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Displaying record number 500

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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 846

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MAb ID	4E10
HXB2 Location	gp160(671-676) DNA(8235..8252)	gp160 Epitope Map
Author Location	gp41( MN)
Research Contact	Herman Katinger, Inst. Appl. Microbiol. University of Agricultural Science, Vienna, Austria, or Polymum Scientific Inc.,
Epitope	NWFDIT	Epitope Alignment
Subtype	B
Ab Type	gp41 MPER (membrane proximal external region)
Neutralizing	P (tier2)  View neutralization details
Contacts and Features	View contacts and features
Species (Isotype)	human(IgG3κ)
Patient
Immunogen	HIV-1 infection
Keywords	acute/early infection, ADCC, adjuvant comparison, 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, broad neutralizer, co-receptor, complement, computational epitope prediction, contact residues, dendritic cells, drug resistance, dynamics, 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, mutation acquisition, 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 378 of 378 notes.

• 4E10: In an effort to identify new Env immunogens able to elicit bNAbs, this study looked at Envs derived from rare individuals who possess bNAbs and are elite viral suppressors, hypothesizing that in at least some people the antibodies may mediate durable virus control. The Env proteins recovered from these individuals may more closely resemble the Envs that gave rise to bNAbs compared to the highly diverse viruses isolated from normal progressors. This study identified a treatment-naive elite suppressor, EN3, whose serum had broad neutralization. The Env sequences of EN3 had much fewer polymorphisms, compared to those of a normal progressor, EN1, who also had broad serum neutralization. This result confirmed other reports of slower virus evolution in elite suppressors. EN3 Envelope proteins were unusual in that most possessed two extra cysteines within an elongated V1 region. The impact of the extra cysteines on the binding to bNAbs, virus infectivity, and sensitivity to neutralization suggested that structural motifs in V1 can affect infectivity, and that rare viruses may be prevented from developing escape. As part of this study, the neutralization of pseudotype viruses for EN3 Env clones was assayed for several bnAbs (PG9, PG16, PGT145, PGT121, PGT128, VRC01, 4E10, and 35O22). Hutchinson2019 (elite controllers, neutralization, vaccine antigen design, polyclonal antibodies)
• 4E10: The study identified a primary HIV-1 Env variant from patient 653116 that consistently supports >300% increased viral infectivity in the presence of autologous or heterologous HIV-positive plasma. In the absence of HIV-positive plasma, viruses with this Env exhibited reduced infectivity that was not due to decreased CD4 binding. This phenotype was mapped to a change Q563R, in the gp41 heptad repeat 1 (HR1) region. The authors provide evidence that Q563R reduces viral infection by disrupting formation of the gp41 six-helix bundle required for virus-cell membrane fusion. Anti-cluster I monoclonal antibodies (240-D, 246-D, F240, T32) targeting HR1 and the C-C loop of gp41 restored infectivity defects observed with Q563R. Viruses with the Q563R mutation were shown to have increased sensitivity to MPER mAbs (10E8, 7H6, 2F5, Z13e1, 4E10). Joshi2020 (viral fitness and reversion)
• 4E10: Plasma from donor PG13 was found to have MPER neutralization activity, and mAb PGZL1 was isolated. When compared to a 4E10, PGZL1 was found to share similar crystal structure, contacts, and some common germline genes, but its neutralization and polyreactivity were less strong. Its structure and germline gene usage also shared commonality with VRC42.01 and 4E10. Zhang2019a (antibody binding site, contact residues)
• 4E10: An elite HIV-controlling patient SA003 was found to have a high level of serum bNAb activity, and broadly neutralizing mAb LN01 IgG3 was isolated from patient serum. MAb 4E10 was used as a comparison in assays of autoreactivity, ADCC, neutralization, binding, and structural analyses. Pinto2019 (ADCC, antibody binding site, neutralization)
• 4E10: 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)
• 4E10: 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)
• 4E10: Pseudoviruses were produced from 37 Env clones of BC subtypes from chronically-infected patients from several regions of China. Neutralization was tested for mAbs 4E10 and 2F5. Three signature sites were identified in association with sensitivity to neutralization: L22, S29, and N706. Wang2011b (neutralization)
• 4E10: This study reported three lineages of bNAbs RV217-VRC42.01, VRC43.01 and VRC46.01 from an individual in the prospective RV217 cohort,targeting the MPER. These Abs used distinct modes of recognition and neutralized 96%, 62%, and 30%, respectively, of a 208-strain virus panel. All three lineages had modest levels of somatic hypermutation, normal Ab-loop lengths and were initiated by the founder virus MPER. The VRC42 lineage is derived from the VH gene segment 1-69 and Vκ segment 3-20 the same genes used by 4E10. The CDR H3 amino acid sequence of 4E10 is quite similar to that of VRC42 antibodies (Figure 4B) and the mapping analyses show similarities between 4E10 and the VRC42 antibodies Krebs2019 (structure, antibody lineage, broad neutralizer)
• 4E10: 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)
• 4E10: 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)
• 4E10: The authors used nuclear magnetic resonance (NMR) to define the structure of the HIV-1 MPER when linked to the transmembrane domain (MPER-TMD) in the context of a lipid bilayer. In particular, they looked at the accessibility of the MPER-TMD to 2F5, 4E10, 10E8 and DH570. The MPER appears to be accessible up to ∼10% of the time to the 2F5, 4E10, and 10E8 Fabs but ∼40% of time to the DH570 Fab. To assess possible functional roles for the MPER in membrane fusion, they generated 17 Env mutants using the sequence of a clade A isolate, 92UG037.8, mutating each of the three structural elements: hydrophobic core, turn, and kink. Mutants W670A (hydrophobic core), F673A (turn), and W680A (kink), while still sensitive to VRC01, became much more resistant to the trimer-specific bNAbs and also gained sensitivity to b6, 3791, and 17b. All mutants with changes at W666 in the hydrophobic core and K683 at the kink lost infectivity almost completely. For the rest of the mutants, infectivity ranged from 4.3 to 50.8% of that of the wild type, showing that key residues important for stabilizing the MPER structure are also critical for Env-induced membrane fusion activity, especially in the context of viral infection. Fu2018 (antibody binding site, antibody interactions, neutralization, variant cross-reactivity, binding affinity, structure)
• 4E10: Isolation of human mAb, E10, from an HIV-1-infected patient sample by single B cell sorting and single cell PCR has been reported. E10 showed binding to gp140 trimer and linear peptides derived from gp41 membrane proximal external region (MPER). F7 peptide contains IgG 4E10 epitope NWFDIT–LW, which indicated that the epitope of E10 may overlap with that of 4E10. Although E10 and 4E10 share the same germline gene family on both VH (IGHV1-69) and VL (IGKV3-20), the amino acid similarities are only 66.14% (VH) and 78.18% (VL), excluding the possibility of E10 as a variant of 4E10. IgG E10 from present study is very similar to broad neutralizing antibody 4E10. Both of them use IGHV1-69, are MPER linear epitope specific and be able to mediate ADCC activity except that E10 is less potent in neutralization (though no direct comparison). Yang2018 (ADCC)
• 4E10: 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). All of the isolates from VC20013 were sensitive to both 2F5 and 4E10. All of the isolates from VC10014 were sensitive to neutralization by 4E10. Sather2014 (neutralization, broad neutralizer)
• 4E10: The authors engineered 10E8-surface mutants to improve its potency and screened for improved neutralization against a 9-virus panel. Two mutations, V5R_HC and S100cF_HC that were found to improve neutralization using this method, were spatially separated from the 10E8 paratope. Arg5HC and Phe100cHC, were added to 10E8v4 to create an optimized 10E8 antibody, 10E8v4-5R+100cF, which retained the extraordinary breadth of 10E8 but with ˜10-fold increased potency. The new antibody was also tested in two-antibody combinations with other monoclonals, and the best overall performance was shown by the combination of 10E8v4-5R+100cF with N6, neutralizing all strains in a 208-isolate HIV-1 panel at < 1µg/mL. 4E10 was compared to 10E8 with respect to Phe100cHC, as both bind the same region of MPER, and they were found to co-recognize membrane and MPER peptide. Kwon2018 (neutralization)
• 4E10: 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. The 4 MPER bNAbs studied were grouped by epitope, either 2F5 or 4E10/10E8/DH511. Bricault2019 (antibody binding site, vaccine antigen design, computational epitope prediction, broad neutralizer)
• 10E8: 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. 4E10 used as a reference Ab. 10E8 was 1 of 2 reference 10E8-like bNAbs - 4E10 and 10E8. Crooks2015
• 4E10: Improvements to the standardization of the HIV-1 pseudovirus production procedure by implementing an automated system for aliquoting of HIV-1 pseudovirus stocks up to liter-scale are described. The automated platform and the aliquoting process were validated on as accuracy, precision, specificity and robustness. Lot-to-lot variations and virus stock integrity were assessed through two parallel neutralization assays run with the automatically aliquoted HIV pseudovirus and a manually aliquoted reference virus of the same type, by using five control reagents: sCD4, b12, 2F5, 4E10 and TriMab consisting of 2G12, IgG1b12 and 2F5. Schultz2018 (assay or method development, neutralization)
• 4E10: 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)
• 4E10: 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)
• 4E10: Assays of poly- and autoreactivity demonstrated that broadly neutralizing NAbs are significantly more poly- and autoreactive than non-neutralizing NAbs. 4E10 is polyreactive, but not autoreactive. Liu2015a (autoantibody or autoimmunity, antibody polyreactivity)
• 4E10: Panels of C clade pseudoviruses were computationally downselected from the panel of 200 C clade viruses defined by Rademeyer et al. 2016. A 12-virus panel was defined for the purpose of screening sera from vaccinees. Panels of 50 and 100 viruses were defined as smaller sets for use in testing magnitude and breadth against C clade. Published neutralization data for 16 mAbs was taken from CATNAP for the computational selections: 10-1074, 10-1074V, PGT121, PGT128, VRC26.25, VRC26.08, PGDM1400, PG9, PGT145, VRC07-523, 10E8, VRC13, 3BNC117, VRC07, VRC01, 4E10. Hraber2017 (assay or method development, neutralization)
• 4E10: 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)
• 4E10: 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 the membrane-proximal external region (MPER) in gp41 for 4E10. Hogan2018 (vaccine antigen design)
• 4E10: 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-MPER NAb 4E10, binds as well as (Kd = 15.8 nM) the binding of 2G12 to Env-ND, and this binding is insensitive to glutaraldehyde treatment . Witt2017 (vaccine antigen design, binding affinity)
• 4E10: 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)
• 4E10: 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-MPER 4E10 was used to prove that the VLP spike included the broad neutralization epitope recognized by it. Huang2017a (therapeutic vaccine, variant cross-reactivity)
• 4E10: 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)
• 4E10: The next generation of a computational neutralization fingerprinting (NFP) being used as a way to predict polyclonal Ab responses to HIV infection is presented. A new panel of 20 pseudoviruses, termed f61, was developed to aid in the assessment of experimental neutralization. This panel was used to assess 22 well-characterized bNAbs and mixtures thereof (HJ16, VRC01, 8ANC195, IGg1b12, PGT121, PGT128, PGT135, PG9, PGT151, 35O22, 10E8, 2F5, 4E10, VRC27, VRC-CH31, VRC-PG20, PG04, VRC23, 12A12, 3BNC117, PGT145, CH01). The new algorithms accurately predicted VRC01-like and PG9-like antibody specificities. Doria-Rose2017 (neutralization, computational epitope prediction)
• 4E10: This review discusses host controls of bNAb responses and why highly antigenic vaccine Envs do not induce bNAbs when used as vaccine immunogens. 4E10 is polyreactive for human host lipids and proteins and binds to RNA splicing factor 3b subunit 3 (SF3B3). Kl mice expressing VDJ rearrangements of 4E10, exhibit severe defects in B-cell development with 95% of immature bone marrow B cells lost at the first tolerance checkpoint and peripheral B cells anergic. Kelsoe2017 (review, antibody polyreactivity)
• 4E10: 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)
• 4E10: A weakly neutralizing antibody was isolated, CAP248-2B. The glycan dependence of CAP248-2B was compared to other known gp120-gp41 interface targeting bNAbs (8ANC195, 35O22, PGT151, 3BC315). CAP248-2B blocks the binding of 35O22, 3BC315, and PGT151 (but not 8ANC195 or 4E10) to cell surface envelope trimers. Wibmer2017 (antibody interactions)
• 4E10: 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. 2F5 and 4E10 were selected as representative mAbs of the MPER class. Cheeseman2017 (genital and mucosal immunity, immunoprophylaxis)
• 4E10: To understand HIV neutralization mediated by the MPER, antibodies and viruses were studied from CAP206, a patient known to produce MPER-targeted neutralizing mAbs. 41 human mAbs were isolated from CAP206 at various timepoints after infection, and 4 macaque mAbs were isolated from animals immunized with CAP206 Env proteins. Two rare, naturally-occuring single-residue changes in Env were identified in transmitted/founder viruses (W680G in CAP206 T/F and Y681D in CH505 T/F) that made the viruses less resistant to neutralization. The results point to the role of the MPER in mediating the closed trimer state, and hence the neutralization resistance of HIV. 4E10 neutralized CAP206 viruses from all timepoints; it was one of several mAbs tested for neutralization of transmitted founder viruses isolated from clade C infected individuals CAP206 and CH505, compared to T/F viruses containing MPER mutations that confer enhanced neutralization sensitivity. Bradley2016a (neutralization)
• 4E10: 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. 4E10 used as a reference Ab. PGT4E10 was 1 of 2 reference 10E8-like bNAbs - 4E10 and 10E8. Crooks2015 (glycosylation, neutralization)
• 4E10: 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)
• 4E10: 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)
• 4E10: 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. MPER Ab 4E10 did not bind cell surface whether gp160 was missing C-terminal or not, but did neutralize 92UG037.8 HIV-1 isolate weakly. Chen2015 (neutralization, binding affinity)
• 4E10: Factors that independently affect bNAb induction and evolution were identified as viral load, length of untreated infection and viral diversity. Ethnically, black subjects induced bNAbs more than white subjects, but this did not correlate with type of Ab response. Fingerprint analyses of induced bNAbs showed strong subtype-dependency, with subtype B inducing significantly higher levels of CD4bs Abs and non-subtype B inducing V2-glycan specific Abs. Of the 239 bNAb antibody inducers found from 4,484 HIV-1 infected subjects,the top 105 inducers' neutralization fingerprint and epitope specificity was determined by comparison to the following antibodies - PG9, PG16, PGDM1400, PGT145 (V2 glycan); PGT121, PGT128, PGT130 (V3 glycan); VRC01, PGV04 (CD4bs) and PGT151 (interface) and 2F5, 4E10, 10E8 (MPER). Rusert2016 (neutralization, broad neutralizer)
• 4E10: 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)
• 4E10: Crystallography was used to examine two nonneutralizing 4E10 Fabs mutated to decrease the hydrophobicity of the CDR-H3 loop. Although the mutations did not affect the affinity for the 4E10 epitope in solution, the two nonneutralizing Fabs were unable to bind to MPER inserted into plasma membrane mimicking the in vivo binding environment. This supports the hypothesis that neutralization by 4E10 requires an antigenic structure more complex than just the linear epitope, and likely constrained by viral membrane lipids. Rujas2015 (antibody binding site, structure)
• 4E10: Crystallography was used to show that 4E10 interacts with an extended target that includes both the gp41 MPER and viral membrane lipids. The 4E10 CDRH1 loop bound to the lipid head groups, while the CDRH3 interacted with the hydrophobic lipid tails. Vaccines targeting the MPER may require a lipid component, so these results will aid in the design of vaccine immunogens that more effectively target the MPER. Irimia2016 (antibody binding site, vaccine antigen design, structure)
• 4E10: The gp41 MPER region targeted by 4E10 and 10E8 is an attractive target for vaccine development. Habte2015 developed a gp41 immunogen, gp41-HR1-54Q, consisting of shortened heptad repeat (HR) regions 1 and 2 and MPER in the context of a 6-helix bundle. Four putative fusion intermediates were engineered by introducing mutations into HR1 of this construct in order to destabilize the 6-helix bundle. One variant elicited antibodies in rabbits that targeted residues W672, I675 and L679, critical for 4E10/10E8 recognition. Banerjee2016 (vaccine antigen design, structure)
• 4E10: This review discusses an array of methods to engineer more effective bNAbs for immunotherapy. Antibody 4E10 is an example of engineering through rational mutations; it has been combined with 10E8 as part of a strategy to combine the CDRs of bnAbs targeting similar epitopes. Hua2016 (immunotherapy, review)
• 4E10: This review discusses the breakthroughs in understanding of the biology of the transmitted virus, the structure and nature of its envelope trimer, vaccine-induced CD8 T cell control in primates, and host control of bnAb elicitation. Haynes2016 (review)
• 4E10: 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. 4E10 has been used as a control in testing CD4 binding site neutralizing specificity of the sera. Sanchez-Merino2016 (neutralization, acute/early infection)
• 4E10: A new, current, mostly tier2 panel of 200 C-clade Env-psuedotyped viruses from early (< 100d) infection in southern Africa was used to assess antibody responses to natural infection and to vaccines. Viruses were assayed with bNAbs targeting the V2 glycan (PG9, VRC26.25), the MPER site (4E10), the CD4 binding site (VRC01), and the V3/C3 glycan site (PGT128). For 4E10 (and all other Abs besides PGT128) there was no significant difference in neutralization between pre-seroconversion and post-seroconversion viruses. Viruses collected pre-seroconversion were more resistant to neutralization by serum than those post-seroconversion. As the epidemic matured over 13 years, viruses also became more resistant to mAbs tested. Rademeyer2016 (assay or method development, neutralization)
• 4E10: 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. MPER-binding, first-generation mAb, 4E10 when compared had a geometric mean of IC₅₀=10.3 µg/ml for the 6/12 viruses it neutralized at a potency of 50%. 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)
• 4E10: This study examined the neutralization of group N, O, and P primary isolates of HIV-1 by diverse antibodies. Cross-group neutralization was observed only with the bNAbs targeting the N160 glycan-V1/V2 site. Four group O isolates, 1 group N isolate, and the group P isolates were neutralized by PG9 and/or PG16 or PGT145 at low concentrations. None of the non-M primary isolates were neutralized by bNAbs targeting other regions, except 10E8, which weakly neutralized 2 group N isolates, and 35O22 which neutralized 1 group O isolate. Bispecific bNAbs (PG9-iMab and PG16-iMab) very efficiently neutralized all non-M isolates with IC₅₀ below 1 ug/mL, except for 2 group O strains. Anti-MPER bNAb 4E10 was unable to neutralize any of the 16 tested non-M primary isolates at an IC₅₀< 10µg/ml. Morgand2015 (neutralization, subtype comparisons)
• 4E10: 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. 4E10, a gp41 MPER bnAb belonged to a group with slopes <1 (like others 10E8 and 2F5), but 10E8 had a significantly lower IC₅₀. Webb2015 (neutralization)
• 4E10: A gp41 immunogen, gp41-HR1-54Q, was developed, consisting of shortened heptad repeat regions 1 and 2 and the MPER. It was efficiently recognized by 3 MPER-binding Abs (2F5, Z13e1 and 4E10). In rabbits, the antigen was highly immunogenic but failed to develop neutralization ability. Habte2015 (vaccine antigen design)
• 4E10: Mice and guinea pigs were immunized with Norovirus P particles displaying conformational 4E10 and 10E8 epitopes. Both mice and guinea pigs developed high levels of MPER-binding antibodies. The sera of guinea pigs, but not mice, showed modest neutralizing ability against HIV Env pseudoviruses, suggesting that Norovirus may be useful as a platform to present epitopes for vaccination strategies. Yu2015 (vaccine antigen design)
• 4E10: A panel of antibodies was tested for binding, stability, and ADCC activity on HIV-infected cells. The differences in killing efficiency were linked to changes in binding of the antibody and the accessibility of the Fc region when bound to infected cells. Ab 4E10 lacked ADCC. Bruel2016 (binding affinity)
• 4E10: To test whether NAbs can inhibit viral transmission through mucosal tissue, 4 bNAbs (PG9, PG16, VRC01, 4E10) were tested in tissue culture models of human colonic and ectocervical tissues. All 4 nAbs reduced HIV transmission, with a relative efficacy of PG16 > PG9 > VRC01 >> 4E10. The nAbs had a good safety profile and were not affected by the presence of semen. Scott2015 (immunotherapy)
• 4E10: The ontogeny of 4E10 was delineated through structural and biophysical comparisons of the mature antibody with multiple potential precursors. 4E10 gained affinity through a small number of mutations to a highly conserved recognition surface. Results suggested that neutralization by 4E10 may involve mechanisms beyond simply binding, also requiring the ability of the antibody to induce conformational changes distant from its binding site. 4E10 is, therefore, unlikely to be re-elicited by conventional vaccination strategies. Pre-binding of 4E10 at the MPER affects the binding of b12 at the CD4 binding site. Finton2014 (antibody interactions, structure, antibody lineage)
• 4E10: 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. 4E10 neutralized 97% of the 199 viruses tested. Hraber2014 (neutralization)
• 4E10: This study aim to develop a replicating vector system for the delivery of HIV-1 antigens on the basis of an apathogenic foamy virus. This consists of the MPER and the fusion peptide proximal region (FPPR). By stepwise shortening of distinct linker residues between both the domains lead to enhanced recognition by 4E10. This indicates that a specific positioning of FPPR and MPER domains is critical for improved Ab binding. Muhle2013 (vaccine antigen design)
• 4E10: A subset of bNAbs that inhibit both cell-free and cell-mediated infection in primary CD4+ lymphocytes have been identified. These antibodies target either the CD4-binding site or the glycan/V3 loop on HIV-1 gp120 and act at low concentrations by inhibiting multiple steps of viral cell to cell transmission. This property of blocking viral transmission to plasmacytoid DCs and interfering with type-I IFN production should be considered an important characteristic defining the potency for therapeutic or prophylactic antiviral strategies. 4E10 was not effective in blocking cell to cell transmission of virus. Malbec2013
• 4E10: The effect of PNGS on viral infectivity and antibody neutralization (2F5, 4E10, b12, VRC01, VRC03, PG9, PG16, 3869) was evaluated through systemic mutations of each PNGS on CRF07_BC strain. Mutations at N197 (C2), N301 (V3), N442 (C4), and N625 (gp41) rendered the virus more susceptible to neutralization by MAbs that recognize the CD4 binding site or gp41. Generally, mutations on V4/V5 loops, C2/C3/C4 regions, and gp41 reduced the neutralization sensitivity to PG16. However, mutation of N289 (C2) made the virus more sensitive to both PG9 and PG16. Mutations at N142 (V1), N355 (C3) and N463 (V5) conferred resistance to neutralization by anti-gp41 MAbs. Available structural information of HIV Env and homology modeling was used to provide a structural basis for the observed biological effects of these mutations. Wang2013 (neutralization, structure)
• 4E10: 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). McCoy2015 (neutralization)
• 4E10: Autoreactivity and polyspecificity of 4E10 using a synthetic human peptidome has been reported. 4E10 was shown to be polyreactive, binding peptides from various proteins, but only in a limited manner. Analysis of B cell development in 4E10 heavy-chain knock-in mice confirmed that 4E10 does recognize self-antigens. Three of the top five hits are from types 1, 2 and 3 inositol trisphosphate receptors, with high scoring peptides sharing a conserved sequence motif. Validation of the top hits was performed by binding analyses and staining of tissue sections, which combined to identify the type 1 inositol trisphosphate receptor as the most likely 4E10 physiological autoantigen. Finton2013 (structure, antibody polyreactivity)
• 4E10: This paper showed that FcγRI occasionally potentiates neutralization by Abs against the V3 loop of gp120 and cluster I of gp41. FcγRI providing a kinetic advantage for neutralizing Abs against partially cryptic epitopes independent of phagocytosis has been reported. The antibiotic bafilomycin A1 and the weak base chloroquine were used as lysosomotropic agents to block phagocytosis in TZM-bl and TZM-bl/FcγRI cells. These treated cells and 2 HIV-1 subtype B Env-pseudotyped viruses (6535.3 and QH0692.42) were assayed with 4E10. Expression of FcγRI dramatically improved the neutralizing activity of 4E10 against both viruses in the absence of lysosomotropic agents. Moreover, neither lysosomotropic agent showed any evidence of reversing the FcγRI-mediated effect on 4E10. Perez2013 (antibody interactions)
• 4E10: This study reported profound negative selection of B cells in 4E10 “knock-in” mice. C57BL/6 embryonic stem cells were modified by gene targeting to introduce HIV antibody H- and L-chain variable exons, replacing the respective J clusters. 4E10H and HL mice had significantly reduced splenic B cell numbers. Results showed that 4E10 is, to a physiologically significant extent, autoreactive. Negative selection occurred by various mechanisms including receptor editing, clonal deletion and receptor downregulation. Doyle-Cooper2013
• 4E10: 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.4E10 did not block Env-Galcer binding. Dennison2014 (ADCC, antibody binding site, antibody interactions, glycosylation)
• 4E10: 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. 4E10 (˜25 μg/mL) yielded partial protection. Yang2014 (immunoprophylaxis, review, antibody gene transfer)
• 4E10: 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)
• 4E10: 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)
• 4E10: A mutant of 4E10 (G100A) was designed to rigidify the CRF H3, decreasing its binding to membranes, and it was consistently able to neutralize viruses with higher potency than wild type 4E10. MPER antibodies, including 4E10 and 10E8, are likely to neutralize by a common mechanism: targeting the fusion-intermediate state of gp41 with the help of their lipid-binding activity. The greater neutralization by 10E8, compared to 4E10, may be due to its preference for cholesterol-rich HIV-1-like membranes and weaker association with cellular membranes. Chen2014 (neutralization, structure)
• 4E10: Tolerance deletion due to mAb autoreactivity limits 2F5 bNAb induction. Autoantigen recognized by 4E10 is splicing factor 3b subunit 3 (SF3B3), so that most 2F5-bearing B cells are deleted in the bone marrow and a minor population survives as anergic B cells. 4E10 binds MPER and uses only VH1-69 and Vκ3-20 just as mAb Cap206-CH12 does even though they are derived from two separate individuals, showing that only a few VH and VL pairs suffice its (and other Ab) production. These are reasons why bNAbs are not readily made and their response is subdominant to other non-neutralizing Env responses. Haynes2013 (review)
• 4E10:This study identified human kynureninase (KYNU) and splicing factor 3b subunit 3 (SF3B3) as the primary conserved, vertebrate self-antigens recognized by the 2F5 and 4E10 antibodies, respectively. 2F5 binds the H4 domain of KYNU which contains the complete 2F5 linear epitope (ELDKWA). 4E10 recognizes an epitope of SF3B3 that is strongly dependent on hydrophobic interactions. Opossums carry a rare KYNU H4 domain that abolishes 2F5 binding, but they retain the SF3B3 4E10 epitope. Immunization of opossums with HIV-1 gp140 induced extraordinary titers of serum antibody to the 2F5 ELDKWA epitope but little or nothing to the 4E10 determinant. Identification of structural motifs shared by vertebrates and HIV-1 provides direct evidence that immunological tolerance can impair humoral responses to HIV-1. Yang2013
