: 26676780. Show all entries for this paper.

Tomaras2008 Georgia D. Tomaras, Nicole L. Yates, Pinghuang Liu, Li Qin, Genevieve G. Fouda, Leslie L. Chavez, Allan C. Decamp, Robert J. Parks, Vicki C. Ashley, Judith T. Lucas, Myron Cohen, Joseph Eron, Charles B. Hicks, Hua-Xin Liao, Steven G. Self, Gary Landucci, Donald N. Forthal, Kent J. Weinhold, Brandon F. Keele, Beatrice H. Hahn, Michael L. Greenberg, Lynn Morris, Salim S. Abdool Karim, William A. Blattner, David C. Montefiori, George M. Shaw, Alan S. Perelson, and Barton F. Haynes. Initial B-Cell Responses to Transmitted Human Immunodeficiency Virus Type 1: Virion-Binding Immunoglobulin M (IgM) and IgG Antibodies Followed by Plasma Anti-gp41 Antibodies with Ineffective Control of Initial Viremia. J. Virol., 82(24):12449-12463, Dec 2008. PubMed ID: 18842730. Show all entries for this paper.

Tomaras2011 Georgia D. Tomaras, James M. Binley, Elin S. Gray, Emma T. Crooks, Keiko Osawa, Penny L. Moore, Nancy Tumba, Tommy Tong, Xiaoying Shen, Nicole L. Yates, Julie Decker, Constantinos Kurt Wibmer, Feng Gao, S. Munir Alam, Philippa Easterbrook, Salim Abdool Karim, Gift Kamanga, John A. Crump, Myron Cohen, George M. Shaw, John R. Mascola, Barton F. Haynes, David C. Montefiori, and Lynn Morris. Polyclonal B Cell Responses to Conserved Neutralization Epitopes in a Subset of HIV-1-Infected Individuals. J. Virol., 85(21):11502-11519, Nov 2011. PubMed ID: 21849452. Show all entries for this paper.

Tong2012 Tommy Tong, Ema T. Crooks, Keiko Osawa, and James M. Binley. HIV-1 Virus-Like Particles Bearing Pure Env Trimers Expose Neutralizing Epitopes but Occlude Nonneutralizing Epitopes. J. Virol., 86(7):3574-3587, Apr 2012. PubMed ID: 22301141. Show all entries for this paper.

Trkola1995a A. Trkola, A. B. Pomales, H. Yuan, B. Korber, P. J. Maddon, G. P. Allaway, H. Katinger, C. F. Barbas III, D. R. Burton, D. D. Ho, and J. P. Moore. Cross-Clade Neutralization of Primary Isolates of Human Immunodeficiency Virus Type 1 by Human Monoclonal Antibodies and Tetrameric CD4-IgG. J. Virol., 69:6609-6617, 1995. Three MAbs, IgG1b12, 2G12, and 2F5 tetrameric CD4-IgG2 were tested for their ability to neutralize primary isolates from clades A-F. 2F5 and CD4-IgG2 were able to neutralize within and outside clade B with a high potency. IgG1b12 and 2G12 could potently neutralize isolates from within clade B, but showed a reduction in efficacy outside of clade B. 2F5 neutralization was dependent on the presence of the sequence: LDKW. PubMed ID: 7474069. Show all entries for this paper.

Trkola1996 A. Trkola, M. Purtscher, T. Muster, C. Ballaun, A. Buchacher, N. Sullivan, K. Srinivasan, J. Sodroski, J. P. Moore, and H. Katinger. Human Monoclonal Antibody 2G12 Defines a Distinctive Neutralization Epitope on the gp120 Glycoprotein of Human Immunodeficiency Virus Type 1. J. Virol., 70:1100-1108, 1996. PubMed ID: 8551569. Show all entries for this paper.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Trkola1998 A. Trkola, T. Ketas, V. N. Kewalramani, F. Endorf, J. M. Binley, H. Katinger, J. Robinson, D. R. Littman, and J. P. Moore. Neutralization Sensitivity of Human Immunodeficiency Virus Type 1 Primary Isolates to Antibodies and CD4-Based Reagents Is Independent of Coreceptor Usage. J. Virol., 72:1876-1885, 1998. PubMed ID: 9499039. Show all entries for this paper.