• 4E10: A model that predicts the concentrations at which MAbs 2F5 and 4E10 effectively neutralize HIV is presented. The model predicts that for these antibodies to be effective at neutralization, the time to disable an epitope must be shorter than the time the antibody remains bound in this conformation, about five minutes or less for 4E10 and 2F5. 2F5 IgG, but not 4E10, is much more effective at neutralization than its Fab fragment. Hu2014 (neutralization)
• 4E10: 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 4E10. Gupta2013
• 4E10: The molecular features, immunoreactivity, and functional avidity of 4E10 were studied. Kunert2004 (antibody sequence)
• 4E10: 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. 4E10 showed high neutralization titer against BG505 pseudovirus in a competitive binding assay as shown in Table 1. Hoffenberg2013 (antibody interactions)
• 4E10: 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. 4E10 neutralized 98% of a cross-clade panel of 157 HIV-1 isolates (Fig. S1) while 1F7 neutralized only 20% of the isolates. Gach2013 (neutralization)
• 4E10: 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, 4E10 and a serum control 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. Gach2014 (neutralization, HAART, ART)
• 4E10: MHC Class II-restricted T_H activation was shown to be a key determinant controlling nonneutralizing MPER Ab responses. T_H H2d epitope KWASLWNWF, partially overlapping the 2F5 MPER epitope, was required for MPER Ab induction. Zhang2014
• 4E10: This study reports development of a new cell line, A3R5-based highly sensitive Ab detection assay. This T-lymphoblastoid cell line stably expresses CCR5 and recognize CCR5-tropic circulating strains of HIV-1. A3R5 cells showed greater neutralization potency compared to the current cell line of choice TZM-bl. 4E10 was used as a reference Ab in neutralization assay comparing A3R5 and TZM-bl. McLinden2013 (assay or method development)
• 4E10: 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. 4E10 is an MPER Ab, with breadth 88%, IC₅₀ 9.98 μg per ml, and its unique feature listed is presence of a pre-transmembrane domain sequence. Kwong2013 (review)
• 4E10: Biosynthesis and structure determination of a micelle-bound MPER trimer, designated as gp41-M-MAT, is reported to highlight the importance of this binding site in designing the vaccines. NMR analysis showed that MPER peptides adopt symmetric α helical conformations exposing binding sites. The helical conformation of 4E10 epitope in gp41-M-MAT is similar to that observed in the co-crystal structure of MPER bopund to 4E10. Contact residues F49, W56 and K59 played major roles in conferring binding affinity in the nanomolar range. Reardon2014 (antibody binding site, structure, contact residues)
• 4E10: 2 HIV-1 infectious molecular clones (IMCs) derived from subtypes C and CRF01_AE HIV-1 primary isolates expressing LucR (IMC.LucR) were engineered to express heterologous gp160 Envs. There was a trend towards increased sensitivity in a subtype mismatched-backbone with 4E10 for both AE and C Envs, indicating possible structural changes in Env imposed by the backbone genes on the MPER. Chenine2013 (assay or method development, neutralization)
• 4E10: Knockin (KI) mice models expressing H chains from MAbs 4E10 and 48d were generated, in addition to previously used KI mice expressing 2F5. Only KI mice expressing MPER+ BnAb HCs triggered a profound early BM developmental blockade, consistent with the self-reactivity of both the 2F5 and 4E10 BnAb HCs being sufficient to trigger clonal B cell deletion. Chen2013
• 4E10: Env pseudo-typed viruses generated from 7 transmitting and 4 non-transmitting mothers and their children were used 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. Baan2013 (neutralization, mother-to-infant transmission)
• 4E10: 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, 4E10. The small panel of 12 Env clones should facilitate assessments of vacine-elicited NAbs. Decamp2014 (assay or method development)
• 4E10: A computational method to predict Ab epitopes at the residue level, based on structure and neutralization panels of diverse viral strains has been described. This method was evaluated using 19 Env-Ab including 4E10, against 181 diverse HIV-1 strains with available Ab-Ag complex structures. Chuang2013 (computational epitope prediction)
• 4E10: 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)
• 4E10: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 4E10 is discussed as the MPER region-targeting,, potent and broadly neutralizing anti-gp41 mAb exhibiting ADCC activity and having a linear epitope. Pollara2013 (ADCC, review)
• 4E10: "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)
• 4E10: 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". 4E10 was used in the anti-gp41 Ab cocktail in SDS-PAGE and western blot experiments to prove that enzymes removed junk Env from VLPs and inactivated virus. Crooks2011 (glycosylation)
• 4E10: Generation of a series of chemically modified MPER immunogens through derivatization of amino acid side chains and evaluation of the binding affinity to their cognate mAbs is described. The modification of peptides has little effect on binding to the antibodies. A selected immunogen containing both 2F5 and 4E10 epitopes and a threonine at T676 elicited the highest anti-peptide IgG titer but not high neutralization. 4E10 has been used as a bnAb directed to MPER. Venditto2013 (antibody interactions, vaccine antigen design, binding affinity)
• 4E10: The role of NK cells and NK cell receptor polymorphisms in the assessment of HIV-1 neutralization is reported. 4E10 was used in viral inhibition assay as a control to compare NK cells participation and activity. Brown2012 (neutralization, NK cells)
• 4E10: 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. None of the selected Env antigens exhibited mutations in the critical recognition determinants of 4E10 Wang2012 (mother-to-infant transmission)
• 4E10: Molecular mechanism of how MPER permeates lipid monolayers containing cholesterol, a main component of the viral envelope, was studied using grazing incidence X-ray diffraction and X-ray reflectivity. MPER did not affect the lateral packing order of lipids, but changed its membrane insertion depth and topology in cholesterol-enriched membranes. This correlated with an increment of the surface area occupied by MPER helices, and the optimal exposure of the 4E10 epitope. Ivankin2012 (antibody binding site, structure)
• 4e10: 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)
• 4E10: 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: gp41 MPER, pre-TM helix, 4E10 class, 4E10 family. Kwong2012 (review, structure, broad neutralizer)
• 4E10: 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)
• 4E10: Different adjuvants, including Freund's adjuvant (FCA/FIA), MF59, Carbopol-971P and 974P were compared on their ability to elicit antibody responses in rabbits. Combination of Carbopol-971P and MF59 induced potent adjuvant activity with significantly higher titer nAbs than FCA/FIA. There was no difference in binding of this MAb to gp140 SF162 with FIA adjuvant, but there was 3-fold decrease of antigenicity with MF59, C971, C974, C971+MF59 C971+MF59 as compared to the unadjuvanted sample. Lai2012 (adjuvant comparison)
• 4E10: 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 the binding and neutralizing properties were evaluated. 4E10, an MPER Ab, was among the 17 bnAbs which were used in to study the mutations in FWR. Fig S4C described the comparison of Ab framework amino acid replacement vs. interactive surface area on 4E10. Klein2013 (neutralization, structure, antibody lineage)
• 4E10: 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. 4E10 has been referred as NAb against MPER. Kovacs2012 (antibody binding site, neutralization, binding affinity)
• 4E10: Crystal structure and mechanistic analysis of 2F5-gp41 complex is reported. 4E10 has been referred as a BnAb directed against the transmembrane gp41 envelope glycoprotein. Studies with protoliposome confirms the importance of lipid membrane and hydrophobic context in the binding of 4E10 to gp41. Ofek2004 (antibody interactions, structure)
• 4E10: The study used the swarm of quasispecies representing Env protein variants to identify mutants conferring sensitivity and resistance to BnAbs. Libraries of Env proteins were cloned and in vitro mutagenesis was used to identify the specific AA responsible for altered neutralization/resistance, which appeared to be associated with conformational changes and exposed epitopes in different regions of gp160. The result showed that sequences in gp41, the CD4bs, and V2 domain act as global regulator of neutralization sensitivity. 4E10 was used as BnAb to screen Env clones. wtR clone was resistant to 4E10, but N197H mutation caused 6 fold increase and Y384H and L702P caused 21 fold increase in neutralization in neutralization. ORourke2012 (neutralization)
• 4E10: 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. 4E10 was used in BN-PAGE trimer shift assay. Melchers2012 (neutralization)
• 4E10: 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. 4E10 has been referred in discussing the breadth and potency of antiCD4 abs. West2012a (antibody lineage)
• 4E10: 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. 4E10 was used to determine and compare the immunogenicity of homo and heterotrimers gp140s. 2F5 and 4E10 bound similarly to the homotrimeric clade A and B Q168/SF162L, Q259/SF162NL and Q461/SF1621 heretotrimers and the corresponding homotrimers. Sellhorn2012 (vaccine antigen design)
• 4E10: This study shows that epitope mapping of plasma antibodies followed by the rational design of MPER peptide tetramer can successfully isolate antigen-reactive single B cells for Ig rescue. Recombinant mAb CAP206-CH12 was isolated using the peptide tetramer antigen. This is a polyreactive mAb and used the same VH and Vk Ig family as mAb 4E10 and overlapped the epitopes. Comparison of IC50 suggested that CAP206-CH12 is less potent than 4E10. Morris2011
• 4E10: The use of computationally derived B cell clonal lineages as templates for HIV-1 immunogen design is discussed. 4E10 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)
• 4E10: Polyclonal B cell responses to conserved neutralization epitopes are reported. Cross-reactive plasma samples were identified and evaluated from 308 subjects tested. 4E10 was used as a control mAb in the comprehensive set of assays performed. Plasma samples C1-0269, C1-0534 and C1-0536 showed activities similar to 4E10. C1-0269 was sensitive to the W672A mutation, which ablated 4E10 neutralization. Tomaras2011 (neutralization, polyclonal antibodies)
• 4E10: 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. Native deglycosylated clade B JFRL gp140 and group M consensus gp140 Env CON-S increased 4E10 reactivity, whereas fully glycosylated gp140 env didn't bind. The authors inferred that glycan interferences control the binding of unmutated ancestor Abs of broad neutralizing mAb to Env gp41. Ma2011 (glycosylation, neutralization)
• 4E10: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. 4E10 has been discussed regarding the sites of HIV-1 vulnerability to neutralizing antibodies and particularly recognition of highly conserved MPER region of Env. Kwong2011 (antibody binding site, neutralization, vaccine antigen design, review)
• 4E10: 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. 4E10 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)
• 4E10: 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. 4E10 has been used as a positive control for epitope mapping and evaluating these anti-gp-41 antibodies. Cloned anti-gp41 antibodies (n=13) did not bind to membrane proximal peptides recognized by 4E10. Mouquet2011 (neutralization)
• 4E10: 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. 4E10 (carboxy-terminal MPER) is discussed in the context of developing broadly cross-neutralizing antibodies. Overbaugh2012 (escape, review)
• 4E10: Neutralization activity was compared against MAb 10E8 and other broad and potent neutralizers in a 181-isolate Env-pseudovirus panel. 4E10 neutralized 98% of viruses at IC50<50 μg/ml and 37% of viruses at IC50<1 μg/ml, compared with 98% and 72% of MAb 10E8, respectively. Huang2012a (neutralization)
• 4E10: Antigenic properties of undigested VLPs and endo H-digested WT trimer VLPs were compared and 4E10 was 100-fold more sensitive to trimer VLPs than other MAbs suggesting increased exposure of the gp41 base. Binding to E168K+ N189A WT VLPs was merely a trend of binding to the parent WT VLPs and uncleaved VLPs. There was no significant correlation between E168K+N189A WT VLP binding and 4E10 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)
• 4E10: Prior to this study, no one has been able to elicit potent and broad neutralizing antibodies, like 2F5 or 4E10, targeting the gp41 MPER region. To address this problem, a recombinant immunogen, designated NCM, consisting of the N- and C-terminal heptad repeats that can form a six-helix bundle (6HB) and the MPER region of gp41 was constructed and expressed. Two mutations (T569A and I675V) previously reported to expose the neutralization epitopes were introduced. NCM and its mutants could react with MAbs NC-1, 2F5, 4E10 specific for 6HB and MPER of gp41, suggesting that these antigens are in the form of a trimer of heterodimer (i.e., 6HB) with three exposed MPER tails. Antigen with double mutations elicited strong antibody response in rabbits and these antibodies exhibited broad and potent neutralizing activity. Wang2011a (vaccine antigen design)
• 4E10: 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)
• 4E10: 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)
• 4E10: 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)
• 4E10: 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)
• 4E10: 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. Anti-HIV-1 MAb reactivity was limited mainly to HIV-1-related antigens. The APS autoAbs reacted strongly with cardiolipin (CL), yet only 4E10 bound CL at high concentrations; both 2F5 and 4E10 bound their HIV-1 epitopes with a 2-3-log higher apparent affinity than CL. Moreover, the polyreactivity of 4E10, but not CL15, could be blocked with dried milk. Singh2011 (antibody polyreactivity)
• 4E10: 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. 4E10 and sCD4 were active against all viruses tested. Observed substitutions at positions 671,674, 675, 676 had minimal effect on viral sensitivity to 4E10. Shang2011 (glycosylation, neutralization, subtype comparisons)
• 4E10: 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. 4E10 neutralized all 14 viruses and shedding activity was high against 13/14 viruses. Ruprecht2011 (neutralization, kinetics)
• 4E10: Anti-MPER MAbs 4E10, 2F5 and Z13e1 were probed for binding to HIV-1 and SIV virions with protein A-conjugated gold (PAG) nanoparticles using negative-stain electron microscopy. The MAbs moderately associated with virions, including those devoid of MPER epitopes, and this interaction was strong enough to resist washout. MPER epitope-bearing virions liganded with CD4 showed a much higher association of anti-MPER antibodies compared to the unliganded virions. The results are consistent with a two-stage binding model where these anti-MPER MAbs bind first to the viral lipid bilayer and then to the MPER epitopes following spontaneous or induced exposure. Rathinakumar2012 (binding affinity)
• 4E10: MPER antigenicity was analyzed in the context of the plasma membrane and a role for the gp41 transmembrane domain (TM) in exposing the epitopes of three bNt MAbs (2F5, 4E10, and Z13e1) was identified. Critical binding residues for the three Nt MAbs were identified using a panel of 24 MPER-TM1 mutants bearing single amino acid substitutions in the MPER; many were previously shown to affect MAb-mediated viral neutralization. Non-Nt mutants of MAbs 2F5 and 4E10 exhibited a reduction in binding to MPER-TM1 and yet maintained binding to synthetic MPER peptides, indicating that MPER-TM1 better approximates the MPER neutralization-competent structure (NCS) than peptides. Replacement of the gp41 TM and CT of MPER-TM1 with the platelet-derived growth factor receptor (PDGFR) TM reduced binding by MAb 4E10, but not 2F5, indicating that the gp41 TM plays a pivotal role in orienting the 4E10 epitope, and more globally, in affecting MPER exposure. Montero2012 (antibody binding site)
• 4E10: A novel function for lentiviral Nef is reported: it renders the HIV-1 virion refractory to the broadly-neutralizing antibodies 2F5 and 4E10. Nef conferred 50-fold resistance to 2F5 and 4E10, but had no effect on HIV-1 neutralization by MPER-specific NAb Z13e1, by the peptide inhibitor T20, nor by a panel of nAbs and other reagents targeting gp120. Given the membrane-dependence of MPER-recognition by 2F5 and 4E10, in contrast to the membrane-independence of Z13e1, it is suggested that Nef alters MPER recognition in the context of the virion membrane. Lai2011 (neutralization)
• 4E10: 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)
• 4E10: A screening platform was developed that chemically mimics viral and host membrane lipids and replicated NAb membrane interactions. The assay is based on a surface plasmon resonance (SPR) spectroscopy and monitors antibody binding to thiol self-assembled monolayers (SAMs). By simply mimicking lipid chemistry, these thiol SAMs allowed to isolate and distinguish chemical groups that could potentially contribute to specific antibody–lipid interactions. Only 2F5 and 4E10 bound strongly to hydrophobic thiols, correlated with findings that suggest that 2F5 and 4E10 embed into the hydrophobic membrane core. This translates to vaccine design by suggesting that immunogens designed to elicit 2F5/4E10-like antibodies may require an accessible hydrophobic component available for B-cell receptor recognition. Hardy2012 (assay or method development)
• 4E10: 2F5 and 4E10 molecular interactions with epitope cores in MPER and lipid bilayers were studied using combined atomic force and confocal microscopies. Both mAbs form lipid-segregated aggregates on supported lipid bilayers (SLBs) and do not induce other significant membrane perturbations. Furthermore, the affinity of MPER toward membranes is differently affected by both mAbs and correlates with the mAbs-epitope core lipid interactions. 2F5 is able to dock the MPER peptide on the membrane, whereas 4E10 extracts the MPER from the lipid bilayer. Franquelim2011 (antibody binding site)
• 4E10: 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. Both wild-type and mutated clones of each subtype were found to be highly sensitive to 4E10. A trend towards a higher resistance of mutated clones compared to wild-type clones was nevertheless observed for 0377-I1, 0978-M1 and 1021-I1 CRF01-AE clones. However, the opposite was observed for 5008CL2, 11005CL3 and 11005CL7 clade B clones with a trend towards a higher sensitivity of the mutated counterparts. Collectively, comparing 2F5/4E10 IC50 toward wild-type or mutated clones did not reveal any significant difference. Thenin2012a (neutralization)
• 4E10: 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 to inhibit mDC-mediated virus spread, compared with cell-free transmission. Blocking the FcRs expressed on mDCs prior to antibody exposure had negligible impact on the ability of 4E10 to inhibit mDC-mediated trans-infection 4E10 and 2F5 bound a significantly greater percentage of mDCs, compared with b12. All abs bound a significantly greater percentage of mDCs, compared with the secondary antibody alone. Lai and Lai/Balenv required significantly higher 4E10 concentrations to block mDC-mediated versus cell-free infection of autologous T cells. 4E10 localized at DC–T cell synaptic junctions in the absence of Gag-eGFP VLPs. Sagar2012 (neutralization, binding affinity)
• 4E10: 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)
• 4E10: 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. Deglycosylation had no apparent difference in the binding of the gp41-MPER directed MAb 2F5. Depetris2012 (glycosylation, binding affinity)
• 4E10: MAbs 4E10 and b12 were examined for antibody-dependent neutralization, or antibody-dependent complement (C)-mediated neutralization, of infection of PBMC by either free HIV-1 or trans infection by HIV bound to erythrocytes. Neutralization of free HIV-1 by b12 was stronger than by 4E10, but b12 neutralized erythrocyte-bound HIV-1 less efficiently than cell-free virus. 4E10 did not neutralize erythrocyte-bound HIV-1 and at a low concentration it caused enhancement of infection. Antibody (4E10)-dependent C activation inhibited trans infection by erythrocyte-bound HIV-1, but caused enhanced infection with cell-free HIV-1 in the presence of erythrocytes. No effects of C were observed with b12. Beck2011 (neutralization)
• 4E10: 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 4E10 to immature particles was greater than to mature virions and the increase was abolished by truncation of the gp41 CT. 4E10 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)
• 4E10: 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. Only one clone was resistant to 4E10 (P1046 J1). Kishko2011 (neutralization, mother-to-infant transmission)
• 4E10: Two HCDR2 allelic variants of the V^H2-5 inferred unmutated ancestor germ line of the 2F5 bNAb (2F5 UAs) are described. Both variant putative germ line Abs bound to gp41 peptide and protein antigens and are thus capable of recognizing either linear or conformational gp41 epitopes. However, their binding affinities for the gp41-inter protein are an order of magnitude weaker than those of 4E10. Alam2011 (binding affinity)
• 4E10: The role of envelope expression context and producer cell type was characterized for nine novel replication-competent chimeric HIV-1 isolates from the dominant circulating HIV-1 subtypes in Africa, where most new HIV-1 infections are occurring. Pseudoviruses generated in 293T cells were the most sensitive to antibody neutralization. Replicating viruses generated in primary lymphocytes were most resistant to neutralization by most monoclonal antibodies including 4E10. PBMC-derived chimeras displayed increased neutralization resistance compared to 293T-derived chimeras for 4E10. Provine2012 (neutralization)
• 4E10: Epitope accessibility of the gp41 neutralizing antibodies, 2F5 and 4E10, is explored either on the functional spike or during receptor-mediated entry and it is determined if these antibodies bind to the static spike on the surface of the HIV-1 or require target cell/receptor engagement to gain access to their MPER binding sites. The neutralization activity of 4E10 against lab-adapted viruses and sensitive and moderately resistant viruses was largely unaffected by relatively rapid antibody-virus washing, suggesting direct interaction with the “static” spike. However, for more neutralization-resistant viruses, the 4E10 could neutralize only under the “no antibody-virus wash” conditions, implying that the MPER epitopes were not accessible prior to receptor engagement. Chakrabarti2011 (antibody binding site, neutralization)
• 4E10: 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. 4E10 was included for comparison and neutralized 19% of contemporary viruses at IC50 < 1 μ g/ml and 81% 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 TriMab and 2F5 clustered with 4E10, most likely due to the proximal localization of the epitopes. Euler2011 (neutralization)
• 4E10: 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)
• 4E10: 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 4E10 neutralized 96% 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 median antibody concentration required to inhibit HIV activity by 50% or 90% (IC50 and IC90 values) was almost 100-fold lower that of b12, 2G12 and 4E10. Walker2011 (neutralization, broad neutralizer)
• 4E10: The characteristics of HIV-1-specific NAbs were evaluated in 100 breast-fed infants of HIV-1-positive mothers who were HIV-1 negative at birth and they were monitored until age 2. A panel of eight viruses that included variants representative of those in the study region as well as more diverse strains was used to determine the breadth of the infant NAbs. 4E10 had low neutralization potency for 2 (BF535.A1 and Q842d16) out of 8 pseudoviruses in the panel, no neutralization potency for 1 (BJ613.E1) and high for the rest of them. Lynch2011 (neutralization, variant cross-reactivity, mother-to-infant transmission)
• 4E10: 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)
• 4E10: The impact of specific changes at distal sites on antibody binding and neutralization was examined on Q461 variants. The changes at position 675 in conjunction with Thr to Ala at position 569 increased the 4E10 neutralization sensitivity by ∼6-fold compared to viruses with only mutation at position 675. There was detectable but modest neutralization by 4E10 with only T569A change. Little to no detectable binding was observed for 4E10. Lovelace2011 (antibody binding site, neutralization, variant cross-reactivity, binding affinity)
• 4E10: A monostratified epithelium using HT-29 cells transduced to express CCR5 was constructed to model the transcytosis of HIV-1 across columnar epithelial cells because CCR5-tropic viruses are the dominant viruses transmitted in vivo and are preferentially transcytosed across intestinal epithelial cells in vitro. 4E10 displayed no inhibitory effect against transcytosis of NL4-3.Balecto. Shen2010a (binding affinity)
• 4E10: 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. 4E10 only neutralized SHIV-SF162P4 (clade B) out of 4 clade C and 2 clade B SHIV strains tested. Siddappa2010 (neutralization, vaccine antigen design, subtype comparisons)
• 4E10: A high resolution gp41 structure, termed HR1-54Q was presented consisting of the N-terminal helical heptad repeat (HR1), the C-terminal helical heptad repeat (HR2), and the (membrane-proximal external region) MPER. HR1-54Q bound to 3 broadly neutralizing Abs that target gp41: 2F5, 4E10, Z13e1, as well as 98-6 MAb that recognizes the six-helix bundle. The binding epitope of 4E10 superimposed very well on the MPER in HR1-54Q and binds tightly to HR1-54Q. HR1-54Q possesses several structural characteristics required for induction of 4E10 including the correct conformation and exposure to solvent that both triggers the immune system and generates Abs that appropriately recognize gp41. Shi2010 (structure)
• 4E10: 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)
• 4E10: The two distinct and conflicting models of C-terminal tail (CTT) topology for HIV-1 gp41 were tested by characterizing the accessibility of KE (Kennedy epitope) sequences of gp41 to Ab binding on the surface of Env-expressing cells and intact mature virions. 4E10 binds effectively to KE in the context of intact virions. Steckbeck2010 (binding affinity)
• 4E10: 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 shows a remarkable breadth of reactivity. 4E10 can provide complete protection against SHIV challenge in macaques when administered alone or in combination with other mAbs. Gonzalez2010 (neutralization, variant cross-reactivity, escape, review)
• 4E10: 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 was mentioned in the context of immunogens based on the epitopes recognized by bNAbs. Walker2010a (review)
• 4E10: This review discusses the types of B-cell responses desired by HIV-1 vaccines and various methods used for eliciting HIV-1 inhibitory antibodies that include induction and characterization of vaccine-induces B-cell responses. 4E10 was mentioned when discussing virus-like particles and liposomes, as 4E10 requires lipid binding in addition to gp41 MPER recognition for neutralization breadth. Tomaras2010 (review)
• 4E10: 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. 33 out of 37 Env clones were neutralized by 4E10 possibly due to the presence of WFXI motif in gp41. The other 4 Env clones were moderately resistant to 4E10 despite having minimum WFXI motif. Ringe2010 (neutralization, variant cross-reactivity)
• 4E10: 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)
• 4E10: 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 4E10 epitopes for all the viruses used are provided. 4E10 showed moderate to high binding affinity to pseudoviruses from clade A (epitope mutants:tWFDIs, NWFDIs), clade B (NWFDIT) and clade D (NWFsIT), weak binding to clade B (sWFsIT), clade C (sWFsIT) and clade CRF01_AE (NWFDIT, NWFDIs), and no binding to clade C (sWFsIT). Pseudoviruses from clade A (NWFDIs), clade B (NWFDIT), clade C, clade D and clade CRF01_AE were neutralized by 4E10. The presence of sCD4 significantly increased the binding affinity of 4E10 to clade A (tWFDIs) and clade C (sWFsIT), although no significant increase in binding affinity was observed for the other pseudoviruses. Peachman2010a (antibody binding site, neutralization, variant cross-reactivity, binding affinity, subtype comparisons)
• 4E10: 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. Two mutations in the gp41 ectodomain (I595F and K655E) and one in the CD4 binding pocket (F423Y) were selected by treatment of viruses with attachment inhibitors BMS-313216 and BMS-378806. Pseudotyped viruses containing all three mutations showed enhanced neutralization sensitivity to MAbs 2F5 and 4E10. The three mutations were shown not to affect the rate of HIV entry into cells indicating that the observed level of sensitivity of the viruses to the two bNAbs was not due to this effect. Zhou2010a (enhancing activity, neutralization)
• 4E10: 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. A panel of mutants were tested to determine whether they can improve the neutralization sensitivity of an extremely neutralization-resistant clinical isolate. 4E10 neutralized wild-type sensitive clone and 11/16 mutants tested (D179N, N179D, D179E, D179Q, D179H, D179S, D179A, D179N-P182S, V1/V2_006, V2_006 and V1_005). ORourke2010 (neutralization, variant cross-reactivity)
• 4E10: MAb m9 showed superior neutralization potency compared to 4E10 in a TZM-bl assay including subtypes A, B, C, D, AE and AG where it neutralized 89% of the isolates tested while 4E10 neutralized 53%. 4E10 also showed lower inhibition potency of cell-to-cell transmission of HIV-1 compared to m9. Zhang2010 (neutralization, variant cross-reactivity)
• 4E10: 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)
• 4E10: 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 with GBV-C E2. MAb 4E10 neutralized a dual-tropic R5-X4 HIV-1 isolate in primary human PBMCs. The TriMAb control including 4E10 did not neutralize the HIV-1 R5 isolate in TZM-bl cells but did in PBMCs. Ag interaction with Anti-GBV-C E2 Abs is similar to that of with 4E10, that reacts with HIV-1 gp41 peptides and permeabilized cells. Mohr2010 (neutralization)
• 4E10: Cross-reactive NAb responses were characterized in 39 acute and chronically HIV-1 infected individuals. Abs targeting the 4E10 epitope were found in three of the patients, and one of those also had Abs targeting the 2F5 epitope. Sather2010 (variant cross-reactivity)
• 4E10: 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. 4E10 neutralized all three viruses tested in a TZM-bl assay, and inhibited fusion induced by Aldrithiol-2 inactivated HIV-1 in Sup-T1 T cells. Lipid binding of 4E10 was not dependent on the presence of β2GP1. Moody2010 (neutralization, binding affinity)
• 4E10: Targeted neutralizing epitopes have been identified based on the change in sensitivity to neutralization due to variations in known immunoepitopes studied in 17 subjects. There was no neutralizing activity that targeted the 4E10 epitope in any of the patient sera when the K665N/W672 mutant was used for screening of neutralizing activity. Nandi2010 (neutralization, escape)
• 4E10: The antigenic structure of Gag-Env pseudovirions was characterized and it was shown that these particles can recapitulate native HIV virion epitope structures. 4E10 bound to the BaL Gag-Env pseudovirions, indicating presence of native trimers. The Gag-Env pseudovirions were further used to identify a subset of antigen-specific B cells in chronically infected HIV subjects. Hicar2010 (binding affinity, structure)
• 4E10: 4E10 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 4E10 for virions to be quantified. There was an overall reduction in the efficiency of capture of molecular clones (MC) relative to pseudotyped virions by 4E10. In addition, nontrimeric Envs from JR-CSF MC virus were more efficiently captured by 4E10 than trimeric JR-FL. It is suggested that the capture of virions by 4E10 is mostly mediated by nonfunctional Env. It was also shown that soluble Env and MPER peptides can associate with Env-deficient particles and mediate 4E10-specific virion capture. Leaman2010 (assay or method development, binding affinity)
• 4E10: 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)
• 4E10: 18 unique Env clones of subtype C HIV-1 derived from six African countries and Scotland were tested for their neutralization susceptibility by MAbs. Five of the gp160 chimeras tested for their neutralization by 4E10 were susceptible to neutralization by this Ab as their core WFXI MPER motif was conserved. Koh2010a (neutralization)
• 4E10: 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 4E10 and there was only a small change in binding affinity to 4E10. gp41 immunogenicity was increased by V1 loop deletion, although gp41 antibodies did not bind to the 4E10 epitope. D368R modification to SF162gp120 did not affect the binding and neutralization by 4E10. Ching2010 (neutralization, binding affinity)
• 4E10: A new computational design of epitope-scaffolds was introduced to design immunogens in which the 4E10 epitope was transplanted into many different small scaffold proteins. 103 4E10 epitope scaffolds were designed that presented a stabilized 4E10 epitope in an immunogenic format of similar structural specificity as MAb 4E10. There was high affinity for 4E10 by the designed epitope-scaffolds when assessed for binding affinity and kinetics. Assessment of crystal structures of epitope-scaffolds showed excellent epitope structural mimicry. Correia2010 (mimotopes, vaccine antigen design, kinetics, binding affinity, structure)
• 4E10: MPER peptide analogs with charged helical C-terminal Api or Aib tails displayed enhanced binding to 4E10 and Z13e1 MAbs. When replacement of Phe673 with residues Phe(2-F)-OH or Phe(β-OH)-OH was combined with the helical Api tail, the peptide analogs were found to bind 4E10 with high affinity. Ingale2010 (binding affinity)
• 4E10: 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 4E10) 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 4E10. Doria-Rose2010 (neutralization)
• 4E10: The review describes several different methods that have been used to isolate and characterize HIV MAbs within the human Ab repertoire. Relative advantages and limitations of methods such as EBV transformation, human hybridoma, non-immortalized B cell culture, combinatorial libraries from B cells and clonal sorting are discussed. Hammond2010 (review)
• 4E10: Addition of bacterial endotoxin (LPS) had no effect on the potency of 4E10 neutralization in TZM-bl assay but addition of LPS in PBMC assay increased neutralization potency of 4E10. 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)
• 4E10: 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 4E10, 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 4E10 on virus infectivity. Significant variation in sensitivity to 4E10 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)
• 4E10: Crystal structure of the extracellular domain of gp41 has been solved including fusion peptide proximal region (FPPR) heptad repeat 1 and MPER to examine their influence on gp41 post fusion conformation. Their presence increased the melting temperature of gp41 complex greatly compared to the core structure of gp41. Comparison of the solved crystal structure with the MPER conformation in complex with 4E10 suggests that 4E10 epitope is present throughout gp41 refolding from a native conformation, and that 4E10 could present its CDR3 loop implicated in bilayer interaction towards the membrane. Buzon2010 (antibody binding site, structure)
• 4E10: 21c binding, autoreactivity, polyreactivity and protective benefits are discussed and compared to other autoreactive MAbs, such as 2F5 and 4E10. Regulation of CD4i MAbs, such as 21c and 17b, by tolerance mechanisms is discussed. Haynes2010 (autoantibody or autoimmunity, antibody polyreactivity)
• 4E10: Subtype B HIV-1 variants from contemporary seroconverters (individuals that seroconverted between 2003 and 2006) showed a trend toward decreased sensitivity to neutralization by 4E10 compared to the variants isolated from historical seroconverters (individuals that seroconverted between 1985 and 1989). Bunnik2010a (neutralization, dynamics)
• 4E10: 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 4E10, neutralizing 100% of HIV-1 primary isolates of subtypes A, B, C, D, F, CRF01_AE and CRF02_AG, while 4E10 neutralized some isolates of subtypes A and D, and all isolates of subtypes B, C, CRF01_AE and CRF02_AG. Unlike sCD4-17b, 4E10 was not equivalently active against virus particles generated from different producer cell types. Lagenaur2010 (neutralization, variant cross-reactivity, subtype comparisons)
• 4E10: 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. 4E10 bound more efficiently to all uncleaved ΔV1V2 variant trimers compared to the full-length trimer, although the differences were minor. Bontjer2010 (binding affinity)
• 4E10: 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 was tested using the known neutralizing Abs. There was no significant effect on 4E10 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)
• 4E10: Review discusses the recent research done to improve the production, quality, and cross-reactivity of binding Abs, neutralizing Abs, monoclonal Abs with broad neutralizing activity, ADCC, and ADCVI Abs, and catalytic Abs. Studies focusing on several aspects of BNAb roles in vaccine development, and studies done to better understand the broad binding capacity and the exposure of epitopes of BNAbs are reviewed. Baum2010 (ADCC, neutralization, binding affinity, review)
• 4E10: Neutralizing activities of 4E10 were similar against parent and GnTI (complex glycans of the neutralizing face are replaced by fully trimmed oligomannose stumps) viruses, and the N301Q mutant virus (glycan at position 301 is removed). This suggests that the antennae of the complex glycans of gp120 and the upper part pf gp41 have little or no influence on 4E10 access to MPER. Removing terminal sialic acid moieties on complex glycans by neuraminidase did not affect virus neutralization sensitivity to 4E10. The ability of 4E10 to complex with and deplete Env trimers on blue native polyacrylamide gel electrophoresis (BN-PAGE) correlated with its ability to neutralize. Binley2010 (glycosylation, neutralization, binding affinity)
• 4E10: GPI-anchored and secretory scFvs of 4E10 were generated. GPI-scFvs were localized in the lipid raft of the plasma membrane. Cells transduced with the secretory 4E10 scFv showed more than 50% neutralization activity against all 11 pseudotype viruses belonging to clades A, B, B', C and E. Cells transduced with 4E10 GPI-scFv neutralized all 11 pseudotype viruses with increased potency compared to secretory scFvs (more than 90% neutralization activity). Wen2010 (neutralization)
• 4E10: Four subjects were found infected with viruses carrying MPER polymorphisms associated with resistance to neutralization by 4E10. In two of the subjects (a mother and child pair), clones resistant to neutralization by 4E10 carried W680G substitution. Another subject had W680R viruses, with varying range of susceptibility to 4E10 neutralization. W680 substitutions in the above subjects were found highly associated with substitutions at positions 677 and 683, where the presence of a charged residue at position 680 resulted in a change in the charge distribution at positions 677 and 683. Substitutions in the resistant viruses were not associated with fitness cost, as a resistant virus was fit enough to be transmitted from the mother to her child. In the fourth subject, F673L substitution was found in one of the viral clones, conferring resistance to 4E10 neutralization. Nakamura2010 (neutralization, escape, mother-to-infant transmission)
• 4E10: L669S substitution in gp41 dramatically increased (>250-fold) neutralization sensitivity of mutant virus to 4E10. Binding affinity of 4E10 to linear peptide with the L669S mutation was higher compared to its binding affinity to the wild type peptide. 4E10 binding affinity was also significantly increased for L669S mutation in peptide-lipid complex compared to the wild type. The lifetime of 2F5 neutralization was shown to be ∼3 fold longer for the L669S virus compared to wild type, indicating that the L669S mutation altered the MPER structure such that 4E10 and 2F5 epitopes were exposed for a longer time. Shen2010 (antibody binding site, neutralization, kinetics)
• 4E10: Neutralization potency of 4E10 was compared to that of HK20 scFv in TZM-based assay using 45 Tier 1 and Tier 2 HIV isolates. 4E10 neutralized 44/45 isolates. Sabin2010 (neutralization, variant cross-reactivity)
• 4E10: Prefusion (gp140), prehairpin intermediate (gp41-inter) and postfusion (gp41-post) constructs were developed to define conformational states recognized by non-neutralizing cluster II Abs. gp41-inter was re-constructed replacing the six helix bundle with GCN4. 4E10 bound to, and showed the same kinetic profile, for both gp41-inter and GCN4-gp41-inter constructs, suggesting identical MPER conformation of the two constructs. Frey2010 (kinetics, binding affinity, structure)
• 4E10: Unlike for b12, decreasing neutralization sensitivity during the course of infection was not observed for 4E10 in 15 patients studied. Bunnik2010 (neutralization)
• 4E10: 4E10 was used in competition assays with gp41 Abs cloned from B cells from patients with broadly neutralizing sera. None of the Abs from these patients competed for binding with 4E10. 4E10 competed for binding with MAbs 2F5 and D17. Pietzsch2010 (antibody interactions, binding affinity)
• 4E10: 4E10 wild type, Fv 4E10, and two Fv 4E10 mutants (4E10-W100A and 4E10-G50E) all bound with comparable affinities to peptides and monomeric and trimeric gp140. However, the affinities for gp140 were about 10-fold weaker than for peptides. W100A and G50E mutations reduced interactions of 4E10 with viral membranes but did not affect binding of 4E10 to peptides or gp140. W100A mutation was shown to reduce the ability of 4E10 to lift the MPER up from the membrane, while G50E had no such effect. In neutralization assays, W100A mutation reduced 4E10 potency while the G50E mutation increased the overall neutralization potency of 4E10. It is suggested that 4E10 primarily interacts with its peptide epitope but that the optimal interaction requires partial lifting of MPER out of the viral membrane, mediated by tryptophan 100. Xu2010 (antibody binding site, neutralization, binding affinity)
• 4E10: Variants of IgG1 4E10 with nonconservative substitutions of tryptophan in the CDRH3 region exhibited similar affinities for epitope peptide compared to 4E10 wild type. However, binding of the variants to viral membrane surfaces and epitope in a membrane context were diminished compared to 4E10 wild type, and correlated with their markedly diminished neutralization activities. Single Asp substitutions had a more deleterious effect on neutralization than single Ala substitutions, and double substitutions acted cooperatively. It is suggested that Trp residues in the CDRH3 region play a crucial role in 4E10 neutralization by enabling 4E10-lipid interactions. Scherer2010 (antibody binding site, neutralization, binding affinity)
• 4E10: A dimerization domain is described in the C-terminal domain of gp41 (C54), where two C54 monomers form an asymmetric, antiparallel coiled coil. 2F5 and 4E10 bind to C54 with higher affinity compared to linear MPER peptides, and the interaction is biphasic described by a two-step conformational change model. 2F5 formed a more stable complex with C54 than 4E10. A conformational change accompanied the interaction of 2F5 and 4E10 with C54. It is suggested that the conformation of C54 dimer is a potential intermediate, capable of interacting with 2F5 and 4E10. Liu2010 (antibody binding site, binding affinity)
• 4E10: The specificities of 4E10 binding to MPER peptides and phospholipids on the viral membrane are reviewed. Implications of 4E10 anti-host cell activity are discussed. 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)
• 4E10: 6 male Indian rhesus macaques were given a dose of 4E10 one day prior and one day after challenge with SHIVBa-L, which was chosen because it was reasonably neutralization sensitive to both 2F5 and 4E10. All animals but one showed the absence of viral replication. Sera of all animals showed no gp120-specific responses, and no cellular immune responses were observed in any animals but one. 4E10 serum half-life was estimated to 4.1 days. 4E10 was shown poor at mediating antibody-dependent cell-mediated virus inhibition (ADCVI) compared to b12. Hessell2010 (immunoprophylaxis)
• 4E10: 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. 4E10 neutralization activity was compared to the three new broadly neutralizing mAbs. 4E10 did not compete for binding to gp41 with any of the new mAbs. 4E10 neutralized 100% of Tier 1 and 99% of Tier 2 viruses, being superior to the new mAbs. Corti2010 (neutralization)
• 4E10: 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. 4E10 was used as a control and it neutralized 5/5 Tier 1 and 5/5 Tier 2 viruses. Scheid2009 (neutralization)
• 4E10: Exogenous epitope tags were introduced in different parts of three variable regions, V1, V2 and V4, of two HIV isolates, SF162 and SF33. In the majority of the cases, tags did not have any effect on the susceptibility of the isolates to neutralization by 4E10. Only two viruses with tags in their V1 and V2 regions were more sensitive to neutralization by 4E10 compared to wild type. Wallace2009 (antibody binding site, neutralization)
• 4E10: 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)
• 4E10: The structure and dynamic of the virion spike and the MPERe are discussed. Data revealing MPER steric barriers to Ab access, and recent results on the model for the structure and accessibility of the MPER on the native spike and the mechanisms of action for 4E10 are reviewed. Implications of the data for immunogen design is discussed. Schief2009 (antibody binding site, review)
• 4E10: TZM-bl and PBMC systems were compared to investigate the influence of target cell environment on HIV entry inhibition. 4E10 was shown to be significantly less active on TZM-bl cells. 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)
• 4E10: 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 (antibody binding site, autologous responses, review)
• 4E10: 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 4E10. Importance of identification and characterization of new epitopes, and of B-cell stimulation, is discussed. Montefiori2009 (review)
• 4E10: Isolates of 12 viruses were shown to be sensitive to neutralization by 4E10 in both PBMC and TZM-bl assays, but the potency of 4E10 against several isolates was considerably lower in the TZM-bl assay. The study suggests that TZM-bl assay can fail to detect neutralizing activity of in vivo relevance. 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)
• 4E10: Ab specificities of a panel of HIV sera were systematically analyzed by selective adsorption with native gp120 and specific mutant variants. To test sera for presence of 4E10-like Abs, MPER peptides overlapping the core epitopes of 2F5 and 4E10 were used. Neutralization of HXB2, SF162 and JRFL by some of the sera was inhibited by the 4E10 peptide, indicating presence of 4E10-like Abs. Sera with limited neutralizing activity were mapped to V3. 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. Li2009c (assay or method development)
• 4E10: 4E10 membrane-binding 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)
• 4E10: 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 4E10, is displayed. Korber2009 (review)
• 4E10: HA-gp41, an antigen representing the trimeric fusion-intermediate conformation of gp41, was constructed and shown to bind to 4E10 with high nanomolar affinity. Rabbits immunized with HA-gp41 produced gp41-specific Abs that recognized epitopes overlapping with 4E10. Sera from immunized animals lacked neutralizing activity. Hinz2009 (vaccine-induced immune responses, kinetics, binding affinity)
• 4E10: 4E10 alone was not able to trigger complement-mediated lysis (CML) of 93BR020 and 92UG037 strains, however, it did so in combination with 2G12. CML was more pronounced when HLA-B44 allo-specific serum was combined with 4E10. Lysis experiments of viruses from three donors showed that 4E10 in combination with allotype-specific Abs B44, B8, A11, Cw4 or Cw7 significantly increased CML. 4E10 in combination with Abs against HLA A1 and Cw3 resulted in significant reduction in CML. Hildgartner2009 (complement)
• 4E10: FcγR-mediated inhibition and neutralization of HIV by 4E10 and other MAbs is reviewed. The review also summarizes the role of ADCC and ADCVI Abs on HIV infection inhibition and neutralization. Forthal2009 (review)
• 4E10: 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. All variants were found more sensitive to neutralization by 4E10 than the wild type, indicating that deletion of V1/V2 increases MPER accessibility. Bontjer2009 (antibody binding site, neutralization)
• 4E10: 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)
• 4E10: 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 4E10 were smaller than those for VRC01. Zhou2010 (neutralization, structure)
• 4E10: Broadly neutralizing sera from elite neutralizers exhibited significant sensitivities to mutations I165A, N332A, and N160K. 4E10 neutralization activity was tested for pseudoviruses with the mutations relative to the WT. 4E10 neutralization was not affected by the three mutations. Unlike PG9 and PG16, 4E10 neutralized kifunensine-treated pseudoviruses with similar potency as wild type pseudoviruses. Walker2010 (neutralization)
• 4E10: Two formats of Ab libraries displayed on the surface of yeast were combined to construct the first scFab yeast display Ab library. 4E10 was used to validate the new display system. 4E10 in the scFab format had a 4-fold higher affinity to ag than 4E10 expressed in the scFv format. 4E10 scFab also exhibited similar binding and neutralization profiles as 4E10 scFv. Walker2009b (assay or method development, neutralization, binding affinity)
• 4E10: EPR and NMR were used to define 4E10-induced MPER conformational changes. Large conformational changes of the MPER were observed upon binding of 4E10, where the Ab straddled the helix-hinge-helix MPER segment and extracted residues W672 and F673. It is suggested that the initial interaction of 4E10 CDRH3 loop with W680 residue allows the MPER to wrap around the base of 4E10 and bring the key residues closer to the hydrophobic CDRH2 loop for extraction. Song2009 (antibody binding site)
• 4E10: Patient sera from 13 HIV controllers and 75 chronic viremic patients were tested for levels of Ab binding to the 4E10 epitope. HIV controllers had the same levels of direct binding Abs to 4E10 peptide epitopes as viremic HIV-1 infected individuals. There was a higher level of binding to the 2F5 peptide than the 4E10 peptide. 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)
• 4E10: 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 ten Indian Envs were sensitive to 4E10, consistent with the presence of a WFXI motif important for 4E10 recognition. Two of the clones contained a PNLG in the 4E10 epitope. 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, but none of those occurred in the 4E10 epitope. Kulkarni2009 (neutralization, acute/early infection)
• 4E10: This MAb was shown to bind to the E2 (656-670) peptide, containing the MAb epitope, but not to E1 (532-546) peptide derived from the FPPR of gp41. Binding of 4E10 to the E2 peptide showed rapid dissociation. Core epitope was shown to be WFNIT. Fiebig2009 (kinetics, binding affinity)
• 4E10: A review about the in vivo efficacy of 4E10 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)
• 4E10: 4E10 neutralization breadth and potency was compared to that of two broadly neutralizing Abs PG9 and PG16 in a panel of 162 multi-clade viruses. 4E10 exhibited lower neutralization potency than PG9 and PG16. Walker2009a (neutralization, variant cross-reactivity)
• 4E10: 4E10 recognition of model cell or viral membranes with or without the presence of the peptide containing the MAb epitope was examined. 4E10 bound to both membranes with high affinity, binding better to the viral membrane, suggesting that involvement of the antigen-binding site is present. Binding of 4E10 increased significantly and exhibited almost irreversible binding in the presence of the membrane bound peptide epitope complex. It is suggested that 4E10 binds specifically to both the membrane and the peptide, most likely in combination, and that the composition of the membrane is important for recognition. Veiga2009 (antibody binding site, kinetics, binding affinity)
• 4E10: Glyco-engineered tobacco plants were used for efficient expression of recombinant 4E10 with quantitative β1,4-galactosylation (AA structure). Antigen binding capacity of 4E10 glycoforms compared to CHO-derived 4E10 was 115-140%. Neutralization activity of fully galactosylated 4E10 was more than 3 times higher than that of other plant-derived glycoforms and CHO-derived 4E10. Strasser2009 (neutralization, binding affinity)
• 4E10: 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 4E10. Sreepian2009 (neutralization, variant cross-reactivity, binding affinity)
• 4E10: Four IgA MAb were isolated from Cambodian exposed but uninfected women through a construction of phage libraries and selection by gp41-ΔMPR and P1. These MAbs were correlated to protection from HIV-1 infection in HEPS. 4E10 could not compete with IgA Fab 43 for binding to P1. Tudor2009 (binding affinity)
• 4E10: 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 4E10. Simek2009 (neutralization)
• 4E10: Substantial increase in neutralization potency (∼5000-fold) of 4E10 was observed in cells expressing FcγRI, and a moderate increase in cells expressing FcγRIIb. Cells expressing FcγRIIa and FcγRIIIa did not have any effect on the neutralization potency of this Ab. None of the FcγRs increased the neutralization potency of 4E10 Fab, but FcγRI had a stronger effect on the IgG1 version of 4E10 than on the IgG3 version. The effect of the FcγRs was observed only for MPER-specific Abs. Thus, FcγRI and FcγRIIb facilitated antibody-mediated neutralization of HIV-1 that was dependent on the Fc region, IgG subclass, and Ab epitope specificity. Perez2009 (isotype switch, neutralization)
• 4E10: Aqueous two-phase partition system (ATPS) was used to successfully separate 4E10 from unclarified tobacco extract with a yield of 84%. 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)
• 4E10: High purity (95%) and high yield (60-80%) of 4E10 purification from transgenic tobacco plants was achieved by using a biomimetic ligand (4E10lig) which mimics both electrostatic and hydrophobic interactions of 4E10-binding sequence. 4E10lig was specific for 4E10 and competed with the 4E10-peptide epitope for the same binding site on the MAb. Yielded MAb was fully active and free of degraded variants. Platis2009 (assay or method development)
• 4E10: Δ9-12a, 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 10-fold more sensitive to neutralization by 4E10 compared to the parental R3A virus. TA1, a mutant with a 15 amino acid deletion of the distal half of V3, also exhibited a 10-fold increase in neutralization sensitivity to 4E10 compared to R3A. Nolan2009 (neutralization)
• 4E10: Swarm analysis of viruses from one patient resulted in isolation of several different clones with different neutralization sensitivities against four HIV-1 positive sera. Comparison of sequences from two clones, one neutralization resistant and the other one not, revealed seven amino acid differences of which only Q655R showed increase in neutralization sensitivity to 4E10. This mutation disrupted a ring of hydrogen bonds in gp41 trimer and favored prehairpin intermediate structure. When 655R was introduced into two other neutralization resistant, unrelated viruses it also significantly increased sensitivity to neutralization by 4E10. ORourke2009 (neutralization, acute/early infection)
• 4E10: Binding of 4E10 to lipid antigens was studied. 4E10 bound to a variety of phospholipids, cardiolipin, a sulfated glycolipid, sulfogalactosyl ceramide, and to two neutral glycolipids. 4E10 also bound to cholesterol, squalene, and lipid A derived from Gram-negative bacteria. Matyas2009 (binding affinity)
• 4E10: Unlike b12, 4E10 was not able to inhibit formation of virological synapses, it did not block the transfer of HIV particles from infected to target cells, and it did not block the trogocytic transfer of CD4 molecules from target to infected cells. Analysis of late events of HIV transmission showed, however, that 4E10 was able to block infection of target cells, indicating that HIV infection is transmitted by a neutralization-sensitive mechanism. Massanella2009
• 4E10: There was an association between 4E10 Abs and anticardiolipin in serum samples from slow progressors. Martinez2009 (autoantibody or autoimmunity)
• 4E10: Crystal structure of a MPER subdomain was determined. The structure suggests that the four hydrophobic residues critical for the neutralization activity of 4E10 are buried within the MPER trimer interface. In experiments, 4E10 was able to bind to monomeric MPER but failed to bind to trimeric MPER. Liu2009 (antibody binding site)
• 4E10: A REMD solution simulation of a 21-amino acid MPER peptide including both 2F5 and 4E10 epitopes showed increased epitope exposure upon reduction of hydrophobic character of the peptide. The 21-aa peptide adopted a favorable conformation for Ab binding in solution, but when inserted into the VP2 puff of the HRV14 it adopted a less favorable conformation. Lapelosa2009 (computational epitope prediction)