Trkola2005 Alexandra Trkola, Herbert Kuster, Peter Rusert, Beda Joos, Marek Fischer, Christine Leemann, Amapola Manrique, Michael Huber, Manuela Rehr, Annette Oxenius, Rainer Weber, Gabriela Stiegler, Brigitta Vcelar, Hermann Katinger, Leonardo Aceto, and Huldrych F. Günthard. Delay of HIV-1 Rebound after Cessation of Antiretroviral Therapy through Passive Transfer of Human Neutralizing Antibodies. Nat. Med., 11(6):615-622, Jun 2005. PubMed ID: 15880120. Show all entries for this paper.

Ueno-Noto2016 Kaori Ueno-Noto and Keiko Takano. Water Molecules inside Protein Structure affect Binding of Monosaccharides with HIV-1 Antibody 2G12. J. Comput. Chem., 37(26):2341-2348, 5 Oct 2016. PubMed ID: 27388036. Show all entries for this paper.

Ugolini1997 S. Ugolini, I. Mondor, P. W. H. I Parren, D. R. Burton, S. A. Tilley, P. J. Klasse, and Q. J. Sattentau. Inhibition of Virus Attachment to CD4+ Target Cells Is a Major Mechanism of T Cell Line-Adapted HIV-1 Neutralization. J. Exp. Med., 186:1287-1298, 1997. PubMed ID: 9334368. Show all entries for this paper.

Upadhyay2014 Chitra Upadhyay, Luzia M. Mayr, Jing Zhang, Rajnish Kumar, Miroslaw K. Gorny, Arthur Nádas, Susan Zolla-Pazner, and Catarina E. Hioe. Distinct Mechanisms Regulate Exposure of Neutralizing Epitopes in the V2 and V3 Loops of HIV-1 Envelope. J. Virol., 88(21):12853-12865, Nov 2014. PubMed ID: 25165106. Show all entries for this paper.

Utachee2009 Piraporn Utachee, Piyamat Jinnopat, Panasda Isarangkura-na-ayuthaya, U. Chandimal de Silva, Shota Nakamura, Uamporn Siripanyaphinyo, Nuanjun Wichukchinda, Kenzo Tokunaga, Teruo Yasunaga, Pathom Sawanpanyalert, Kazuyoshi Ikuta, Wattana Auwanit, and Masanori Kameoka. Phenotypic Studies on Recombinant Human Immunodeficiency Virus Type 1 (HIV-1) Containing CRF01\_AE env Gene Derived from HIV-1-Infected Patient, Residing in Central Thailand. Microbes Infect., 11(3):334-343, Mar 2009. PubMed ID: 19136072. Show all entries for this paper.

Vaine2008 Michael Vaine, Shixia Wang, Emma T. Crooks, Pengfei Jiang, David C. Montefiori, James Binley, and Shan Lu. Improved Induction of Antibodies against Key Neutralizing Epitopes by Human Immunodeficiency Virus Type 1 gp120 DNA Prime-Protein Boost Vaccination Compared to gp120 Protein-Only Vaccination. J. Virol., 82(15):7369-7378, Aug 2008. PubMed ID: 18495775. Show all entries for this paper.

Vaine2010 Michael Vaine, Shixia Wang, Qin Liu, James Arthos, David Montefiori, Paul Goepfert, M. Juliana McElrath, and Shan Lu. Profiles of Human Serum Antibody Responses Elicited by Three Leading HIV Vaccines Focusing on the Induction of Env-Specific Antibodies. PLoS One, 5(11):e13916, 2010. PubMed ID: 21085486. Show all entries for this paper.

Vaine2011 Michael Vaine, Maria Duenas-Decamp, Paul Peters, Qin Liu, James Arthos, Shixia Wang, Paul Clapham, and Shan Lu. Two Closely Related Env Antigens from the Same Patient Elicited Different Spectra of Neutralizing Antibodies against Heterologous HIV-1 Isolates. J. Virol., 85(10):4927-4936, May 2011. PubMed ID: 21411542. Show all entries for this paper.