• 4E10: Monovalent and bivalent structures of 4E10 differing in size, valency, and flexibility were compared. All of the 4E10 reagents exhibited high antigen binding affinities but the bivalent 4E10 bound to gp41 with higher affinities. All of the 4E10 constructs neutralized a panel of subtype B virus isolates, with the bivalent forms exhibiting only modest improvements in neutralization potency compared to the monovalent forms, suggesting that cross-linking HIV-1 epitopes does not contribute to the neutralizing mechanism of 4E10. Increased distance and flexibility between Ab combining sites did correlate with enhanced neutralization for 4E10, suggesting restricted mobility of the trimeric spikes in the viral surface. The size of construct also correlated with neutralization potency of 4E10, suggesting that the 4E10 epitope on gp41 is presented in a sterically constrained environment. Klein2009 (antibody binding site, neutralization, kinetics, binding affinity)
• 4E10: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:1-69, IGHD:3-16, D-RF:nd, IGHJ:1. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner. Gorny2009 (antibody sequence)
• 4E10: Three plasmas with broadly cross-neutralizing activities and high titers of MPER Abs were identified among 156 chronically infected patients. Viruses were neutralized 10-fold more efficiently by MPER Abs eluted from one of the plasmas than by 4E10. JR-FL virus was better neutralized by these MPER abs than by 2F5, 4E10 and Z13e1. Alanine scanned mutants of the MPER showed increased sensitivity to neutralization by 4E10 and the three plasmas. Neutralization by 4E10 was ablated by residues with changes at W672, F673, T676 and W680. Gray2009a (neutralization)
• 4E10: Ten new non-neutralizing, cross-reactive mAbs were found in immunized mice. 4E10 only reacted with a subset of different Env subtypes tested due to amino acid substitutions in the epitope. Positive control V3 mAb F39F and gp41 mAb 4E10 and 7B2 were used to assess the activity of gp140 proteins following immobilization. Gao2009 (variant cross-reactivity)
• 4E10: 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). 4E10 neutralized some viruses better in the virus infectivity assays compared to pseudovirus 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)
• 4E10: Four groups of Abs were detected in a patient directed against mimotopes of MPER, V3, C1 and LLP2. The MPER mimotope shared key amino acid residues with the 4E10 epitope. The mimotope was able to bind 4E10-like Abs, and a peptide presenting the 4E10 epitope strongly competed for 4E10 binding. Plasma from this patient also showed high reactivity against cardiolipine. This indicated presence of 4E10-like Abs in this patient. There were no mutations in the key amino acids of the 4E10 epitope of the patient virus, but D674 and N677K mutations were observed at latter time points that may have impact on 4E10 neutralization sensitivity. Indeed, the earliest virus from the patient as very sensitive to neutralization by 4E10, while the second time point isolate showed 50-fold decrease in sensitivity, and the late viruses demonstrated low or no sensitivity to 4E10. Dieltjens2009 (autoantibody or autoimmunity, mutation acquisition, neutralization, dynamics)
• 4E10: Binding of 4E10 to its nominal epitope, and to a longer biepitope peptide-liposome conjugate was best described by a two step encounter-docking model. Less efficient docking of 4E10 to its nominal epitope compared to 2F5 correlated with the less exposed nature of 4E10 nominal epitope on the membrane surface. Both 2F5 and 4E10 showed a more efficient docking to the biepitope peptide-liposome structures than to nominal epitopes, indicating that the conjugate provides a more favorable MPER orientation. 4E10 nominal epitope also had higher helical content than the biepitope conjugate. Anchoring of the MPER peptides to the membrane via a hydrophobic anchor sequence was shown to be required for efficient 4E10 binding. Dennison2009 (antibody binding site, kinetics)
• 4E10: 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. 4E10 inhibited both chimeras to an extent similar to 4E10 inhibition of the wildtype derived HIV-2KR.X7 virus. Davis2009 (neutralization)
• 4E10: Neutralization profiles of cloned Envs derived from recent heterosexual infections by subtypes A, C, D, and A/D from Kenya were determined. 4E10 neutralized 7/31 variants from 4/14 subjects. Presence of mutations in the 4E10 epitope was common but did not predict neutralization sensitivity of the variants. Blish2009 (neutralization, acute/early infection)
• 4E10: Two MPER derived peptides (N-preTM and PreTM-C) containing the full 4E10 epitope were used to analyze lipid bilayer perturbation. Both peptides had comparable capacities in associating with, inserting into, and permeabilizing the membrane, however, N-preTM-induced permeabilization was specifically blocked by 4E10 while PreTM-C was not, indicating different accessibility of the 4E10 epitope on the two peptides. It was also shown that N-preTM induced graded release of vesicular contents while PreTM-C followed an all-or-none mechanism of permeabilization, supporting the existence of different MPER membrane-bound lytic structures. Apellaniz2009 (antibody binding site)
• 4E10: Three 4E10 mutants, with Ala substitutions in their CDR H3 loops, bound to gp41 with somewhat reduced affinity compared to wildtype, indicating that CD3 loop does not make major contribution to contact with gp41. However, the three 4E10 mutants did not bind, or bound weakly, to lipid bilayers, indicating that the hydrophobic residues of CDR H3 loop are necessary for 4E10 interaction with viral membrane. Two of the 4E10 mutants also failed to neutralize BG1168 and SF162 strains, both which are neutralized by wildtype 4E10. The third mutant neutralized the two viruses with lower potency compared to wildtype Ab. In addition, it was shown that gp41-inter effectively blocks neutralization of HIV-1 by 4E10. These results indicate a two-step mechanism of 4E10 binding and neutralization: 1) 4E10 attaches to the viral membrane through CDR H3 loops. 2) 4E10 binds to the MPER after gp41 has undergone conformational changes and assumes its prehairpin intermediate conformation. The results also indicate the importance of the HIV-1 membrane in binding and neutralization by 4E10 and that a lipid component may be required for an immunogen to induce 4E10-like Ab responses. Alam2009 (antibody binding site, neutralization, kinetics, binding affinity)
• 4E10: 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 three of the patients, virus variants were moderately sensitive to neutralization by 4E10, while in two of the patients, viruses from all time points had higher levels of resistance to 4E10 neutralization. In two patients, increasing number of virus variants were resistant to 4E10 neutralization during the course of infection. Mutations in the 4E10 epitope were found in all patients at all time points, but only one, at position 667, was suggested to play a role in the resistance to 4E10 neutralization. Bunnik2009 (neutralization, escape)
• 4E10: A buried surface area analysis of gp41 revealed that core epitope residues of 2F5 and 4E10 MAbs are more conserved than those of Z13, explaining the greater neutralization breadth of 2F5 and 4E10. Bryson2009 (structure)
• 4E10: The lipid binding properties of 4E10, and the similarity to binding properties of anti-PIP mAbs, are discussed. Potential role of liposomes containing lipid A for induction of NAbs to lipids of HIV-1 is reviewed. Alving2008 (autoantibody or autoimmunity, review)
• 4E10: 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 4E10, with 18 of 19 envelopes sensitive to neutralization by this Ab. Schweighardt2007 (assay or method development, neutralization)
• 4E10: 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 4E10 in different HIV-1 clades is provided. McKnight2007 (variant cross-reactivity)
• 4E10: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. 4E10 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 4E10, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed. Phogat2007 (review)
• 4E10: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including 4E10 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)
• 4E10: 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 4E10 Ab, indicating that the neutralization properties are not altered by the new method. Kirchherr2007 (assay or method development, neutralization)
• 4E10: 4E10 structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit anti-gp41 Abs, are reviewed in detail. The effect of the autoreactivity of 4E10 on vaccine antigen design is discussed. Lin2007 (vaccine antigen design, review, structure)
• 4E10: This review summarizes 4E10 Ab epitope, properties and neutralization activity. 4E10 use in passive immunization studies in primates and possible mechanisms explaining protection against infection are discussed. Also, 4E10 autoreactivity and its implications for active immunizations are discussed. Kramer2007 (immunotherapy, review)
• 4E10: 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 4E10 MAb are described. Willey2008 (review)
• 4E10: 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 4E10 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)
• 4E10: 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 4E10, but there was a modest heightened resistance of acute Envs compared to chronic Envs to neutralization by 4E10. Keele2008 (neutralization, acute/early infection)
• 4E10: 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 4E10 epitope fail to induce broadly neutralizing Abs are discussed. Haynes2008 (vaccine antigen design, review)
• 4E10: 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, 4E10 inhibited transmission of CCR5-tropic viruses while transmission of 4E10-neutralized X4 variants increased, indicating that X4 HIV-1 has an advantage over R5 in transmission when neutralized with 4E10. vanMontfort2008 (co-receptor, neutralization, dendritic cells)
• 4E10: The newly detected MAb m44 was shown to neutralize a panel of primary HIV-1 isolates with higher potency than 4E10, and the neutralization potency of the two mAbs was comparable for a subtype C SHIV strain. 4E10 did not compete with m44 for binding. A fusion protein of gp41 constructed for alanine-scanning mutagenesis bound to 4E10, indicating that its antigenic structure was intact. 4E10 bound to self antigens in lipid binding assays. Zhang2008 (neutralization, binding affinity)
• 4E10: MPER structure and interaction with 4E10 was studied by NMR, EPR and SPR techniques. The MPER region was shown to have an L-shaped structure, with the conserved C-terminal residues immersed in the membrane and the variable N-terminal residues exposed to the aqueous phase. 4E10 was shown to extract its epitope from the viral membrane in a multistep process: i) initial interaction of the Ab with N671 residue orients the peptide with the respect to Ab binding pocket, ii) the hydrophobic residues of the Ab induce rearrangement of multiple side chains of the peptide, with the F673 residue rotated into the Ab binding pocket, iii) insertion of F673 and W672 residues into the 4E10 binding pocket bends the N-terminal segment of the peptide in the opposite direction. The key requirement for neutralization is suggested to be induction of structural rearrangement of the MPER hinge by 4E10. It is also suggested that exposure of the membrane-embedded residues of the MPER region to the immune system in their native L-shaped form may elicit neutralizing Abs. Sun2008 (antibody binding site, structure)
• 4E10: Trimeric envelope glycoproteins with a partial deletion of the V2 loop derived from subtype B SF162 and subtype C TV1 were compared. 4E10 recognized both B and C trimers, indicating that the 4E10 epitope was 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)
• 4E10: 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 4E10, 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. The two escape mutant viruses were moderately more sensitive to the 4E10 neutralization than the parental isolates, which were resistant to neutralization by this Ab. There were no sequence-based explanations for the increased neutralization sensitivity of the escape viruses by 4E10. 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)
• 4E10: This minireview summarizes data on differences in neutralizing activities of MAbs and pooled human sera using a traditional primary cell neutralization assay and the more standardized TZM-bl reporter cell line assay. Also, suggestions are made on how to improve and standardize neutralization assays for comparable use in different laboratories. 4E10 neutralization was tested against a panel of 60 HIV-1 primary isolates (10 each from clades A-D, CRF01_AE and CRF02_AG) in the two assays. 17 viruses from the PBMC assay and 1 virus from the TZM-assay were not neutralized by this Ab. Only 52% of concordance between the two assays were shown for 4E10, and, as observed in other studies, 4E10 displayed much broader neutralization in the TZM-assay. It is suggested that the process of endocytosis in the TZM-assay alters exposure of the MPER region allowing 4E10 to neutralize more efficiently. In total, however, the assay discordances were shown to be bi-directional and not attributable to assay sensitivity. Polonis2008 (assay or method development, neutralization, review, subtype comparisons)
• 4E10: The sensitivity of R5 envelopes derived from several patients and several tissue sites, including brain tissue, lymph nodes, blood, and semen, was tested to a range of inhibitors and Abs targeting CD4, CCR5, and various sites on the HIV envelope. All but one envelope 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 no clear correlation between macrophage-tropism and neutralization sensitivity to 4E10, indicating that variation in macrophage tropism is not caused by variation in the membrane proximal region of Env. Peters2008a (neutralization)
• 4E10: For assessment of gp41 immunogenic properties, five soluble GST-fusion proteins encompassing C-terminal 30, 64, 100, 142, or 172 (full-length) amino acids of gp41 ectodomain were generated from M group consensus env sequence. Although all five protein fragments contained the same epitope recognized by 4E10, GST-gp41-30 and -100 fragments were about 20- and 5-fold less reactive to 4E10, respectively, compared to the other three protein fragments which had similar reactivity. Patients considered as slow progressors generally exhibited larger Ab reactivity against the 30aa fragment, indicating that these Abs target MPER region and exhibit 2F5- and 4E10-like properties. Plasma from these patients also exhibited broader and more potent neutralizing activity against several HIV-1 isolates. Plasma from 4 out of 44 patients reacted with peptides that bind 4E10, indicating that these patients mounted 4E10-like Ab response. Penn-Nicholson2008 (rate of progression)
• 4E10: 4E10 was shown to bind to Envs used in typical epitope binding assays, unlike the neutralizing Abs 8K8, DN9, and D5 used in this study. 4E10 neutralized all HIV-1 isolates tested, and its neutralization potency was 1 to 2 orders of magnitude higher than that one of mAbs 8K8 and D5. 4E10 displayed some cardiolipin binding activity. Nelson2008 (autoantibody or autoimmunity, neutralization, binding affinity)
• 4E10: The study compared the in-membrane recognition and blocking activity of the 2F5 and 4E10 MAbs, using solution-diffusing, unstressed phospholipid vesicles with sizes that approximate to that of the HIV virion, and an MPER-derived sequences that combines the full length 2F5 and 4E10 epitopes. 2F5 MAb had lower affinity for membrane-bound species than 4E10 MAb, as defined by inhibition data together with direct electron microscopy and flow cytometry determination of the vesicle-antibody association. Huarte2008a (antibody binding site)
• 4E10: 4E10 reacted with maltose-binding proteins MBP30 and MBP32, containing both HR1 and HR2 domains of gp41, and with MBP37 and MBP44, containing only the HR2 domain, but not with MBP-HR1, containing only the HR1 domain. Vincent2008 (antibody binding site)
• 4E10: Neutralization susceptibility of CRF01_AE Env-recombinant viruses, derived from blood samples of Thai HIV-1 infected patients in 2006, was tested to 4E10. Most CRF01_AE viruses showed high susceptibility to 4E10, including viruses with and without conserved 4E10 epitopes, suggesting that the susceptibility of CRF01_AE to 4E10 is not determined by the conservation of the core epitope sequence. Several X4R5 viruses were less susceptible to 4E10 compared with X4 or R5 viruses. There was no correlation observed between virus neutralization susceptibility to 4E10 and viral infectivity, the length of the gp120 variable regions, or the number of PNLG sites. Utachee2009 (co-receptor, neutralization, subtype comparisons)
• 4E10: CTB-MPR649-684 (cholera toxin subunit B and residues 649-684 of gp41 MPER region) peptide was developed for vaccine studies in rabbits. 4E10 affinity to the CTB-MPR peptide was equivalent to 4E10 affinity toward an MPR peptide, indicating that the fusion peptide presented antigenically competent MPR. Sera from immunized rabbits displayed no neutralizing activity, but could inhibit epithelial transcytosis of virus, indicating elicitation of non-neutralizing Abs capable of stopping mucosal transmission and infection of target cells. Matoba2008 (binding affinity)
• 4E10: A MPER peptide, AISpreTM, overlapping 2F5 and 4E10 epitope sequences, was capable of breaching the permeability barrier of lipid vesicles. 4E10 blocked the peptide bilayer-destabilizing activity, however, inclusion of sphingomyelin raft-lipids into the membrane bilayer reduced significantly the affinity of 4E10 for AISpreTM. In contrast, inclusion of cholesterol induced higher 4E10 affinity for the AISpreTM peptide. AISpreTM appears to insert less deeply into the lipid bilayer in the presence of cholesterol, which might increase 4E10 epitope accessibility for Ab binding. Thus, 4E10 epitope accessibility is affected by envelope lipid composition. Huarte2008 (antibody binding site)
• 4E10: Comparing specific signals of selection among gp41 sequences from different HIV-1 M subtypes and circulating recombinant forms revealed presence of 12 sites evolving under positive selection across multiple major HIV-1 lineages. Nine sites detected to be under positive selection in the external exposed domains of gp41 had a significant tendency to be located within neutralizing and other Ab epitopes. Comparison of two matched datasets of HIV-1 subtype C, sampled from patients with acute or chronic infections, showed 6 gp41 sites evolving under different selection pressures during acute and chronic infection. One of those sites was within the epitope of 4E10, which evolved under strong positive selection in the chronically infected patients, but under neutral or mildly negative selection in the acutely infected patients. Bandawe2008 (mutation acquisition, acute/early infection, escape)
• 4E10: 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. 4E10 neutralized all 27 Env-pseudotyped viruses. Chong2008 (neutralization, subtype comparisons)
• 4E10: 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 4E10 did not appear during the first 40 days after plasma virus detection. Tomaras2008 (acute/early infection)
• 4E10: The neutralization profile of early R5, intermediate R5X4, and late X4 viruses from a rhesus macaque infected with SHIV-SF162P3N was assessed. 4E10 moderately neutralized the late X4 and the intermediate R5X4 viruses, but did not neutralize the parental R5. Tasca2008 (co-receptor, neutralization)
• 4E10: pIg-tail expression system was used to construct a panel of cell-surface expression plasmids encoding the extracellular domain of gp41 with deletion of fusion peptide (FP), and/or introduction of L568P mutation. Deletion of FP resulted in significantly increased antigenicity of 4E10 epitope, indicating that FP and MPER may interact with each other, resulting in obstruction of the 4E10 epitope in MPER. L568P mutation resulted in significant enhancement of 4E10 binding to its epitope, suggesting that the mutation may destabilize the gp41 6-HB core conformation exposing the 4E10 epitope. Mice were immunized with DNA plasmids of FP-deleted and L568P mutant gp41, and with peptide containing the 4E10 epitope. Deletion of FP did not enhance the immunogenicity of the 4E10 epitope, however, the L568P mutation resulted in increased Ab response against 4E10 epitope compared to the response by peptide alone. Li2008a (antibody binding site, vaccine antigen design, binding affinity)
• 4E10: The IC50 for 4E10 in a standard neutralization assay is 6.3 nM but is increased 10-fold in the postattachment neutralization assay to 59 nM. The neutralization half-life for 4E10 is 15.9 minutes but is increased 4-fold to 57.9 minutes in the presence of N36Mut(e,g), peptide, which is a class 3 inhibitor that prolongates temporal window of neutralization by disrupting trimerization of the N-heptad repeat (N-HR) in the prehairpin intermediate by sequestering the N-HR into N-HR/N36Mut(e,g) heterodimers. HXB2 was neutralized synergistically by 4E10 and N36Mut(e,g), where the formation of N-HR/N36Mut(e,g) heterodimers enhances the probability of 4E10 binding and the binding of 4E10 enhances the probability of N-HR/N36Mut(e,g) heterodimer formation, greatly diminishing the probability of 6-helix bundle formation. HXB2 was also synergistically neutralized by 4E10 and sCD4. Gustchina2008 (antibody binding site, neutralization, kinetics)
• 4E10: 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. 4E10 did not inhibit binding of the three neutralizing VHH Abs to gp120. Forsman2008 (antibody interactions)
• 4E10: 3 viral quasispecies from an HIV-1 C-subtype infected child had different sensitivities to neutralization by 4E10, conferred by a rare mutation, F673L in the 4E10 epitope. Moderate changes in sensitivity were modulated by secondary positions in this epitope and motifs in the cytoplasmic tail. Gray2008 (neutralization, escape)
• 4E10: NMR structure of P1, a minimal MPER region that permits interaction with the mucosal galactosyl ceramide HIV-receptor, was analyzed in interaction with 4E10 at different pH. The best fit between NMR P1 and crystal structures of the Ab was at pH 6 and 5. The binding of 4E10 to P1 inserted into the liposomes of different compositions mimicking various biological membranes revealed 5- to 10-fold higher affinity of 4E10 to P1 in the lipid environment compared to aqueous environment, suggesting that specific lipid environment stabilizes the appropriate structure of the HIV-1 peptide. Coutant2008 (antibody binding site, kinetics, binding affinity, structure)
• 4E10: 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. Three different assays were used to analyze gp41-directed neutralizing activity. MAb 4E10 was shown to neutralize equivalently in the standard and post-CD4/CCR5 assay. Weak post-CD4/CCR5 neutralization was detected in five subtype B and two subtype C plasmas. 4E10 was shown to neutralize several of the MPER-engrafted mutant viruses, but the subtype B plasmas did not exactly recapitulate this activity except in one case, where the activity of the plasma against two mutants suggested presence of 4E10-like Abs. Neutralization of four subtype B plasmas was substantially inhibited by a 4E10 peptide, suggesting presence of 4E10-like Abs. Binley2008 (neutralization, subtype comparisons)
• 4E10: V3 loop deletions were introduced into three different primary HIV-1 strains: R3A, DH12, and TYBE. The deletions included: ΔV3(12,12) containing the first and the last 12 residues of the V3 loop, ΔV3(9,9) containing first and last 9 residues, and ΔV3(6,6) containing first and last 6 residues. Only HIV-1 R3A ΔV3(9,9) was able to support cell fusion. Passaging of this virus resulted in a virus strain (TA1) that replicated with wildtype kinetics, and that acquired several adaptive changes in gp120 and gp41 while retaining the V3 loop truncation. 4E10 exhibited modestly enhanced neutralization activity against TA1 and a ΔV1/V2 virus, while it failed to neutralize R3A. Laakso2007 (neutralization)
• 4E10: The ability of 4E10 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 moderately to completely resistant to neutralization by 4E10, although viruses isolated later in the course of infection showed increased sensitivity to 4E10 in one of the patients. In the parenteral transmission, one of the recipients had early viruses resistant to 4E10 neutralization, and one had viruses sensitive to 4E10 neutralization. The neutralization sensitivity patterns of recipient viruses to 4E10 did not correlate to the neutralization sensitivity patterns of their donors in the homosexual couples, while the HIV-1 variants from the parenteral pairs were similarly resistant/sensitive to neutralization by 4E10. Resistance to 4E10 did not correlate with sequence variation within the 4E10 epitope. Quakkelaar2007a (neutralization, acute/early infection, mother-to-infant transmission)
• 4E10: Four different co-receptor switch mutants were generated from ADA and BaL wildtype Envs (ADA-1, ADA-3, BaL-1B, and BaL2A) and the intermediate transition mutations were studied on either CCR5 or CXCR4 expressing cells for their sensitivity to 4E10 compared to wildtype. Most of the ADA-1 and ADA-3 mutants were more sensitive to 4E10 than the wildtype on both CCR5 and CXCR4 cells. BaL-1B mutants were highly sensitive to entry inhibition by 4E10 on CCR5 cells, which further increased on CXCR4 cells. BaL-2A mutants varied in their sensitivity to 4E10 inhibition, where only the final BaL-2A mutant, with all four mutations, was significantly more sensitive to 4E10 than the wildtype virus. Pastore2007 (co-receptor, neutralization)
• 4E10: 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. Antiviral activity of 4E10 was not clearly demonstrated. Development of resistance to 4E10 was not observed despite ongoing viral replication. Plasma HIV-1 RNA levels did not increase following cessation of Ab infusion. Plasma viremia was essentially identical between patients not receiving MAb therapy and patients receiving 4E10 and 2F5 in the face of 2G12 resistance. 4E10 also failed to accumulate with repeated infusions in patient plasma. Long-term suppression of viremia was achieved in 3/10 patients. Mehandru2007 (escape, immunotherapy, supervised treatment interruptions (STI))
• 4E10: 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 4E10 binding to wild type and mutant JR-FL, and 4E10 inhibited infection of the two pseudoviruses with comparable potencies. Dey2008 (binding affinity)
• 4E10: This study explored features of Env that would enhance exposure of conserved HIV-1 epitopes. The changes in neutralization susceptibility, mediated by two mutations, T569A (in the HR1) and I675V (in the MPER), were unparalleled in their magnitude and breadth on diverse HIV-1 Env proteins. The variant with both TA and IV mutations was >360-fold more susceptible to 2F5, 2.8-fold more susceptible to b12, >780-fold more susceptible to sCD4 and resulted in 18-fold enhanced susceptibility to autologous plasma and >35-fold enhanced susceptibility to the plasma pool. It was also >180-fold more susceptible to 4E10. Mutants with only one IV mutation was >24-fold more susceptible to 4E10. Blish2008 (antibody binding site, enhancing activity)
• 4E10: Molecular mechanism of neutralization by MPER antibodies, 2F5 and 4E10, was studied. Preparations of trimeric HIV-1 Env protein in the prefusion, the prehairpin intermediate and postfusion conformations were used. The epitopes for 2F5 and 4E10 were found to be exposed only on a form designed to mimic an prehairpin intermediate state during viral entry, which helps to explain the rarity of 2F5- and 2E10-like antibody responses. Frey2008 (antibody binding site, binding affinity)
• 4E10: Addition of a glycosylation site at position V295N in two different subtype C envelope clones resulted in a twofold increase in neutralization sensitivity of the corresponding viruses to 4E10. Gray2007a (neutralization)
• 4E10: 4E10 peptide SLWNWFNITNWLWYIK was used in MAbs 5A9 and 13H11 characterization. 4E10 showed strong binding to HIV-1 infected cells Alam2008 (antibody interactions)
• 4E10: The potency of 4E10 was 25-fold higher than the potency of new neutralizing Fab 3674 in neutralization of laboratory and primary strains of HIV-1 subtypes A, B and C. Gustchina2007 (neutralization, subtype comparisons)
• 4E10: 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 4E10 and other MAbs. Antibodies induced by immunization with these centralized proteins did not, however, have the breadth and potency compared to that of 4E10 and other broadly neutralizing MAbs. 4E10 physical characteristics of autoantibodies as a possible reason for lack of 4E10 broad production is also discussed. Gao2007 (antibody binding site, neutralization, review)
• 4E10: Neutralizing activity of 4E10 against a panel of HIV-1 primary isolates from different clades was assessed in a PBMC-assay. The neutralizing activity was shown to be less potent than that of the newly characterized m48 MAb. Zhang2006a (neutralization, variant cross-reactivity, subtype comparisons)
• 4E10: The epitope recognition sequence for this Ab was introduced into the corresponding region of SIVmac239 and the replication of this viral variant (SIVmac239/4E10) was similar to the parental virus. SIVmac239/4E10 was specifically neutralized by MAb 4E10. SIVmac239/4E10 was neutralized by a LTNP plasma and somewhat with three other plasmas but addition of a 4E10 Ab inhibitor did not block the neutralization suggesting that 4E10 specificity represent only small fraction of neutralizing activity in plasma. Yuste2006 (neutralization, SIV)
• 4E10: Significant levels of 4E10 were shown to bind to HA/gp41 expressed on cell surfaces and this Ab did stain cells expressing HA/gp41 in a fluorescence assay. However, a much smaller percentage of the HIV 89.6 Env expressing cells were stained with this Ab than with 2G12, indicating that this Ab recognition site on gp41 is masked by the gp120 subunit in the HIV Env protein and that it is more easily accessible on the HA/gp41 chimeric protein. Ye2006 (antibody binding site, binding affinity)
• 4E10: SHIV SF162p4 virus used as challenge in ISCOM vaccinated macaques was shown to be highly sensitive to neutralization by this Ab. Pahar2006 (neutralization)
• E10: All subtype C env-pseudotyped clones derived from individuals in acute/early stage of HIV-1 infection were neutralized by this Ab. One clone had a slightly different motif (WFNM) than the reported required WFXI in the epitope, yet it was highly susceptible to neutralization by 4E10, indicating additional flexibility in the 4E10 core epitope. Li2006a (neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
• 4E10: This Ab is shown to have the capacity to penetrate into the membrane interfaces and recognize isolated peptide-epitope sequence embedded into the membrane, where immersion into the lipid bilayer does not interfere with 4E10 recognition ability. The association of 4E10 with membranes is shown to be nonspecific. Sanchez-Martinez2006 (antibody binding site)
• E10: Binding of this Ab to pre-TM sequence was shown not to be affected by presence of FP (fusion peptide) sequence. Lorizate2006a (antibody binding site, binding affinity)
• 4E10: This study showed that 4E10 Ab is able to specifically block the membrane-restructuring activity by recognizing preTM peptides inserted into the viral external membrane monolayer in the gp41 pre-fusion state. The recognition and blocking occurs in the presence of cholesterol and correlates with pore-formation blocking, suggesting interference of the formation of fusion-competent complexes. Lorizate2006 (antibody binding site)
• 4E10: This MAb was used as a positive control in the neutralization assays. It neutralized two of three subtype B and 4 of 6 non-B primary isolates. Gorny2006 (neutralization, variant cross-reactivity, subtype comparisons)
• 4E10: 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)
• 4E10: 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 resistant to neutralization by 4E10. The gp41 sequence was the same in all pseudoviruses, indicating that changes in gp120 can mediate sensitivity of gp41 to neutralization. Blay2007 (neutralization)
• 4E10: 4E10 was shown to recognize liposomes containing phosphatidylinositol-4-phosphate (PIP) to the same extent that it recognized anionic liposomes lacking PIP. Binding of 4E10 to pure PIP was inhibited by Ca2+. Once bound to PIP, 4E10 could not be stripped off by addition of Ca2+, indicating an irreversible bond of 4E10 to PIP phospholipid fatty acids. Beck2007 (antibody binding site)
• 4E10: To test the immunogenicity of three molecularly engineered gp41 variants on the cell surface their reactivity with 4E10 was assessed. The reactivity of 4cSSL24 variant was comparable to gp160 while the other two variants showed somewhat lower expression levels. When guinea pigs were immunized with the three variants, the level of the specific anti-gp41 Ab responses was low with the anti-gp41 response preferentially directed to the C-helical domain, away from the MPER region. Kim2007 (vaccine antigen design, binding affinity)
• 4E10: (R5)X4 viruses from early and late timepoints after X4 emergence were found to be more sensitive to neutralization by 4E10 than their coexisting R5 variants in one patient. Only early (R5)X4 viruses were more sensitive to neutralization by 4E10 in another patient. Bunnik2007 (co-receptor, neutralization)
• 4E10: 4E10-neutralized HIV-1 captured on Raji-DC-SIGN cells or immature monocyte-derived DCs (iMDDCs) was transferred to CD4+ T lymphocytes with 1.5 fold higher efficiency than non-neutralized virus. vanMontfort2007 (enhancing activity, neutralization, dendritic cells)
• 4E10: 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, 4E10 exhibited dose-dependent reactivity with cardiolipin and phosphatidylserine, and low binding to β2GP1 and prothrombin. 4E10 induced prolongations of clotting times in human plasma, but those were mild and did not exceed grade I toxicities. Vcelar2007 (antibody interactions, autoantibody or autoimmunity, binding affinity, immunotherapy)
• 4E10: The structure of the 4E10 MAb, particularly its CDRH3 region's binding mechanisms to the MPER region of gp41, and possibly the cellular membrane as well, are reviewed. Engineering of Abs based on revealed structures of broadly neutralizing MAbs is discussed. Burton2005 (antibody binding site, review, structure)
• 4E10: 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)
• 4E10: A trimeric gp41 construct comprising the env transmembrane domain and the extracellular C-terminal region (gp41ctm) was incorporated into liposomes. 4E10 bound to the liposome-incorporated gp41ctm, indicating that its extracellular region is accessible to this Ab. Sera from mice immunized with either gp41ctm alone or with gp41ctm-liposome did not show any significant neutralization activity, indicating that the construct might not properly expose its 4E10 epitope. Lenz2005 (antibody binding site, neutralization)
• 4E10: 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. All 19 pseudotyped viruses were highly sensitive to neutralization by 4E10 as were the MN, SF162.LS and IIIB strains. All 12 Env-pseudotyped viruses were more sensitive to neutralization by 4E10 than their uncloned parental PBMC-grown viruses. Li2005a (assay or method development, neutralization)
• 4E10: 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 4E10 were similar, while a significant decrease in viral neutralization sensitivity to 4E10 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)
• 4E10: A short review of studies on 4E10 interaction with autoantigens, epitope accessibility, structure, and neutralizing capability. The reasons why 4E10 appears infrequently in nature are discussed. Nabel2005 (antibody binding site, neutralization, immunotherapy, review)
• 4E10: 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)
• 4E10: Escape mutations in HR1 of gp41 that confer resistance to Enfuvirtide reduced infection and fusion efficiency and also delayed fusion kinetics of HIV-1. The mutations also conferred increased neutralization sensitivity of virus to 4E10. Enhanced neutralization correlated with reduced fusion kinetics, indicating that the mutations result in Env proteins remaining in the CD4-triggered state for a longer period of time. Reeves2005 (antibody binding site, drug resistance, neutralization, escape, HAART, ART)
• 4E10: More that 90% of viruses from both acutely and chronically infected HIV-1 patients were inhibited by this Ab, however, viruses from acute patients were significantly more sensitive to 4E10 than viruses from chronic patients. The epitope of this Ab was highly conserved among all isolates tested suggesting that the higher susceptibility of acute viruses may be due to better epitope accessibility. The sensitivity of viruses to 4E10 was also highly correlated to their sensitivities to 2F5. Rusert2005 (antibody binding site, antibody interactions, neutralization, acute/early infection)
• 4E10: 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, immunotherapy, review, structure)
• 4E10: 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 while no escape was observed for 4E10 and 2F5. 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. No such differences were observed for 2F5 or 4E10, suggesting that high levels of NAbs are required for inhibition in vivo, and that the in vivo concentrations of 4E10 and 2F5 might have been too low to control viremia and exert a selective pressure. Trkola2005 (acute/early infection, escape, immunotherapy, HAART, ART, supervised treatment interruptions (STI))
• 4E10: 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, variant cross-reactivity, immunotherapy)
• 4E10: 4E10 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. Neutralization by 4E10 in the standard format was undetectable, which changed to modest with the gp41 tail truncation and/or addition of a disulfide bridge linking gp120 and gp41. 4E10 was also able to neutralize in post-CD4 and post-CD4/CCR5 formats, suggesting that it binds Env trimers at various stages of infection. None of the analyzed HIV-1+ human plasmas neutralized in the post-CD4/CCR5 format indicating absence of 2F5 and 4E10 - like Abs. Crooks2005 (antibody binding site, assay or method development, neutralization)
• 4E10: 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, antibody polyreactivity)
• 4E10: This review summarizes data on 447-52D and 2219 crystallographic structures when bound to V3 peptides and their corresponding neutralization capabilities. 4E10, like 447-52D and like other HIV-1 neutralizing Abs, was shown to have long CDR H3 loop, which is suggested to help Abs access recessed binding sites on the virus. Stanfield2005 (antibody binding site, review, structure)
• 4E10: 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). 4E10 was recognized less efficiently on the V2- and V3- deleted proteins than on SF162gp140. 4E10 was found to equally neutralize SF162 and Δ2F5.4E10, which is a virus with mutations in the 2F5 and 4E10 epitopes and is resistant to neutralization by 2F5 and 4E10. This indicates that 4E10-like Abs were not present in sera from the gp140-immunized animals nor in the SHIV-infected and in the HIVIG sera. Derby2006 (antibody binding site, neutralization)
• 4E10: Sera from rabbits immunized with either monomeric gp120, trimeric cleavage-defective gp140 or disulfide-stabilized soluble trimeric gp140 were tested for neutralization of chimeric SIVmac239 viruses expressing epitope for this Ab. Little or no neutralization was observed indicating that little or no Ab activity in these rabbit sera was directed against the gp41 region. Beddows2007 (neutralization, vaccine antigen design)
• 4E10: Env-pseudotyped viruses were constructed from the gp160 envelope genes from seven children infected with subtype C HIV-1. 4E10 alone or in combination with IgG1b12, 2G12 and 2F5 neutralized all of the seven viruses. Gray2006 (neutralization, variant cross-reactivity, responses in children, mother-to-infant transmission)
• 4E10: Pharmacokinetic properties of this Ab were studied in HIV infected patients infused with high doses of 4E10. 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 5.5 days. Joos2006 (kinetics, immunotherapy)
• 4E10: The majority of broadly cross-reactive neutralizing (BCN) Envs were neutralized at lower concentrations of 4E10 than the non-BCN Envs. Amino acid variability of the 4E10 epitope was examined. The presence of T at position 662 was associated with increased sensitivity to neutralization by this Ab. Cham2006 (neutralization, variant cross-reactivity, escape, subtype comparisons)
• 4E10: Neutralization of HIV-1 primary isolates of different HIV-1 clades (A, B, C, D, E) by 4E10 was determined in cells expressing high or low surface concentrations of CD4 and CCR5 receptors. CD4 cell surface concentration had no effect on the inhibitory activity of this Ab while the CCR5 surface concentration had a significant effect decreasing the 50% inhibitory concentration of 4E10 in cell lines with low CCR5. Choudhry2006 (co-receptor, neutralization, variant cross-reactivity, subtype comparisons)
• 4E10: Genetic variability and co-variation of the MAb 2F5, 4E10 and Z13 epitopes in B and non B clades was investigated. A significant shift in the predominant sequence patterns over time was observed for all three epitopes. Also, significant inter-subtype genetic variability of the three epitopes was detected. However, the 4E10 epitope displayed a more similar variability within B clade and non-B clades, concurring with the cross-clade neutralizing activity of this MAb. Epitope co-variation was also noted, as one third of the recently isolated HIV-1 strains displayed simultaneous epitope variants. Dong2006 (antibody binding site, subtype comparisons)
• 4E10: 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)
• 4E10: The antigenic determinants recognized by 4E10 were characterized using recombinant glycosylated full-length Ags, and nonglycosylated and truncated Ags. This Ab recognized three peptides located at the N-terminal region of gp120 and gp41, respectively. It is suggested that 4E10 binds to the fusogenic peptide of gp41 and the N-terminal region of gp120, inhibiting insertion of fusogenic peptide into the host cell membrane. Hager-Braun2006 (antibody binding site, variant cross-reactivity, binding affinity)
• 4E10: The optimal length of the 4E10 epitope was determined to the gp41 residues 671 to 683. Several residues in the epitope were shown to be essential for 4E10 recognition (W672, F673 and T676) and five more were shown to make significant contributions to 4E10 binding (N671, D674, I675, W680 and L679). When helix-promoting residues and helix-inducing tethers were incorporated, several peptides showed improved affinity over the starting peptide suggesting that they may be more likely to elicit 4E10-like neutralizing Abs. Brunel2006 (kinetics, binding affinity, structure)
• 4E10: Inhibition of R5 HIV replication by monoclonal and polyclonal IgGs and IgAs in iMDDCs was evaluated. The HIV-neutralizing activity of 4E10 was observed to be higher in iMDDCs than in PHA-stimulated PBMCs using both HIV-1 Bx08 and BaL. Holl2006a (neutralization, dendritic cells)
• 4E10: This study found that, contrary to expectations, the viruses resistant to b12, 4E10, 2G12 and 2F5 neutralization did not have lower replication kinetics than viruses sensitive to neutralization. Viruses from early infection tended to have relatively low replications rates. Quakkelaar2007 (neutralization, viral fitness and reversion, escape)
• 4E10: 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, but was still less potent than 4E10 at neutralizing several pseudotyped Envs. 4E10 was found to be less effective inhibitor of biotinylated Z13e1 than the other way around. Neutralization assays of HIV-1 JR2 MPER alanine mutants showed that mutants W666A and W672A were completely resistant to neutralization by 4E10. In contrast to a previous publication, it was also found that neutralization of HIV-1 JR-FL by 4E10 was not greatly improved in going from the Fab to IgG format. Nelson2007 (antibody binding site)
• 4E10: High levels of gp120-specific Abs were elicited when mice and rabbits were immunized by DNA priming and protein boosting with G1 and G2 grafts, consisting of 2F5 and 4E10, and 4E10 epitopes, respectively, engrafted into the V1/V2 region of gp120. A consistent NAb response against the homologous JR-FL virus was detected in rabbits but not in mice. 4E10 bound to the engrafted construct, but embedding the MPER epitopes in the immunogenic V1/V2 region did not result in eliciting anti-MPER antibodies in mice or rabbits. 4E10 binding to G2 was greater than to G1, and could be enhanced by deletion of one or two amino acid residues immediately preceding the 4E10 epitope, presumably due to rotation of the epitope along the alpha-helix in the engrafted region. Law2007 (vaccine antigen design)
• 4E10: 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, escape, review, subtype comparisons, structure)
• 4E10: This review summarizes current knowledge of HIV-1 lipid-protein interactions and antibodies to liposomal phospholipids and cholesterol. A potential use of Abs to lipids to neutralize HIV-1 and a potential role of the broadly neutralizing HIV-1 Abs, mainly 2F5 and 4E10, in binding to phospholipids is discussed. Alving2006 (antibody binding site, neutralization, review)
• 4E10: 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. 4E10 was shown to bind specifically to CON6, CON-S and subtype B recombinant proteins but not to subtype A and C recombinant proteins or to the two subtype B gp120 proteins. The specific binding of 4E10 to CON-S indicated that its conformational epitope was intact. Liao2006 (antibody binding site, vaccine antigen design, subtype comparisons)
• 4E10: Kinetics experiments of 4E10 binding to MPER region during viral fusion showed that the 4E10 kinetics resembled those of the six-helix bundle formation and fusion blocker C34, indicating that the function of MPER in the fusion cascade is still in effect at a late stage in the fusion reaction. Binding of 4E10 was shown to decrease upon triggering HIV-1 Env-expressing cells with appropriate target cells and addition of C34 did not counteract this loss, suggesting that changes in exposure of MPER occur independently of the six-helix bundle formation. Dimitrov2007 (antibody binding site, neutralization, kinetics, binding affinity)
• 4E10: Chimeric SIV viruses containing 2F5 and 4E10 epitopes were not neutralized by the broadly neutralizing sera from two clade B and one clade A infected asymptomatic individuals, indicating that MPER NAb epitopes did not account for the broad neutralizing activity observed. Dhillon2007 (antibody binding site, neutralization)
• 4E10: 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 (vaccine antigen design)
• 4E10: 2F5, 4E10, and m46 neutralization was more potent when tested in a HeLa cell line expressing low CCR5 than in a HeLa cell line expressing high CCR5 levels. PBMC tend to have low CCR5 expression. Choudhry2007 (assay or method development, neutralization)
• 4E10: Structural effects of both increasing peptide length and introducing helix-promoting constraints in the 4E10 epitope were investigated. Helical constraints increased binding affinity of the peptide epitope for 4E10 by increasing the stability of the complex and allowing interaction with an additional helical turn including Leu679 and Trp680. Crystal structures of the 4E10 bound to peptide epitopes revealed that the gp140 residues Trp672, Phe673, Ile675, Thr676 Leu679 and Trp680 have the most significant contact with the antibody, and the core motif was redefined as: WFX(I/L)(T/S)XX(L/I)W. Cardoso2007 (antibody binding site, vaccine antigen design, structure)
• 4E10: 7/15 and 9/15 subtype A HIV-1 envelopes from samples taken early in infection were neutralized by MAbs 4E10 and 2F5, respectively, and the potency was generally modest. Mutational patterns in the MAb binding sites did not readily explain the observed patterns of sensitivity and resistance. Blish2007 (neutralization, variant cross-reactivity, acute/early infection, subtype comparisons)
• 4E10: The autoantibody nature of the two membrane proximal HIV-1 neutralizing antibodies, 2F5 and 4E10, was evaluated by comparison to human anti-cardiolipin mAbs derived from a primary antiphospholipid syndrome patient. Both 2F5 and 4E10 bound specifically to cardiolipin. CDR3 sequence similarities between 2F5, 4E10 and anti-cardiolipin mAbs were observed. A difference in the binding mode of both 2F5 and 4E10 when binding to peptide in solution versus peptide conjugated to lipids was observed, in that binding to the peptide-lipid conjugate was best fit by a two step conformational change model. These results suggest that these antibodies share binding and structural similarities with human autoantibodies and their induction by vaccines or natural infection therefore might be limited by immune tolerance mechanisms. Alam2007 (kinetics, antibody sequence)
• 4E10: 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 varied between completely resistant or somewhat sensitive to neutralization by membrane proximal Nabs 4E10 and 2F5. The most sensitive Con B construct was the truncated version of Con B Env with a stop codon immediately following the membrane spanning domain, suggesting that truncation of the gp41 cytoplasmic domain facilitates greater accessibility of the MPER region. The Con B gp160 was quite resistant, and the gp160-201N/S more sensitive, to 4E10 and 2F5. Kothe2007 (vaccine antigen design, variant cross-reactivity)
• 4E10: 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)
• 4E10: This study confirmed binding of 4E10 to cardiolipin (CL) and showed that this Ab also binds to phosphatidylinositol phosphate (PIP). Binding of 4E10 to CL and PIP was inhibited by phosphocholine and enhanced by inositol (PIP only). Anti-PIP mouse monoclonal antibodies had neutralizing antibodies against 2 HIV primary isolates. Brown2007 (mimics, neutralization, binding affinity)
• 4E10: Alanine scanning mutations of the 21 amino acid region between positions 660-680 showed only 3 substitutions that reduced 4E10 binding, positions lleldkwanlwnWFdisnwlW. No single Ala mutation was resistant to both 2F4 and 4E10. Ala substitutions in 11/20 positions enhanced neutralization sensitivity, LLeLdkWanLWNwfdIsNWLw. For peptides T20 and 4E10 neutralization was synergistic. Zwick2005 (antibody binding site, escape)
• 4E10: 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. No viruses escaped 4E10, but only one virus in one patient had the NWFDIT epitope sequence; the W, F and I were conserved in all patients but the other amino acids varied both before and after treatment. A patient carrying the epitope sequence nwfSit had the least 4E10 sensitive virus. 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 the core of the 4E10 epitope, NWFDIT, 5/11 cases had a T->I escape; 2/11 had a F->L change; and 2/11 had substantial deletions, of WNWF overlapping, or NWLWYI adjacent to the epitope. 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)
• 4E10: 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)
• 4E10: gp41 and p15E of the porcine endogenous retrovirus (PERV) share structural and functional similarities, and epitopes in the membrane proximal region of p15E are able to elicit NAbs upon immunization with soluble p15E. Rabbits immunized with a VSV recombinant expressing an HIV-1 membrane-proximal external region (MPER) fused to PERV p15E, with a fusion p15E-HIV MPER protein boost, elicited HIV specific NAbs. The MPER contains the 4E10 epitope. Luo2006 (vaccine antigen design)
• 4E10: 2F5 and 4E10 both bind to membrane proximal regions of gp41, and have long hydrophobic CDR3 regions characteristic of polyspecific autoreactive antibodies. Of 35 Env-specific MAbs tested, only 2F5 and 4E10 were found to be reactive with phospholipid cardiolipin. Vaccine induction of antibodies that react with these gp41 membrane proximal regions may be rare because of elimination due to autoantigen mimicry. 4E10 also reacted with systemic lupus erythematosis (SLE) autoantigen SS-A/Ro, and both 4E10 and 2F5 reacted with HEp-2 cells with diffuse cytoplasmic and nuclear patterns indicating polyspecific autoreactivity. Haynes2005 (antibody binding site)
• 4E10: The crystal structure of 4E10 complexed with a 13 aa peptide (KGWNWFDITNWGK) that contains the NWFDIT binding site was resolved to 2.2 A resolution. 4E10 has a canonical beta sandwich Ig-fold, with H3/H2 loop hydrophobicity and a long CDR H3 loop that mediates C-terminal base and central amino acid interactions; it extends beyond the peptide and its orientation suggests it could potentially allow hydrophobic contacts with the viral membrane. 4E10 complex formation induces a conformational change in the peptide such that it forms an amphipathic alpha-helix with a hydrophobic face that interacts with 4E10, with Trp672 primary, and Phe673, Ile675 and Thr676 secondary, contact points. Cardoso2005 (structure)
• 4E10: Nabs against HIV-1 M group isolates were tested for their ability to neutralize 6 randomly selected HIV-1 O group strains. IgG1b12 could neutralize some O group strains when used on its own, and quadruple combination of b12, 2F5, 2G12, and 4E10, could neutralize the six Group O viruses tested between 62-97%. The linear epitope, NWFDIT, of 4E10 is conserved in 3/6 group O strains. Ferrantelli2004a (variant cross-reactivity)
• 4E10; 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 antibodies may be protective against mother-to-infant transmission of HIV. Ferrantelli2004 (mother-to-infant transmission)
• 4E10: 93 viruses from different clades were tested for their neutralization cross-reactivity using a panel of HIV antibodies. 4E10 was the most cross-reactive, moderately reactive in all 93 viruses tested from each subtype. WFXI was defined as the core motif, and this core is highly conserved in all M group gp41 sequences. How potent the neutralizing activity is somewhat context dependent. Binley2004 (variant cross-reactivity, subtype comparisons)
• 4E10: 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) can confer partial or complete protection to infant macaques from subsequent oral SHIV challenge. Safrit2004 (immunoprophylaxis, mother-to-infant transmission)
• 4E10: 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 4E10 was greater than 50 for CCcon19, and was 44 for CC1/85, so the primary virus was weakly neutralized by 4E10. Pugach2004 (variant cross-reactivity, viral fitness and reversion)
• 4E10: An antigen panel representing different regions of gp41 was generated, and sera from 23 individuals were screened. Anti-gp41 titers were very high, and sera bound to many regions of gp41, there were no immunologically silent regions. Many individuals had broad responses to diverse regions. High titer responses tended to focus on the N-heptad, C-heptad and 2F5-4E10 regions, but there was no correlation between neutralization capacity of sera and the particular peptides recognized. 4E10 responded to the three antigens that carried the minimal NWFNIT epitope, but was conformation and context sensitive. Opalka2004 (assay or method development)
• 4E10: This paper reviews MAbs that bind to HIV-1 Env. 4E10 binds to a region of gp41 proximal to cluster II (aa 662-676), neighboring the binding site of the broadly neutralizing MAb 2F5 and overlapping the epitope of neutralizing Fab Z13. 4E10 is the most broadly neutralizing MAb, neutralizing primary isolates from clades A, B, C, D, and CRF01 (E), although not the most potent. Gorny2003 (antibody binding site, variant cross-reactivity, subtype comparisons)
• 4E10: 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)
• 4E10: 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. Wang2003 (vaccine antigen design, review)
• 4E10: Porcine endogenous retroviruses (PERVS) are a concern in the context of porcine xenotransplantation into humans; possible strategies for protection include PERV knockout animals or vaccines. Goats immunized with the PERV transmembrane protein revealed two NAb epitope, E1 and E2. E2's epitope (FEGWFN) binds to a sequence that is perfectly preserved in all PERVS and highly conserved in all gammaretroviruses: MuLV carries FEGLFN, FeLV FEGWFN, and it shares three amino acids with the core epitope for the anti-HIV human neutralizing MAb 4E10, (LWNWFN). Fiebig2003
• 4E10: 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 (antibody interactions, immunoprophylaxis, mother-to-infant transmission)
• 4E10: 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. gp41 NAbs 2F5 and 4E10 are able to potently neutralize the SOS pseudovirion post-attachment. Binley2003 (vaccine antigen design)
• 4E10: Review of NAbs illustrating gp41's conformational change and exposure of the 4E10/Z13 epitope in the transient pre-hairpin form. Ferrantelli2002 (antibody binding site)
• 4E10: Passive immunization of neonate macaques with a combination of F105+2G12+2F5 conferred complete protection against oral challenge with SHIV-vpu+ ---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, subtype comparisons)
• 4E10: 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, subtype comparisons)
• 4E10: 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. Zwick2001c (antibody interactions)
• 4E10: MAbs 4E10 and Z13 both bind proximally to 2F5 to a conserved linear epitope that has some conformational aspects -- both bind to MN virions, bind weakly to infected cells in a manner that is not disrupted by sCD4 and neutralize some primary isolates from clades B, C, and E -- maps minimal 4E10 epitope to NWFDIT, contrary to an earlier report -- different strains were refractive to neutralization by broadly neutralizing Abs IgG1b12, 2F5, Z13 and 4E10. Zwick2001b (variant cross-reactivity, subtype comparisons)
• 4E10: 4E10 binds proximal to 2F5 and neutralizes primary isolates of clades A, B, C, D, and E. Viruses that were resistant to 2F5 were neutralized by 4E10 and vice versa. Stiegler2001 (antibody binding site)
• 4E10: Included in a multi-lab study for antibody characterization, binding and neutralization assay comparison. DSouza1994 (variant cross-reactivity)
• 4E10: MAbs generated by hybridoma, electrofusion of PBL from HIV-1+ volunteers with CB-F7 heteromyeloma cells -- also binds to MHC class II proteins -- anti-class II Abs are only found in HIV-1 positive people -- this paper maps 4E10's binding site to AEGTDRV, gp160(823-829), but the later Zwick et al. study in 2001 revised the epitope location. Buchacher1992,Buchacher1994 (antibody binding site, antibody generation)