Vamvaka2016 Evangelia Vamvaka, Richard M. Twyman, Andre Melro Murad, Stanislav Melnik, Audrey Yi-Hui Teh, Elsa Arcalis, Friedrich Altmann, Eva Stoger, Elibio Rech, Julian K. C. Ma, Paul Christou, and Teresa Capell. Rice Endosperm Produces an Underglycosylated and Potent Form of the HIV-Neutralizing Monoclonal Antibody 2G12. Plant Biotechnol. J., 14(1):97-108, Jan 2016. PubMed ID: 25845722. Show all entries for this paper.

vanGils2011 Marit J. van Gils, Evelien M. Bunnik, Brigitte D. Boeser-Nunnink, Judith A. Burger, Marijke Terlouw-Klein, Naomi Verwer, and Hanneke Schuitemaker. Longer V1V2 Region with Increased Number of Potential N-Linked Glycosylation Sites in the HIV-1 Envelope Glycoprotein Protects against HIV-Specific Neutralizing Antibodies. J. Virol., 85(14):6986-6995, Jul 2011. PubMed ID: 21593147. Show all entries for this paper.

vanMontfort2007 Thijs van Montfort, Alexey A. Nabatov, Teunis B. H. Geijtenbeek, Georgios Pollakis, and William A. Paxton. Efficient Capture of Antibody Neutralized HIV-1 by Cells Expressing DC-SIGN and Transfer to CD4+ T Lymphocytes. J. Immunol., 178(5):3177-85, 1 Mar 2007. PubMed ID: 17312166. Show all entries for this paper.

vanMontfort2008 Thijs van Montfort, Adri A. M. Thomas, Georgios Pollakis, and William A. Paxton. Dendritic Cells Preferentially Transfer CXCR4-Using Human Immunodeficiency Virus Type 1 Variants to CD4+ T Lymphocytes in trans. J. Viro.l, 82(16):7886-7896, Aug 2008. PubMed ID: 18524826. Show all entries for this paper.

Vcelar2007 Brigitta Vcelar, Gabriela Stiegler, Hermann M. Wolf, Wolfgang Muntean, Bettina Leschnik, Saurabh Mehandru, Martin Markowitz, Christine Armbruster, Renate Kunert, Martha M. Eibl, and Hermann Katinger. Reassessment of Autoreactivity of the Broadly Neutralizing HIV Antibodies 4E10 and 2F5 and Retrospective Analysis of Clinical Safety Data. AIDS, 21(16):2161-2170, 18 Oct 2007. PubMed ID: 18090042. Show all entries for this paper.

Veillette2014 Maxime Veillette, Anik Désormeaux, Halima Medjahed, Nour-Elhouda Gharsallah, Mathieu Coutu, Joshua Baalwa, Yongjun Guan, George Lewis, Guido Ferrari, Beatrice H. Hahn, Barton F. Haynes, James E. Robinson, Daniel E. Kaufmann, Mattia Bonsignori, Joseph Sodroski, and Andres Finzi. Interaction with Cellular CD4 Exposes HIV-1 Envelope Epitopes Targeted by Antibody-Dependent Cell-Mediated Cytotoxicity. J. Virol., 88(5):2633-2644, Mar 2014. PubMed ID: 24352444. Show all entries for this paper.

Vermeire2009 Kurt Vermeire, Kristel Van Laethem, Wouter Janssens, Thomas W. Bell, and Dominique Schols. Human Immunodeficiency Virus Type 1 Escape from Cyclotriazadisulfonamide-Induced CD4-Targeted Entry Inhibition Is Associated with Increased Neutralizing Antibody Susceptibility. J. Virol., 83(18):9577-9583, Sep 2009. PubMed ID: 19570853. Show all entries for this paper.

Verrier2001 F. Verrier, A. Nadas, M. K. Gorny, and S. Zolla-Pazner. Additive effects characterize the interaction of antibodies involved in neutralization of the primary dualtropic human immunodeficiency virus type 1 isolate 89.6. J. Virol., 75(19):9177--86, Oct 2001. URL: http://jvi.asm.org/cgi/content/full/75/19/9177. PubMed ID: 11533181. Show all entries for this paper.

Virnik2018 Konstantin Virnik, Edmund Nesti, Cody Dail, Aaron Scanlan, Alexei Medvedev, Russell Vassell, Andrew T. McGuire, Leonidas Stamatatos, and Ira Berkower. Live Rubella Vectors Can Express Native HIV Envelope Glycoproteins Targeted by Broadly Neutralizing Antibodies and Prime the Immune Response to an Envelope Protein Boost. Vaccine, 36(34):5166-5172, 16 Aug 2018. PubMed ID: 30037665. Show all entries for this paper.

vonBredow2016 Benjamin von Bredow, Juan F. Arias, Lisa N. Heyer, Brian Moldt, Khoa Le, James E. Robinson, Susan Zolla-Pazner, Dennis R. Burton, and David T. Evans. Comparison of Antibody-Dependent Cell-Mediated Cytotoxicity and Virus Neutralization by HIV-1 Env-Specific Monoclonal Antibodies. J. Virol., 90(13):6127-6139, 1 Jul 2016. PubMed ID: 27122574. Show all entries for this paper.

Vu2006 John R. Vu, Timothy Fouts, Katherine Bobb, Jennifer Burns, Brenda McDermott, David I. Israel, Karla Godfrey, and Anthony DeVico. An Immunoglobulin Fusion Protein Based on the gp120-CD4 Receptor Complex Potently Inhibits Human Immunodeficiency Virus Type 1 In Vitro. AIDS Res. Hum. Retroviruses, 22(6):477-490, Jun 2006. PubMed ID: 16796521. Show all entries for this paper.

Walker2009a Laura M. Walker, Sanjay K. Phogat, Po-Ying Chan-Hui, Denise Wagner, Pham Phung, Julie L. Goss, Terri Wrin, Melissa D. Simek, Steven Fling, Jennifer L. Mitcham, Jennifer K. Lehrman, Frances H. Priddy, Ole A. Olsen, Steven M. Frey, Phillip W . Hammond, Protocol G Principal Investigators, Stephen Kaminsky, Timothy Zamb, Matthew Moyle, Wayne C. Koff, Pascal Poignard, and Dennis R. Burton. Broad and Potent Neutralizing Antibodies from an African Donor Reveal a new HIV-1 Vaccine Target. Science, 326(5950):285-289, 9 Oct 2009. PubMed ID: 19729618. Show all entries for this paper.

Walker2010 Laura M. Walker, Melissa D. Simek, Frances Priddy, Johannes S. Gach, Denise Wagner, Michael B. Zwick, Sanjay K. Phogat, Pascal Poignard, and Dennis R. Burton. A Limited Number of Antibody Specificities Mediate Broad and Potent Serum Neutralization in Selected HIV-1 Infected Individuals. PLoS Pathog., 6(8), 2010. PubMed ID: 20700449. Show all entries for this paper.

Walker2010a Laura M. Walker and Dennis R. Burton. Rational Antibody-Based HIV-1 Vaccine Design: Current Approaches and Future Directions. Curr. Opin. Immunol., 22(3):358-366, Jun 2010. PubMed ID: 20299194. Show all entries for this paper.

Walker2011 Laura M. Walker, Michael Huber, Katie J. Doores, Emilia Falkowska, Robert Pejchal, Jean-Philippe Julien, Sheng-Kai Wang, Alejandra Ramos, Po-Ying Chan-Hui, Matthew Moyle, Jennifer L. Mitcham, Phillip W. Hammond, Ole A. Olsen, Pham Phung, Steven Fling, Chi-Huey Wong, Sanjay Phogat, Terri Wrin, Melissa D. Simek, Protocol G. Principal Investigators, Wayne C. Koff, Ian A. Wilson, Dennis R. Burton, and Pascal Poignard. Broad Neutralization Coverage of HIV by Multiple Highly Potent Antibodies. Nature, 477(7365):466-470, 22 Sep 2011. PubMed ID: 21849977. Show all entries for this paper.

Walker2011a Laura M. Walker, Devin Sok, Yoshiaki Nishimura, Olivia Donau, Reza Sadjadpour, Rajeev Gautam, Masashi Shingai, Robert Pejchal, Alejandra Ramos, Melissa D. Simek, Yu Geng, Ian A. Wilson, Pascal Poignard, Malcolm A. Martin, and Dennis R. Burton. Rapid development of Glycan-Specific, Broad, and Potent Anti-HIV-1 gp120 Neutralizing Antibodies in an R5 SIV/HIV Chimeric Virus Infected Macaque. Proc. Natl. Acad. Sci. U.S.A, 108(50):20125-20129, 13 Dec 2011. PubMed ID: 22123961. Show all entries for this paper.