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Banerjee2016 Saikat Banerjee, Heliang Shi, Habtom H. Habte, Yali Qin, and Michael W. Cho. Modulating Immunogenic Properties of HIV-1 gp41 Membrane-Proximal External Region by Destabilizing Six-Helix Bundle Structure. Virology, 490:17-26, Mar 2016. PubMed ID: 26803471. Show all entries for this paper.

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Beauparlant2017 David Beauparlant, Peter Rusert, Carsten Magnus, Claus Kadelka, Jacqueline Weber, Therese Uhr, Osvaldo Zagordi, Corinna Oberle, Maria J. Duenas-Decamp, Paul R. Clapham, Karin J. Metzner, Huldrych F. Gunthard, and Alexandra Trkola. Delineating CD4 dependency of HIV-1: Adaptation to infect low level CD4 expressing target cells widens cellular tropism but severely impacts on envelope functionality. PLoS Pathog, 13(3):e1006255 doi, Mar 2017. PubMed ID: 28264054 Show all entries for this paper.

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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.

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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.

Bradley2016a Todd Bradley, Ashley Trama, Nancy Tumba, Elin Gray, Xiaozhi Lu, Navid Madani, Fatemeh Jahanbakhsh, Amanda Eaton, Shi-Mao Xia, Robert Parks, Krissey E. Lloyd, Laura L. Sutherland, Richard M. Scearce, Cindy M. Bowman, Susan Barnett, Salim S. Abdool-Karim, Scott D. Boyd, Bruno Melillo, Amos B. Smith, 3rd., Joseph Sodroski, Thomas B. Kepler, S. Munir Alam, Feng Gao, Mattia Bonsignori, Hua-Xin Liao, M Anthony Moody, David Montefiori, Sampa Santra, Lynn Morris, and Barton F. Haynes. Amino Acid Changes in the HIV-1 gp41 Membrane Proximal Region Control Virus Neutralization Sensitivity. EBioMedicine, 12:196-207, Oct 2016. PubMed ID: 27612593. 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.

Brown2007 Bruce K. Brown, Nicos Karasavvas, Zoltan Beck, Gary R. Matyas, Deborah L. Birx, Victoria R. Polonis, and Carl R. Alving. Monoclonal Antibodies to Phosphatidylinositol Phosphate Neutralize Human Immunodeficiency Virus Type 1: Role of Phosphate-Binding Subsites. J. Virol., 81(4):2087-2091, Feb 2007. PubMed ID: 17151131. 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.

Bruel2016 Timothée Bruel, Florence Guivel-Benhassine, Sonia Amraoui, Marine Malbec, Léa Richard, Katia Bourdic, Daniel Aaron Donahue, Valérie Lorin, Nicoletta Casartelli, Nicolas Noël, Olivier Lambotte, Hugo Mouquet, and Olivier Schwartz. Elimination of HIV-1-Infected Cells by Broadly Neutralizing Antibodies. Nat. Commun., 7:10844, 3 Mar 2016. PubMed ID: 26936020. Show all entries for this paper.

Brunel2006 Florence M. Brunel, Michael B. Zwick, Rosa M. F. Cardoso, Josh D. Nelson, Ian A. Wilson, Dennis R. Burton, and Philip E. Dawson. Structure-Function Analysis of the Epitope for 4E10, a Broadly Neutralizing Human Immunodeficiency Virus Type 1 Antibody. J. Virol., 80(4):1680-1687, Feb 2006. PubMed ID: 16439525. Show all entries for this paper.

Bryson2009 Steve Bryson, Jean-Philippe Julien, Rosemary C. Hynes, and Emil F. Pai. Crystallographic Definition of the Epitope Promiscuity of the Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5: Vaccine Design Implications. J. Virol., 83(22):11862-11875, Nov 2009. PubMed ID: 19740978. Show all entries for this paper.

Buchacher1992 Andrea Buchacher, Renate Predl, Christa Tauer, Martin Purtscher, Gerhard Gruber, Renate Heider, Fraz Steindl, Alexandra Trkola, Alois Jungbauer, and Herman Katinger. Human Monoclonal Antibodies against gp41 and gp120 as Potential Agent for Passive Immunization. Vaccines, 92:191-195, 1992. 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.

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.

Buzon2010 Victor Buzon, Ganesh Natrajan, David Schibli, Felix Campelo, Michael M. Kozlov, and Winfried Weissenhorn. Crystal Structure of HIV-1 gp41 Including Both Fusion Peptide and Membrane Proximal External Regions. PLoS Pathog, 6(5):e1000880, May 2010. PubMed ID: 20463810. 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.

Cardoso2005 Rosa M. F. Cardoso, Michael B. Zwick, Robyn L. Stanfield, Renate Kunert, James M. Binley, Hermann Katinger, Dennis R. Burton, and Ian A. Wilson. Broadly Neutralizing Anti-HIV Antibody 4E10 Recognizes a Helical Conformation of a Highly Conserved Fusion-Associated Motif in gp41. Immunity, 22(2):163-173, Feb 2005. PubMed ID: 15723805. Show all entries for this paper.

Cardoso2007 Rosa M. F. Cardoso, Florence M. Brunel, Sharon Ferguson, Michael Zwick, Dennis R. Burton, Philip E. Dawson, and Ian A. Wilson. Structural Basis of Enhanced Binding of Extended and Helically Constrained Peptide Epitopes of the Broadly Neutralizing HIV-1 Antibody 4E10. J. Mol. Biol., 365(5):1533-1544, 2 Feb 2007. PubMed ID: 17125793. Show all entries for this paper.

Chakrabarti2011 B. K. Chakrabarti, L. M. Walker, J. F. Guenaga, A. Ghobbeh, P. Poignard, D. R. Burton, and R. T. Wyatt. Direct Antibody Access to the HIV-1 Membrane-Proximal External Region Positively Correlates with Neutralization Sensitivity. J. Virol., 85(16):8217-8226, Aug 2011. PubMed ID: 21653673. 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.

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.

Chen2013 Yao Chen, Jinsong Zhang, Kwan-Ki Hwang, Hilary Bouton-Verville, Shi-Mao Xia, Amanda Newman, Ying-Bin Ouyang, Barton F. Haynes, and Laurent Verkoczy. Common Tolerance Mechanisms, but Distinct Cross-Reactivities Associated with gp41 and Lipids, Limit Production of HIV-1 Broad Neutralizing Antibodies 2F5 and 4E10. J. Immunol., 191(3):1260-1275, Aug 1 2013. PubMed ID: 23825311. Show all entries for this paper.

Chen2014 Jia Chen, Gary Frey, Hanqin Peng, Sophia Rits-Volloch, Jetta Garrity, Michael S. Seaman, and Bing Chen. Mechanism of HIV-1 Neutralization by Antibodies Targeting a Membrane-Proximal Region of gp41. J. Virol., 88(2):1249-1258, Jan 2014. PubMed ID: 24227838. 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.

Chenine2013 Agnès-Laurence Chenine, Lindsay Wieczorek, Eric Sanders-Buell, Maggie Wesberry, Teresa Towle, Devin M. Pillis, Sebastian Molnar, Robert McLinden, Tara Edmonds, Ivan Hirsch, Robert O'Connell, Francine E. McCutchan, David C. Montefiori, Christina Ochsenbauer, John C. Kappes, Jerome H. Kim, Victoria R. Polonis, and Sodsai Tovanabutra. Impact of HIV-1 Backbone on Neutralization Sensitivity: Neutralization Profiles of Heterologous Envelope Glycoproteins Expressed in Native Subtype C and CRF01\_AE Backbone. PLoS One, 8(11):e76104, 2013. PubMed ID: 24312165. 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.

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.

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.