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Wang2006 Shixia Wang, Ranajit Pal, John R. Mascola, Te-Hui W. Chou, Innocent Mboudjeka, Siyuan Shen, Qin Liu, Stephen Whitney, Timothy Keen, B. C. Nair, V. S. Kalyanaraman, Philip Markham, and Shan Lu. Polyvalent HIV-1 Env Vaccine Formulations Delivered by the DNA Priming Plus Protein Boosting Approach Are Effective in Generating Neutralizing Antibodies against Primary Human Immunodeficiency Virus Type 1 Isolates From Subtypes A, B, C, D and E. Virology, 350(1):34-47, 20 Jun 2006. PubMed ID: 16616287. Show all entries for this paper.

Wang2007b Jingsong Wang, Hengguang Li, Guozhang Zou, and Lai-Xi Wang. Novel Template-Assembled Oligosaccharide Clusters as Epitope Mimics for HIV-Neutralizing Antibody 2G12. Design, Synthesis, and Antibody Binding Study. Org. Biomol. Chem., 5(10):1529-1540, 21 May 2007. PubMed ID: 17571181. Show all entries for this paper.

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Wang2012 Shixia Wang, Michael Kishko, Shengqin Wan, Yan Wang, Frank Brewster, Glenda E. Gray, Avye Violari, John L. Sullivan, Mohan Somasundaran, Katherine Luzuriaga, and Shan Lu. Pilot Study on the Immunogenicity of Paired Env Immunogens from Mother-to-Child Transmitted HIV-1 Isolates. Hum. Vaccin. Immunother., 8(11):1638-1647, 1 Nov 2012. PubMed ID: 23151449. Show all entries for this paper.

Wang2018a Hongye Wang, Ting Yuan, Tingting Li, Yanpeng Li, Feng Qian, Chuanwu Zhu, Shujia Liang, Daniel Hoffmann, Ulf Dittmer, Binlian Sun, and Rongge Yang. Evaluation of Susceptibility of HIV-1 CRF01\_AE Variants to Neutralization by a Panel of Broadly Neutralizing Antibodies. Arch. Virol., 163(12):3303-3315, Dec 2018. PubMed ID: 30196320. Show all entries for this paper.

Webb2015 Nicholas E. Webb, David C. Montefiori, and Benhur Lee. Dose-Response Curve Slope Helps Predict Therapeutic Potency and Breadth of HIV Broadly Neutralizing Antibodies. Nat. Commun., 6:8443, 29 Sep 2015. PubMed ID: 26416571. Show all entries for this paper.

Wen2018 Yingxia Wen, Hung V. Trinh, Christine E Linton, Chiara Tani, Nathalie Norais, DeeAnn Martinez-Guzman, Priyanka Ramesh, Yide Sun, Frank Situ, Selen Karaca-Griffin, Christopher Hamlin, Sayali Onkar, Sai Tian, Susan Hilt, Padma Malyala, Rushit Lodaya, Ning Li, Gillis Otten, Giuseppe Palladino, Kristian Friedrich, Yukti Aggarwal, Celia LaBranche, Ryan Duffy, Xiaoying Shen, Georgia D. Tomaras, David C. Montefiori, William Fulp, Raphael Gottardo, Brian Burke, Jeffrey B. Ulmer, Susan Zolla-Pazner, Hua-Xin Liao, Barton F. Haynes, Nelson L. Michael, Jerome H. Kim, Mangala Rao, Robert J. O'Connell, Andrea Carfi, and Susan W. Barnett. Generation and Characterization of a Bivalent Protein Boost for Future Clinical Trials: HIV-1 Subtypes CR01\_AE and B gp120 Antigens with a Potent Adjuvant. PLoS One, 13(4):e0194266, 2018. PubMed ID: 29698406. Show all entries for this paper.

West2009 Anthony P. West, Jr., Rachel P. Galimidi, Christopher P. Foglesong, Priyanthi N. P. Gnanapragasam, Kathryn E. Huey-Tubman, Joshua S. Klein, Maria D. Suzuki, Noreen E. Tiangco, Jost Vielmetter, and Pamela J. Bjorkman. Design and Expression of a Dimeric Form of Human Immunodeficiency Virus Type 1 Antibody 2G12 with Increased Neutralization Potency. J. Virol., 83(1):98-104, Jan 2009. PubMed ID: 18945777. Show all entries for this paper.

West2010 Anthony P. West, Jr., Rachel P. Galimidi, Christopher P. Foglesong, Priyanthi N. P. Gnanapragasam, Joshua S. Klein, and Pamela J. Bjorkman. Evaluation of CD4-CD4i Antibody Architectures Yields Potent, Broadly Cross-Reactive Anti-Human Immunodeficiency Virus Reagents. J. Virol., 84(1):261-269, Jan 2010. PubMed ID: 19864392. Show all entries for this paper.

West2012a Anthony P. West, Jr., Ron Diskin, Michel C. Nussenzweig, and Pamela J. Bjorkman. Structural Basis for Germ-Line Gene Usage of a Potent Class of Antibodies Targeting the CD4-Binding Site of HIV-1 gp120. Proc. Natl. Acad. Sci. U.S.A., 109(30):E2083-E2090, 24 Jul 2012. PubMed ID: 22745174. Show all entries for this paper.

West2013 Anthony P. West, Jr., Louise Scharf, Joshua Horwitz, Florian Klein, Michel C. Nussenzweig, and Pamela J. Bjorkman. Computational Analysis of Anti-HIV-1 Antibody Neutralization Panel Data to Identify Potential Functional Epitope Residues. Proc. Natl. Acad. Sci. U.S.A., 110(26):10598-10603, 25 Jun 2013. PubMed ID: 23754383. Show all entries for this paper.

Willey2008 Suzanne Willey and Marlén M. I. Aasa-Chapman. Humoral Immunity to HIV-1: Neutralisation and Antibody Effector Functions. Trends Microbiol., 16(12):596-604, Dec 2008. PubMed ID: 18964020. Show all entries for this paper.

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Wu2009a Lan Wu, Tongqing Zhou, Zhi-yong Yang, Krisha Svehla, Sijy O'Dell, Mark K. Louder, Ling Xu, John R. Mascola, Dennis R. Burton, James A. Hoxie, Robert W. Doms, Peter D. Kwong, and Gary J. Nabel. Enhanced Exposure of the CD4-Binding Site to Neutralizing Antibodies by Structural Design of a Membrane-Anchored Human Immunodeficiency Virus Type 1 gp120 Domain. J. Virol., 83(10):5077-5086, May 2009. PubMed ID: 19264769. Show all entries for this paper.

Wu2010 Xueling Wu, Zhi-Yong Yang, Yuxing Li, Carl-Magnus Hogerkorp, William R. Schief, Michael S. Seaman, Tongqing Zhou, Stephen D. Schmidt, Lan Wu, Ling Xu, Nancy S. Longo, Krisha McKee, Sijy O'Dell, Mark K. Louder, Diane L. Wycuff, Yu Feng, Martha Nason, Nicole Doria-Rose, Mark Connors, Peter D. Kwong, Mario Roederer, Richard T. Wyatt, Gary J. Nabel, and John R. Mascola. Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1. Science, 329(5993):856-861, 13 Aug 2010. PubMed ID: 20616233. Show all entries for this paper.

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Xiao2009 Xiaodong Xiao, Weizao Chen, Yang Feng, Zhongyu Zhu, Ponraj Prabakaran, Yanping Wang, Mei-Yun Zhang, Nancy S. Longo, and Dimiter S. Dimitrov. Germline-Like Predecessors of Broadly Neutralizing Antibodies Lack Measurable Binding to HIV-1 Envelope Glycoproteins: Implications for Evasion of Immune Responses and Design of Vaccine Immunogens. Biochem. Biophys. Res. Commun., 390(3):404-409, 18 Dec 2009. PubMed ID: 19748484. Show all entries for this paper.

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Yang2002 Xinzhen Yang, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt, and Joseph Sodroski. Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin. J. Virol., 76(9):4634-4642, 1 May 2002. PubMed ID: 11932429. Show all entries for this paper.

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Yang2010a Qiang Yang, Cishan Li, Yadong Wei, Wei Huang, and Lai-Xi Wang. Expression, Glycoform Characterization, and Antibody-Binding of HIV-1 V3 Glycopeptide Domain Fused with Human IgG1-Fc. Bioconjug. Chem., 21(5):875-883, 19 May 2010. PubMed ID: 20369886. Show all entries for this paper.

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Yang2014 Lili Yang and Pin Wang. Passive Immunization against HIV/AIDS by Antibody Gene Transfer. Viruses, 6(2):428-447, Feb 2014. PubMed ID: 24473340. Show all entries for this paper.