Choudhry2006 Vidita Choudhry, Mei-Yun Zhang, Ilia Harris, Igor A. Sidorov, Bang Vu, Antony S. Dimitrov, Timothy Fouts, and Dimiter S. Dimitrov. Increased Efficacy of HIV-1 Neutralization by Antibodies at Low CCR5 Surface Concentration. Biochem. Biophys. Res. Commun., 348(3):1107-1115, 29 Sep 2006. PubMed ID: 16904645. Show all entries for this paper.

Choudhry2007 Vidita Choudhry, Mei-Yun Zhang, Igor A. Sidorov, John M. Louis, Ilia Harris, Antony S. Dimitrov, Peter Bouma, Fatim Cham, Anil Choudhary, Susanna M. Rybak, Timothy Fouts, David C. Montefiori, Christopher C. Broder, Gerald V. Quinnan, Jr., and Dimiter S. Dimitrov. Cross-Reactive HIV-1 Neutralizing Monoclonal Antibodies Selected by Screening of an Immune Human Phage Library Against an Envelope Glycoprotein (gp140) Isolated from a Patient (R2) with Broadly HIV-1 Neutralizing Antibodies. Virology, 363(1):79-90, 20 Jun 2007. PubMed ID: 17306322. Show all entries for this paper.

Chuang2013 Gwo-Yu Chuang, Priyamvada Acharya, Stephen D. Schmidt, Yongping Yang, Mark K. Louder, Tongqing Zhou, Young Do Kwon, Marie Pancera, Robert T. Bailer, Nicole A. Doria-Rose, Michel C. Nussenzweig, John R. Mascola, Peter D. Kwong, and Ivelin S. Georgiev. Residue-Level Prediction of HIV-1 Antibody Epitopes Based on Neutralization of Diverse Viral Strains. J. Virol., 87(18):10047-10058, Sep 2013. PubMed ID: 23843642. Show all entries for this paper.

Correia2010 Bruno E. Correia, Yih-En Andrew Ban, Margaret A. Holmes, Hengyu Xu, Katharine Ellingson, Zane Kraft, Chris Carrico, Erica Boni, D. Noah Sather, Camille Zenobia, Katherine Y. Burke, Tyler Bradley-Hewitt, Jessica F. Bruhn-Johannsen, Oleksandr Kalyuzhniy, David Baker, Roland K. Strong, Leonidas Stamatatos, and William R. Schief. Computational Design of Epitope-Scaffolds Allows Induction of Antibodies Specific for a Poorly Immunogenic HIV Vaccine Epitope. Structure, 18(9):1116-1126, 8 Sep 2010. PubMed ID: 20826338. 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.

Coutant2008 Jérôme Coutant, Huifeng Yu, Marie-Jeanne Clément, Annette Alfsen, Flavio Toma, Patrick A. Curmi, and Morgane Bomsel. Both Lipid Environment and pH Are Critical for Determining Physiological Solution Structure of 3-D-Conserved Epitopes of the HIV-1 gp41-MPER Peptide P1. FASEB J., 22(12):4338-4351, Dec 2008. PubMed ID: 18776068. 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.

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.

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.

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.

Dennison2009 S. Moses Dennison, Shelley M. Stewart, Kathryn C. Stempel, Hua-Xin Liao, Barton F. Haynes, and S. Munir Alam. Stable Docking of Neutralizing Human Immunodeficiency Virus Type 1 gp41 Membrane-Proximal External Region Monoclonal Antibodies 2F5 and 4E10 Is Dependent on the Membrane Immersion Depth of Their Epitope Regions. J. Virol., 83(19):10211-10223, Oct 2009. PubMed ID: 19640992. 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.

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.

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.

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.

Dimitrov2007 Antony S. Dimitrov, Amy Jacobs, Catherine M. Finnegan, Gabriela Stiegler, Hermann Katinger, and Robert Blumenthal. Exposure of the Membrane-Proximal External Region of HIV-1 gp41 in the Course of HIV-1 Envelope Glycoprotein-Mediated Fusion. Biochemistry, 46(5):1398-1401, 6 Feb 2007. PubMed ID: 17260969. Show all entries for this paper.

Dong2006 Xiao-Nan Dong and Ying-Hua Chen. Neutralizing Epitopes in the Membrane-Proximal Region of HIV-1 gp41: Genetic Variability and Co-Variation. Immunol. Lett., 106(2):180-186, 15 Aug 2006. PubMed ID: 16859756. 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.

Doria-Rose2017 Nicole A. Doria-Rose, Han R. Altae-Tran, Ryan S. Roark, Stephen D. Schmidt, Matthew S. Sutton, Mark K. Louder, Gwo-Yu Chuang, Robert T. Bailer, Valerie Cortez, Rui Kong, Krisha McKee, Sijy O'Dell, Felicia Wang, Salim S. Abdool Karim, James M. Binley, Mark Connors, Barton F. Haynes, Malcolm A. Martin, David C. Montefiori, Lynn Morris, Julie Overbaugh, Peter D. Kwong, John R. Mascola, and Ivelin S. Georgiev. Mapping Polyclonal HIV-1 Antibody Responses via Next-Generation Neutralization Fingerprinting. PLoS Pathog., 13(1):e1006148, Jan 2017. PubMed ID: 28052137. Show all entries for this paper.

Doyle-Cooper2013 Colleen Doyle-Cooper, Krystalyn E. Hudson, Anthony B. Cooper, Takayuki Ota, Patrick Skog, Phillip E. Dawson, Michael B. Zwick, William R. Schief, Dennis R. Burton, and David Nemazee. Immune Tolerance Negatively Regulates B Cells in Knock-In Mice Expressing Broadly Neutralizing HIV Antibody 4E10. J. Immunol., 191(6):3186-3191, 15 Sep 2013. PubMed ID: 23940276. Show all entries for this paper.

DSouza1994 M. P. D'Souza, S. J. Geyer, C. V. Hanson, R. M. Hendry, G. Milman, and Collaborating Investigators. Evaluation of Monoclonal Antibodies to HIV-1 Envelope by Neutralization and Binding Assays: An International Collaboration. AIDS, 8:169-181, 1994. PubMed ID: 7519019. 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.

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.

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.

Fiebig2003 Uwe Fiebig, Oliver Stephan, Reinhard Kurth, and Joachim Denner. Neutralizing Antibodies against Conserved Domains of p15E of Porcine Endogenous Retroviruses: Basis for a Vaccine for Xenotransplantation? Virology, 307(2):406-413, 15 Mar 2003. PubMed ID: 12667808. Show all entries for this paper.

Fiebig2009 Uwe Fiebig, Mirco Schmolke, Magdalena Eschricht, Reinhard Kurth, and Joachim Denner. Mode of Interaction between the HIV-1-Neutralizing Monoclonal Antibody 2F5 and Its Epitope. AIDS, 23(8):887-895, 15 May 2009. PubMed ID: 19414989. Show all entries for this paper.

Finton2013 Kathryn A. K. Finton, Kevin Larimore, H. Benjamin Larman, Della Friend, Colin Correnti, Peter B. Rupert, Stephen J. Elledge, Philip D. Greenberg, and Roland K. Strong. Autoreactivity and Exceptional CDR Plasticity (but Not Unusual Polyspecificity) Hinder Elicitation of the Anti-HIV Antibody 4E10. PLoS Pathog., 9(9):e1003639, 2013. PubMed ID: 24086134. Show all entries for this paper.

Finton2014 Kathryn A. K. Finton, Della Friend, James Jaffe, Mesfin Gewe, Margaret A. Holmes, H. Benjamin Larman, Andrew Stuart, Kevin Larimore, Philip D. Greenberg, Stephen J. Elledge, Leonidas Stamatatos, and Roland K. Strong. Ontogeny of Recognition Specificity and Functionality for the Broadly Neutralizing Anti-HIV Antibody 4E10. PLoS Pathog., 10(9):e1004403, Sep 2014. PubMed ID: 25254371. 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.

Franquelim2011 Henri G. Franquelim, Salvatore Chiantia, Ana Salomé Veiga, Nuno C. Santos, Petra Schwille, and Miguel A. R. B. Castanho. Anti-HIV-1 Antibodies 2F5 and 4E10 Interact Differently with Lipids to Bind Their Epitopes. AIDS, 25(4):419-428, 20 Feb 2011. PubMed ID: 21245727. 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.

Frey2010 Gary Frey, Jia Chen, Sophia Rits-Volloch, Michael M. Freeman, Susan Zolla-Pazner, and Bing Chen. Distinct Conformational States of HIV-1 gp41 Are Recognized by Neutralizing and Non-Neutralizing Antibodies. Nat. Struct. Mol. Biol., 17(12):1486-1491, Dec 2010. PubMed ID: 21076402. Show all entries for this paper.

Fu2018 Qingshan Fu, Md Munan Shaik, Yongfei Cai, Fadi Ghantous, Alessandro Piai, Hanqin Peng, Sophia Rits-Volloch, Zhijun Liu, Stephen C. Harrison, Michael S. Seaman, Bing Chen, and James J. Chou. Structure of the Membrane Proximal External Region of HIV-1 Envelope Glycoprotein. Proc. Natl. Acad. Sci. U.S.A., 115(38):E8892-E8899, 18 Sep 2018. PubMed ID: 30185554. 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.

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.

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.

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.

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.

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.

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.

Gray2008 Elin S. Gray, Penny L. Moore, Frederic Bibollet-Ruche, Hui Li, Julie M. Decker, Tammy Meyers, George M. Shaw, and Lynn Morris. 4E10-Resistant Variants in a Human Immunodeficiency Virus Type 1 Subtype C-Infected Individual with an Anti-Membrane-Proximal External Region-Neutralizing Antibody Response. J. Virol., 82(5):2367-2375, Mar 2008. PubMed ID: 18094155. Show all entries for this paper.

Gray2009a Elin S. Gray, Maphuti C. Madiga, Penny L. Moore, Koleka Mlisana, Salim S. Abdool Karim, James M. Binley, George M. Shaw, John R. Mascola, and Lynn Morris. Broad Neutralization of Human Immunodeficiency Virus Type 1 Mediated by Plasma Antibodies against the gp41 Membrane Proximal External Region. J. Virol., 83(21):11265-11274, Nov 2009. PubMed ID: 19692477. 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.

Gustchina2007 Elena Gustchina, John M. Louis, Son N. Lam, Carole A. Bewley, and G. Marius Clore. A Monoclonal Fab Derived from a Human Nonimmune Phage Library Reveals a New Epitope on gp41 and Neutralizes Diverse Human Immunodeficiency Virus Type 1 Strains. J. Virol., 81(23):12946-12953, Dec 2007. PubMed ID: 17898046. 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.

Habte2015 Habtom H. Habte, Saikat Banerjee, Heliang Shi, Yali Qin, and Michael W. Cho. Immunogenic Properties of a Trimeric gp41-Based Immunogen Containing an Exposed Membrane-Proximal External Region. Virology, 486:187-197, Dec 2015. PubMed ID: 26454663. Show all entries for this paper.

Hager-Braun2006 Christine Hager-Braun, Hermann Katinger, and Kenneth B. Tomer. The HIV-Neutralizing Monoclonal Antibody 4E10 Recognizes N-Terminal Sequences on the Native Antigen. J. Immunol., 176(12):7471-7481, 15 Jun 2006. PubMed ID: 16751393. Show all entries for this paper.

Hammond2010 Philip W. Hammond. Accessing the Human Repertoire for Broadly Neutralizing HIV Antibodies. MAbs, 2(2):157-164, Mar-Apr 2010. PubMed ID: 20168075. Show all entries for this paper.

Hardy2012 Gregory J. Hardy, Yee Lam, Shelley M. Stewart, Kara Anasti, S. Munir Alam, and Stefan Zauscher. Screening the Interactions between HIV-1 Neutralizing Antibodies and Model Lipid Surfaces. J. Immunol. Methods, 376(1-2):13-19, 28 Feb 2012. PubMed ID: 22033342. 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.

Haynes2010 Barton F. Haynes, Nathan I. Nicely, and S. Munir Alam. HIV-1 Autoreactive Antibodies: Are They Good or Bad for HIV-1 Prevention? Nat. Struct. Mol. Biol., 17(5):543-545, May 2010. PubMed ID: 20442740. 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.

Haynes2013 Barton F. Haynes and M. Juliana McElrath. Progress in HIV-1 Vaccine Development. Curr. Opin. HIV AIDS, 8(4):326-332, Jul 2013. PubMed ID: 23743722. Show all entries for this paper.

Haynes2016 Barton F. Haynes, George M. Shaw, Bette Korber, Garnett Kelsoe, Joseph Sodroski, Beatrice H. Hahn, Persephone Borrow, and Andrew J. McMichael. HIV-Host Interactions: Implications for Vaccine Design. Cell Host Microbe, 19(3):292-303, 9 Mar 2016. PubMed ID: 26922989. Show all entries for this paper.

Hessell2010 Ann J. Hessell, Eva G. Rakasz, David M. Tehrani, Michael Huber, Kimberly L. Weisgrau, Gary Landucci, Donald N. Forthal, Wayne C. Koff, Pascal Poignard, David I. Watkins, and Dennis R. Burton. Broadly Neutralizing Monoclonal Antibodies 2F5 and 4E10 Directed Against the Human Immunodeficiency Virus Type 1 gp41 Membrane-Proximal External Region Protect against Mucosal Challenge by Simian-Human Immunodeficiency Virus SHIVBa-L. J. Virol., 84(3):1302-1313, Feb 2010. PubMed ID: 19906907. Show all entries for this paper.

Hicar2010 Mark D. Hicar, Xuemin Chen, Bryan Briney, Jason Hammonds, Jaang-Jiun Wang, Spyros Kalams, Paul W. Spearman, and James E. Crowe, Jr. Pseudovirion Particles Bearing Native HIV Envelope Trimers Facilitate a Novel Method for Generating Human Neutralizing Monoclonal Antibodies Against HIV. J. Acquir. Immune Defic. Syndr., 54(3):223-235, Jul 2010. PubMed ID: 20531016. 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.

Hinz2009 Andreas Hinz, Guy Schoehn, Heribert Quendler, David Lutje Hulsik, Gabi Stiegler, Hermann Katinger, Michael S. Seaman, David Montefiori, and Winfried Weissenhorn. Characterization of a Trimeric MPER Containing HIV-1 gp41 Antigen. Virology, 390(2):221-227, 1 Aug 2009. PubMed ID: 19539967. 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.

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.

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.

Hraber2017 Peter Hraber, Cecilia Rademeyer, Carolyn Williamson, Michael S. Seaman, Raphael Gottardo, Haili Tang, Kelli Greene, Hongmei Gao, Celia LaBranche, John R. Mascola, Lynn Morris, David C. Montefiori, and Bette Korber. Panels of HIV-1 Subtype C Env Reference Strains for Standardized Neutralization Assessments. J. Virol., 91(19), 1 Oct 2017. PubMed ID: 28747500. Show all entries for this paper.

Hu2014 Bin Hu, Hua-Xin Liao, S. Munir Alam, and Byron Goldstein. Estimating the Probability of Polyreactive Antibodies 4E10 and 2F5 Disabling a gp41 Trimer after T Cell-HIV Adhesion. PLoS Comput. Biol., 10(1):e1003431, Jan 2014. PubMed ID: 24499928. Show all entries for this paper.

Hua2016 Casey K. Hua and Margaret E. Ackerman. Engineering Broadly Neutralizing Antibodies for HIV Prevention and Therapy. Adv. Drug Deliv. Rev., 103:157-173, 1 Aug 2016. PubMed ID: 26827912. 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.

Huang2012a Jinghe Huang, Gilad Ofek, Leo Laub, Mark K. Louder, Nicole A. Doria-Rose, Nancy S. Longo, Hiromi Imamichi, Robert T. Bailer, Bimal Chakrabarti, Shailendra K. Sharma, S. Munir Alam, Tao Wang, Yongping Yang, Baoshan Zhang, Stephen A. Migueles, Richard Wyatt, Barton F. Haynes, Peter D. Kwong, John R. Mascola, and Mark Connors. Broad and Potent Neutralization of HIV-1 by a gp41-Specific Human Antibody. Nature, 491(7424):406-412, 15 Nov 2012. PubMed ID: 23151583. 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.

Huarte2008 Nerea Huarte, Maier Lorizate, Renate Kunert, and José L. Nieva. Lipid Modulation of Membrane-Bound Epitope Recognition and Blocking by HIV-1 Neutralizing Antibodies. FEBS Lett, 582(27):3798-3804, 12 Nov 2008. PubMed ID: 18930052. Show all entries for this paper.

Huarte2008a Nerea Huarte, Maier Lorizate, Rubén Maeso, Renate Kunert, Rocio Arranz, José M. Valpuesta, and José L. Nieva. The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 4E10 Monoclonal Antibody Is Better Adapted to Membrane-Bound Epitope Recognition and Blocking than 2F5. J. Virol., 82(18):8986-8996, Sep 2008. PubMed ID: 18596094. 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.

Ingale2010 Sampat Ingale, Johannes S. Gach, Michael B. Zwick, and Philip E. Dawson. Synthesis and Analysis of the Membrane Proximal External Region Epitopes of HIV-1. J. Pept. Sci., 16(12):716-722, Dec 2010. PubMed ID: 21104968. Show all entries for this paper.

Irimia2016 Adriana Irimia, Anita Sarkar, Robyn L. Stanfield, and Ian A. Wilson. Crystallographic Identification of Lipid as an Integral Component of the Epitope of HIV Broadly Neutralizing Antibody 4E10. Immunity, 44(1):21-31, 19 Jan 2016. PubMed ID: 26777395. Show all entries for this paper.

Ivankin2012 Andrey Ivankin, Beatriz Apellániz, David Gidalevitz, and José L. Nieva. Mechanism of Membrane Perturbation by the HIV-1 gp41 Membrane-Proximal External Region and Its Modulation by Cholesterol. Biochim. Biophys. Acta, 1818(11):2521-2528, Nov 2012. PubMed ID: 22692008. 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.

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.

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.

Kelsoe2017 Garnett Kelsoe and Barton F. Haynes. Host Controls of HIV Broadly Neutralizing Antibody Development. Immunol. Rev., 275(1):79-88, Jan 2017. PubMed ID: 28133807. Show all entries for this paper.

Kim2007 Mikyung Kim, Zhisong Qiao, Jessica Yu, David Montefiori, and Ellis L. Reinherz. Immunogenicity of Recombinant Human Immunodeficiency Virus Type 1-Like Particles Expressing gp41 Derivatives in a Pre-Fusion State. Vaccine, 25(27):5102-5114, 28 Jun 2007. PubMed ID: 17055621. 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.

Klein2009 Joshua S. Klein, Priyanthi N. P. Gnanapragasam, Rachel P. Galimidi, Christopher P. Foglesong, Anthony P. West, Jr., and Pamela J. Bjorkman. Examination of the Contributions of Size and Avidity to the Neutralization Mechanisms of the Anti-HIV Antibodies b12 and 4E10. Proc. Natl. Acad. Sci. U.S.A., 106(18):7385-7390, 5 May 2009. PubMed ID: 19372381. 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.

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.

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.

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.

Krebs2019 Shelly J. Krebs, Young D. Kwon, Chaim A. Schramm, William H. Law, Gina Donofrio, Kenneth H. Zhou, Syna Gift, Vincent Dussupt, Ivelin S. Georgiev, Sebastian Schätzle, Jonathan R. McDaniel, Yen-Ting Lai, Mallika Sastry, Baoshan Zhang, Marissa C. Jarosinski, Amy Ransier, Agnes L. Chenine, Mangaiarkarasi Asokan, Robert T. Bailer, Meera Bose, Alberto Cagigi, Evan M. Cale, Gwo-Yu Chuang, Samuel Darko, Jefferson I. Driscoll, Aliaksandr Druz, Jason Gorman, Farida Laboune, Mark K. Louder, Krisha McKee, Letzibeth Mendez, M. Anthony Moody, Anne Marie O'Sullivan, Christopher Owen, Dongjun Peng, Reda Rawi, Eric Sanders-Buell, Chen-Hsiang Shen, Andrea R. Shiakolas, Tyler Stephens, Yaroslav Tsybovsky, Courtney Tucker, Raffaello Verardi, Keyun Wang, Jing Zhou, Tongqing Zhou, George Georgiou, S Munir Alam, Barton F. Haynes, Morgane Rolland, Gary R. Matyas, Victoria R. Polonis, Adrian B. McDermott, Daniel C. Douek, Lawrence Shapiro, Sodsai Tovanabutra, Nelson L. Michael, John R. Mascola, Merlin L. Robb, Peter D. Kwong, and Nicole A. Doria-Rose. Longitudinal Analysis Reveals Early Development of Three MPER-Directed Neutralizing Antibody Lineages from an HIV-1-Infected Individual. Immunity, 50(3):677-691.e13, 19 Mar 2019. PubMed ID: 30876875. 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.

Kunert2004 Renate Kunert, Susanne Wolbank, Gabriela Stiegler, Robert Weik, and Hermann Katinger. Characterization of Molecular Features, Antigen-Binding, and In Vitro Properties of IgG and IgM Variants of 4E10, an Anti-HIV Type 1 Neutralizing Monoclonal Antibody. AIDS Res. Hum. Retroviruses, 20(7):755-762, Jul 2004. PubMed ID: 15307922. Show all entries for this paper.

Kwon2018 Young D. Kwon, Gwo-Yu Chuang, Baoshan Zhang, Robert T. Bailer, Nicole A. Doria-Rose, Tatyana S. Gindin, Bob Lin, Mark K. Louder, Krisha McKee, Sijy O'Dell, Amarendra Pegu, Stephen D. Schmidt, Mangaiarkarasi Asokan, Xuejun Chen, Misook Choe, Ivelin S. Georgiev, Vivian Jin, Marie Pancera, Reda Rawi, Keyun Wang, Rajoshi Chaudhuri, Lisa A. Kueltzo, Slobodanka D. Manceva, John-Paul Todd, Diana G. Scorpio, Mikyung Kim, Ellis L. Reinherz, Kshitij Wagh, Bette M. Korber, Mark Connors, Lawrence Shapiro, John R. Mascola, and Peter D. Kwong. Surface-Matrix Screening Identifies Semi-specific Interactions that Improve Potency of a Near Pan-reactive HIV-1-Neutralizing Antibody. Cell Rep., 22(7):1798-1809, 13 Feb 2018. PubMed ID: 29444432. 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.

Laakso2007 Meg M. Laakso, Fang-Hua Lee, Beth Haggarty, Caroline Agrawal, Katrina M. Nolan, Mark Biscone, Josephine Romano, Andrea P. O. Jordan, George J. Leslie, Eric G. Meissner, Lishan Su, James A. Hoxie, and Robert W. Doms. V3 Loop Truncations in HIV-1 Envelope Impart Resistance to Coreceptor Inhibitors and Enhanced Sensitivity to Neutralizing Antibodies. PLoS Pathog., 3(8):e117, 24 Aug 2007. PubMed ID: 17722977. 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.

Lai2011 Rachel P. J. Lai, Jin Yan, Jonathan Heeney, Myra O. McClure, Heinrich Göttlinger, Jeremy Luban, and Massimo Pizzato. Nef Decreases HIV-1 Sensitivity to Neutralizing Antibodies that Target the Membrane-Proximal External Region of TMgp41. PLoS Pathog, 7(12):e1002442, Dec 2011. PubMed ID: 22194689. Show all entries for this paper.