Yasmeen2014 Anila Yasmeen, Rajesh Ringe, Ronald Derking, Albert Cupo, Jean-Philippe Julien, Dennis R. Burton, Andrew B. Ward, Ian A. Wilson, Rogier W. Sanders, John P. Moore, and Per Johan Klasse. Differential Binding of Neutralizing and Non-Neutralizing Antibodies to Native-Like Soluble HIV-1 Env Trimers, Uncleaved Env Proteins, and Monomeric Subunits. Retrovirology, 11:41, 2014. PubMed ID: 24884783. Show all entries for this paper.

Yates2018 Nicole L. Yates, Allan C. deCamp, Bette T. Korber, Hua-Xin Liao, Carmela Irene, Abraham Pinter, James Peacock, Linda J. Harris, Sheetal Sawant, Peter Hraber, Xiaoying Shen, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayapan, Phillip W. Berman, Merlin L. Robb, Giuseppe Pantaleo, Susan Zolla-Pazner, Barton F. Haynes, S. Munir Alam, David C. Montefiori, and Georgia D. Tomaras. HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees. J. Virol., 92(8), 15 Apr 2018. PubMed ID: 29386288. Show all entries for this paper.

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Yoshimura2010 Kazuhisa Yoshimura, Shigeyoshi Harada, Junji Shibata, Makiko Hatada, Yuko Yamada, Chihiro Ochiai, Hirokazu Tamamura, and Shuzo Matsushita. Enhanced Exposure of Human Immunodeficiency Virus Type 1 Primary Isolate Neutralization Epitopes through Binding of CD4 Mimetic Compounds. J. Virol., 84(15):7558-7568, Aug 2010. PubMed ID: 20504942. Show all entries for this paper.

Yu2018 Wen-Han Yu, Peng Zhao, Monia Draghi, Claudia Arevalo, Christina B. Karsten, Todd J. Suscovich, Bronwyn Gunn, Hendrik Streeck, Abraham L. Brass, Michael Tiemeyer, Michael Seaman, John R. Mascola, Lance Wells, Douglas A. Lauffenburger, and Galit Alter. Exploiting Glycan Topography for Computational Design of Env Glycoprotein Antigenicity. PLoS Comput. Biol., 14(4):e1006093, Apr 2018. PubMed ID: 29677181. Show all entries for this paper.

Yuan2005 Wen Yuan, Stewart Craig, Xinzhen Yang, and Joseph Sodroski. Inter-Subunit Disulfide Bonds in Soluble HIV-1 Envelope Glycoprotein Trimers. Virology, 332(1):369-383, 5 Feb 2005. PubMed ID: 15661168. Show all entries for this paper.

Yuan2006 Wen Yuan, Jessica Bazick, and Joseph Sodroski. Characterization of the Multiple Conformational States of Free Monomeric and Trimeric Human Immunodeficiency Virus Envelope Glycoproteins after Fixation by Cross-Linker. J. Virol., 80(14):6725-6737, Jul 2006. PubMed ID: 16809278. Show all entries for this paper.

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Zhang2002 Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155. Show all entries for this paper.

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Zhang2008 Mei-Yun Zhang, Bang K. Vu, Anil Choudhary, Hong Lu, Michael Humbert, Helena Ong, Munir Alam, Ruth M. Ruprecht, Gerald Quinnan, Shibo Jiang, David C. Montefiori, John R. Mascola, Christopher C. Broder, Barton F. Haynes, and Dimiter S. Dimitrov. Cross-Reactive Human Immunodeficiency Virus Type 1-Neutralizing Human Monoclonal Antibody That Recognizes a Novel Conformational Epitope on gp41 and Lacks Reactivity against Self-Antigens. J. Virol., 82(14):6869-6879, Jul 2008. PubMed ID: 18480433. Show all entries for this paper.

Zhang2010 Mei-Yun Zhang, Andrew Rosa Borges, Roger G. Ptak, Yanping Wang, Antony S. Dimitrov, S. Munir Alam, Lindsay Wieczorek, Peter Bouma, Timothy Fouts, Shibo Jiang, Victoria R. Polonis, Barton F. Haynes, Gerald V. Quinnan, David C. Montefiori, and Dimiter S. Dimitrov. Potent and Broad Neutralizing Activity of a Single Chain Antibody Fragment against Cell-Free and Cell-Associated HIV-1. mAbs, 2(3):266-274, May-Jun 2010. PubMed ID: 20305395. Show all entries for this paper.

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