Lai2012 Rachel P. J. Lai, Michael S. Seaman, Paul Tonks, Frank Wegmann, David J. Seilly, Simon D. W. Frost, Celia C. LaBranche, David C. Montefiori, Antu K. Dey, Indresh K. Srivastava, Quentin Sattentau, Susan W. Barnett, and Jonathan L. Heeney. Mixed Adjuvant Formulations Reveal a New Combination That Elicit Antibody Response Comparable to Freund's Adjuvants. PLoS One, 7(4):e35083, 2012. PubMed ID: 22509385. 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.

Lapelosa2009 Mauro Lapelosa, Emilio Gallicchio, Gail Ferstandig Arnold, Eddy Arnold, and Ronald M. Levy. In Silico Vaccine Design Based on Molecular Simulations of Rhinovirus Chimeras Presenting HIV-1 gp41 Epitopes. J. Mol. Biol., 385(2):675-691, 16 Jan 2009. PubMed ID: 19026659. 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.

Lenz2005 Oliver Lenz, Matthias T Dittmar, Andreas Wagner, Boris Ferko, Karola Vorauer-Uhl, Gabriela Stiegler, and Winfried Weissenhorn. Trimeric Membrane-Anchored gp41 Inhibits HIV Membrane Fusion. J. Biol. Chem., 280(6):4095-4101, 11 Feb 2005. PubMed ID: 15574416. 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.

Li2008a Jing Li, Xi Chen, Shibo Jiang, and Ying-Hua Chen. Deletion of Fusion Peptide or Destabilization of Fusion Core of HIV gp41 Enhances Antigenicity and Immunogenicity of 4E10 Epitope. Biochem. Biophys. Res. Commun., 376(1):60-64, 7 Nov 2008. PubMed ID: 18762167. 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.

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.

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.

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.

Liu2009 Jie Liu, Yiqun Deng, Antu K. Dey, John P. Moore, and Min Lu. Structure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation. Biochemistry, 48(13):2915-2923, 7 Apr 2009. PubMed ID: 19226163. Show all entries for this paper.

Liu2010 Jie Liu, Yiqun Deng, Qunnu Li, Antu K. Dey, John P. Moore, and Min Lu. Role of a Putative gp41 Dimerization Domain in Human Immunodeficiency Virus Type 1 Membrane Fusion. J. Virol., 84(1):201-209, Jan 2010. PubMed ID: 19846514. 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.

Lorizate2006 Maier Lorizate, Antonio Cruz, Nerea Huarte, Renate Kunert, Jesús Pérez-Gil, and José L. Nieva. Recognition and Blocking of HIV-1 gp41 Pre-Transmembrane Sequence by Monoclonal 4E10 Antibody in a Raft-Like Membrane Environment. J. Biol. Chem., 281(51):39598-39606, 22 Dec 2006. PubMed ID: 17050535. Show all entries for this paper.

Lorizate2006a Maier Lorizate, Igor de la Arada, Nerea Huarte, Silvia Sánchez-Martínez, Beatriz G. de la Torre, David Andreu, José L. R. Arrondo, and José L. Nieva. Structural Analysis and Assembly of the HIV-1 Gp41 Amino-Terminal Fusion Peptide and the Pretransmembrane Amphipathic-At-Interface Sequence. Biochemistry, 45(48):14337-14346, 5 Dec 2006. PubMed ID: 17128972. 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.

Lovelace2011 Erica Lovelace, Hengyu Xu, Catherine A. Blish, Roland Strong, and Julie Overbaugh. The Role of Amino Acid Changes in the Human Immunodeficiency Virus Type 1 Transmembrane Domain in Antibody Binding and Neutralization. Virology, 421(2):235-244, 20 Dec 2011. PubMed ID: 22029936. Show all entries for this paper.

Luo2006 Min Luo, Fei Yuan, Yanxia Liu, Siming Jiang, Xijun Song, Pengfei Jiang, Xiaolei Yin, Mingxiao Ding, and Hongkui Deng. Induction of Neutralizing Antibody against Human Immunodeficiency Virus Type 1 (HIV-1) by Immunization with gp41 Membrane-Proximal External Region (MPER) Fused with Porcine Endogenous Retrovirus (PERV) p15E Fragment. Vaccine, 24(4):4354-4342, 23 Jan 2006. PubMed ID: 16143433. Show all entries for this paper.

Lynch2011 John B. Lynch, Ruth Nduati, Catherine A. Blish, Barbra A. Richardson, Jennifer M. Mabuka, Zahra Jalalian-Lechak, Grace John-Stewart, and Julie Overbaugh. The Breadth and Potency of Passively Acquired Human Immunodeficiency Virus Type 1-Specific Neutralizing Antibodies Do Not Correlate with the Risk of Infant Infection. J. Virol., 85(11):5252-5261, Jun 2011. PubMed ID: 21411521. 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.

Malbec2013 Marine Malbec, Françoise Porrot, Rejane Rua, Joshua Horwitz, Florian Klein, Ari Halper-Stromberg, Johannes F. Scheid, Caroline Eden, Hugo Mouquet, Michel C. Nussenzweig, and Olivier Schwartz. Broadly Neutralizing Antibodies That Inhibit HIV-1 Cell to Cell Transmission. J. Exp. Med., 210(13):2813-2821, 16 Dec 2013. PubMed ID: 24277152. 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.

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.

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.

Massanella2009 Marta Massanella, Isabel Puigdomènech, Cecilia Cabrera, Maria Teresa Fernandez-Figueras, Anne Aucher, Gerald Gaibelet, Denis Hudrisier, Elisabet García, Margarita Bofill, Bonaventura Clotet, and Julià Blanco. Antigp41 Antibodies Fail to Block Early Events of Virological Synapses but Inhibit HIV Spread between T Cells. AIDS, 23(2):183-188, 14 Jan 2009. PubMed ID: 19098487. Show all entries for this paper.

Matoba2008 Nobuyuki Matoba, Tagan A. Griffin, Michele Mittman, Jeffrey D. Doran, Annette Alfsen, David C. Montefiori, Carl V. Hanson, Morgane Bomsel, and Tsafrir S. Mor. Transcytosis-Blocking Abs Elicited by an Oligomeric Immunogen Based on the Membrane Proximal Region of HIV-1 gp41 Target Non-Neutralizing Epitopes. Curr. HIV Res., 6(3):218-229, May 2008. PubMed ID: 18473785. 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.

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.

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.

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.

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.

Montero2012 Marinieve Montero, Naveed Gulzar, Kristina-Ana Klaric, Jason E. Donald, Christa Lepik, Sampson Wu, Sue Tsai, Jean-Philippe Julien, Ann J. Hessell, Shixia Wang, Shan Lu, Dennis R. Burton, Emil F. Pai, William F. DeGrado, and Jamie K. Scott. Neutralizing Epitopes in the Membrane-Proximal External Region of HIV-1 gp41 Are Influenced by the Transmembrane Domain and the Plasma Membrane. J. Virol., 86(6):2930-2941, Mar 2012. PubMed ID: 22238313. 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.

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.

Morgand2015 Marion Morgand, Mélanie Bouvin-Pley, Jean-Christophe Plantier, Alain Moreau, Elodie Alessandri, François Simon, Craig S. Pace, Marie Pancera, David D. Ho, Pascal Poignard, Pamela J. Bjorkman, Hugo Mouquet, Michel C. Nussenzweig, Peter D. Kwong, Daniel Baty, Patrick Chames, Martine Braibant, and Francis Barin. A V1V2 Neutralizing Epitope Is Conserved in Divergent Non-M Groups of HIV-1. J. Acquir. Immune Defic. Syndr., 21 Sep 2015. PubMed ID: 26413851. Show all entries for this paper.

Morris2011 Lynn Morris, Xi Chen, Munir Alam, Georgia Tomaras, Ruijun Zhang, Dawn J. Marshall, Bing Chen, Robert Parks, Andrew Foulger, Frederick Jaeger, Michele Donathan, Mira Bilska, Elin S. Gray, Salim S. Abdool Karim, Thomas B. Kepler, John Whitesides, David Montefiori, M. Anthony Moody, Hua-Xin Liao, and Barton F. Haynes. Isolation of a Human Anti-HIV gp41 Membrane Proximal Region Neutralizing Antibody by Antigen-Specific Single B Cell Sorting. PLoS One, 6(9):e23532, 2011. PubMed ID: 21980336. 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.

Muhle2013 Michael Mühle, Kerstin Hoffmann, Martin Löchelt, and Joachim Denner. Construction and Characterisation of Replicating Foamy Viral Vectors Expressing HIV-1 Epitopes Recognised by Broadly Neutralising Antibodies. Antiviral Res., 100(2):314-320, Nov 2013. PubMed ID: 24055836. 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.

Nakamura2010 Kyle J. Nakamura, Johannes S Gach, Laura Jones, Katherine Semrau, Jan Walter, Frederic Bibollet-Ruche, Julie M. Decker, Laura Heath, William D. Decker, Moses Sinkala, Chipepo Kankasa, Donald Thea, James Mullins, Louise Kuhn, Michael B. Zwick, and Grace M. Aldrovandi. 4E10-Resistant HIV-1 Isolated from Four Subjects with Rare Membrane-Proximal External Region Polymorphisms. PLoS One, 5(3):e9786, 2010. PubMed ID: 20352106. 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.

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.

Nelson2008 Josh D. Nelson, Heather Kinkead, Florence M. Brunel, Dan Leaman, Richard Jensen, John M. Louis, Toshiaki Maruyama, Carole A. Bewley, Katherine Bowdish, G. Marius Clore, Philip E. Dawson, Shana Frederickson, Rose G. Mage, Douglas D. Richman, Dennis R. Burton, and Michael B. Zwick. Antibody Elicited against the gp41 N-Heptad Repeat (NHR) Coiled-Coil Can Neutralize HIV-1 with Modest Potency but Non-Neutralizing Antibodies Also Bind to NHR Mimetics. Virology, 377(1):170-183, 20 Jul 2008. PubMed ID: 18499210. 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.

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.

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.

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.

ORourke2012 Sara M. O'Rourke, Becky Schweighardt, Pham Phung, Kathryn A. Mesa, Aaron L. Vollrath, Gwen P. Tatsuno, Briana To, Faruk Sinangil, Kay Limoli, Terri Wrin, and Phillip W. Berman. Sequences in Glycoprotein gp41, the CD4 Binding Site, and the V2 Domain Regulate Sensitivity and Resistance of HIV-1 to Broadly Neutralizing Antibodies. J. Virol., 86(22):12105-12114, Nov 2012. PubMed ID: 22933284. 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.

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.

Pastore2007 Cristina Pastore, Rebecca Nedellec, Alejandra Ramos, Oliver Hartley, John L. Miamidian, Jacqueline D. Reeves, and Donald E. Mosier. Conserved Changes in Envelope Function during Human Immunodeficiency Virus Type 1 Coreceptor Switching. J. Virol., 81(15):8165-8179, Aug 2007. PubMed ID: 17507486. 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.

Penn-Nicholson2008 Adam Penn-Nicholson, Dong P. Han, Soon J. Kim, Hanna Park, Rais Ansari, David C. Montefiori, and Michael W. Cho. Assessment of Antibody Responses against gp41 in HIV-1-Infected Patients Using Soluble gp41 Fusion Proteins and Peptides Derived from M Group Consensus Envelope. Virology, 372(2):442-456, 15 Mar 2008. PubMed ID: 18068750. 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.

Perez2013 Lautaro G. Perez, Susan Zolla-Pazner, and David C. Montefiori. Antibody-Dependent, Fc-gamma-RI-Mediated Neutralization of HIV-1 in TZM-bl Cells Occurs Independently of Phagocytosis. J. Virol., 87(9):5287-5290, May 2013. PubMed ID: 23408628. 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.

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.

Pietzsch2010 John Pietzsch, Johannes F. Scheid, Hugo Mouquet, Michael S. Seaman, Christopher C. Broder, and Michel C. Nussenzweig. Anti-gp41 Antibodies Cloned from HIV-Infected Patients with Broadly Neutralizing Serologic Activity. J. Virol., 84(10):5032-5042, May 2010. PubMed ID: 20219932. Show all entries for this paper.

Pinto2019 Dora Pinto, Craig Fenwick, Christophe Caillat, Chiara Silacci, Serafima Guseva, Francois Dehez, Christophe Chipot, Sonia Barbieri, Andrea Minola, David Jarrossay, Georgia D. Tomaras, Xiaoying Shen, Agostino Riva, Maciej Tarkowski, Olivier Schwartz, Timothee Bruel, Jeremy Dufloo, Michael S. Seaman, David C. Montefiori, Antonio Lanzavecchia, Davide Corti, Giuseppe Pantaleo, and Winfried Weissenhorn. Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01. Cell Host Microbe, 26(5):623-637e8 doi, Nov 2019. PubMed ID: 31653484 Show all entries for this paper.

Platis2009 Dimitris Platis, Anastasios Maltezos, Julian K.-C. Ma, and Nikolaos E. Labrou. Combinatorial De Novo Design and Application of a Biomimetic Affinity Ligand for the Purification of Human Anti-HIV mAb 4E10 from Transgenic Tobacco. J. Mol. Recognit., 22(6):415-424, Nov-Dec 2009. PubMed ID: 19431140. 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.

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.

Polonis2008 Victoria R. Polonis, Bruce K. Brown, Andrew Rosa Borges, Susan Zolla-Pazner, Dimiter S. Dimitrov, Mei-Yun Zhang, Susan W. Barnett, Ruth M. Ruprecht, Gabriella Scarlatti, Eva-Maria Fenyö, David C. Montefiori, Francine E. McCutchan, and Nelson L. Michael. Recent Advances in the Characterization of HIV-1 Neutralization Assays for Standardized Evaluation of the Antibody Response to Infection and Vaccination. Virology, 375(2):315-320, 5 Jun 2008. PubMed ID: 18367229. 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.

Provine2012 Nicholas M. Provine, Valerie Cortez, Vrasha Chohan, and Julie Overbaugh. The Neutralization Sensitivity of Viruses Representing Human Immunodeficiency Virus Type 1 Variants of Diverse Subtypes from Early in Infection Is Dependent on Producer Cell, as Well as Characteristics of the Specific Antibody and Envelope Variant. Virology, 427(1):25-33, 25 May 2012. PubMed ID: 22369748. 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.

Quakkelaar2007 Esther D. Quakkelaar, Evelien M. Bunnik, Floris P. J. van Alphen, Brigitte D. M. Boeser-Nunnink, Ad C. van Nuenen, and Hanneke Schuitemaker. Escape of Human Immunodeficiency Virus Type 1 from Broadly Neutralizing Antibodies Is Not Associated with a Reduction of Viral Replicative Capacity In Vitro. Virology, 363(2):447-453, 5 Jul 2007. PubMed ID: 17355886. 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.

Rademeyer2016 Cecilia Rademeyer, Bette Korber, Michael S. Seaman, Elena E. Giorgi, Ruwayhida Thebus, Alexander Robles, Daniel J. Sheward, Kshitij Wagh, Jetta Garrity, Brittany R. Carey, Hongmei Gao, Kelli M. Greene, Haili Tang, Gama P. Bandawe, Jinny C. Marais, Thabo E. Diphoko, Peter Hraber, Nancy Tumba, Penny L. Moore, Glenda E. Gray, James Kublin, M. Juliana McElrath, Marion Vermeulen, Keren Middelkoop, Linda-Gail Bekker, Michael Hoelscher, Leonard Maboko, Joseph Makhema, Merlin L. Robb, Salim Abdool Karim, Quarraisha Abdool Karim, Jerome H. Kim, Beatrice H. Hahn, Feng Gao, Ronald Swanstrom, Lynn Morris, David C. Montefiori, and Carolyn Williamson. Features of Recently Transmitted HIV-1 Clade C Viruses that Impact Antibody Recognition: Implications for Active and Passive Immunization. PLoS Pathog., 12(7):e1005742, Jul 2016. PubMed ID: 27434311. Show all entries for this paper.

Rathinakumar2012 Ramesh Rathinakumar, Moumita Dutta, Ping Zhu, Welkin E. Johnson, and Kenneth H. Roux. Binding of Anti-Membrane-Proximal gp41 Monoclonal Antibodies to CD4-Liganded and -Unliganded Human Immunodeficiency Virus Type 1 and Simian Immunodeficiency Virus Virions. J. Virol., 86(3):1820-1831, Feb 2012. PubMed ID: 22090143. Show all entries for this paper.

Raviv2005 Yossef Raviv, Mathias Viard, Julian W. Bess, Jr., Elena Chertova, and Robert Blumenthal. Inactivation of Retroviruses with Preservation of Structural Integrity by Targeting the Hydrophobic Domain of the Viral Envelope. J. Virol., 79(19):12394-12400, Oct 2005. PubMed ID: 16160166. Show all entries for this paper.

Reardon2014 Patrick N. Reardon, Harvey Sage, S. Moses Dennison, Jeffrey W. Martin, Bruce R. Donald, S. Munir Alam, Barton F. Haynes, and Leonard D. Spicer. Structure of an HIV-1-Neutralizing Antibody Target, the Lipid-Bound gp41 Envelope Membrane Proximal Region Trimer. Proc. Natl. Acad Sci. U.S.A., 111(4):1391-1396, 28 Jan 2014. PubMed ID: 24474763. Show all entries for this paper.

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.

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.

Rujas2015 Edurne Rujas, Naveed Gulzar, Koldo Morante, Kouhei Tsumoto, Jamie K. Scott, José L. Nieva, and Jose M. M. Caaveiro. Structural and Thermodynamic Basis of Epitope Binding by Neutralizing and Nonneutralizing Forms of the Anti-HIV-1 Antibody 4E10. J. Virol., 89(23):11975-11989, Dec 2015. PubMed ID: 26378169. 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.

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.

Rusert2016 Peter Rusert, Roger D. Kouyos, Claus Kadelka, Hanna Ebner, Merle Schanz, Michael Huber, Dominique L. Braun, Nathanael Hozé, Alexandra Scherrer, Carsten Magnus, Jacqueline Weber, Therese Uhr, Valentina Cippa, Christian W. Thorball, Herbert Kuster, Matthias Cavassini, Enos Bernasconi, Matthias Hoffmann, Alexandra Calmy, Manuel Battegay, Andri Rauch, Sabine Yerly, Vincent Aubert, Thomas Klimkait, Jürg Böni, Jacques Fellay, Roland R. Regoes, Huldrych F. Günthard, Alexandra Trkola, and Swiss HIV Cohort Study. Determinants of HIV-1 Broadly Neutralizing Antibody Induction. Nat. Med., 22(11):1260-1267, Nov 2016. PubMed ID: 27668936. 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.

Sanchez-Martinez2006 Silvia Sánchez-Martínez, Maier Lorizate, Hermann Katinger, Renate Kunert, and José L. Nieva. Membrane Association and Epitope Recognition by HIV-1 Neutralizing Anti-gp41 2F5 and 4E10 Antibodies. AIDS Res. Hum. Retroviruses, 22(10):998-1006, Oct 2006. PubMed ID: 17067270. 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.

Sather2010 D. Noah Sather and Leonidas Stamatatos. Epitope Specificities of Broadly Neutralizing Plasmas from HIV-1 Infected Subjects. Vaccine, 28 Suppl 2:B8-B12, 26 May 2010. PubMed ID: 20510750. 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.

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.

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.

Scherer2010 Erin M. Scherer, Daniel P. Leaman, Michael B. Zwick, Andrew J. McMichael, and Dennis R. Burton. Aromatic Residues at the Edge of the Antibody Combining Site Facilitate Viral Glycoprotein Recognition through Membrane Interactions. Proc. Natl. Acad. Sci. U.S.A., 107(4):1529-1534, 26 Jan 2010. PubMed ID: 20080706. Show all entries for this paper.

Schief2009 William R. Schief, Yih-En Andrew Ban, and Leonidas Stamatatos. Challenges for Structure-Based HIV Vaccine Design. Curr. Opin. HIV AIDS, 4(5):431-440, Sep 2009. PubMed ID: 20048708. Show all entries for this paper.

Schultz2018 Anke Schultz, Anja Germann, Martina Fuss, Marcella Sarzotti-Kelsoe, Daniel A. Ozaki, David C. Montefiori, Heiko Zimmermann, and Hagen von Briesen. Validation of an Automated System for Aliquoting of HIV-1 Env-Pseudotyped Virus Stocks. PLoS One, 13(1):1-20, Jan 2018. PubMed ID: 29300769. Show all entries for this paper.

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.

Scott2015 Yanille M. Scott, Seo Young Park, and Charlene S. Dezzutti. Broadly Neutralizing Anti-HIV Antibodies Prevent HIV Infection of Mucosal Tissue Ex Vivo. Antimicrob. Agents Chemother., 60(2):904-912, Feb 2016. PubMed ID: 26596954. 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.

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.

Shen2010a Ruizhong Shen, Ernesto R. Drelichman, Diane Bimczok, Christina Ochsenbauer, John C. Kappes, Jamie A. Cannon, Daniela Tudor, Morgane Bomsel, Lesley E. Smythies, and Phillip D. Smith. GP41-Specific Antibody Blocks Cell-Free HIV Type 1 Transcytosis through Human Rectal Mucosa and Model Colonic Epithelium. J. Immunol., 184(7):3648-3655, 1 Apr 2010. PubMed ID: 20208001. Show all entries for this paper.

Shi2010 Wuxian Shi, Jen Bohon, Dong P. Han, Habtom Habte, Yali Qin, Michael W. Cho, and Mark R. Chance. Structural Characterization of HIV gp41 with the Membrane-Proximal External Region. J. Biol. Chem., 285(31):24290-24298, 30 Jul 2010. PubMed ID: 20525690. 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.

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.

Song2009 Likai Song, Zhen-Yu J. Sun, Kate E. Coleman, Michael B. Zwick, Johannes S. Gach, Jia-huai Wang, Ellis L. Reinherz, Gerhard Wagner, and Mikyung Kim. Broadly Neutralizing Anti-HIV-1 Antibodies Disrupt a Hinge-Related Function of gp41 at the Membrane Interface. Proc. Natl. Acad. Sci. U.S.A., 106(22):9057-9062, 2 Jun 2009. PubMed ID: 19458040. 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.

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.

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.

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.

Steckbeck2010 Jonathan D. Steckbeck, Chengqun Sun, Timothy J. Sturgeon, and Ronald C. Montelaro. Topology of the C-Terminal Tail of HIV-1 gp41: Differential Exposure of the Kennedy Epitope on Cell and Viral Membranes. PLoS One, 5(12):e15261, 2010. PubMed ID: 21151874. 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.

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.

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.

Sun2008 Zhen-Yu J. Sun, Kyoung Joon Oh, Mikyung Kim, Jessica Yu, Vladimir Brusic, Likai Song, Zhisong Qiao, Jia-huai Wang, Gerhard Wagner, and Ellis L. Reinherz. HIV-1 Broadly Neutralizing Antibody Extracts Its Epitope from a Kinked gp41 Ectodomain Region on the Viral Membrane. Immunity, 28(1):52-63, Jan 2008. PubMed ID: 18191596. 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.

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.

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.

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.

Tomaras2010 Georgia D. Tomaras and Barton F. Haynes. Strategies for Eliciting HIV-1 Inhibitory Antibodies. Curr. Opin. HIV AIDS, 5(5):421-427, Sep 2010. PubMed ID: 20978384. 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.

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.

Tudor2009 D. Tudor, M. Derrien, L. Diomede, A.-S. Drillet, M. Houimel, C. Moog, J.-M. Reynes, L. Lopalco, and M. Bomsel. HIV-1 gp41-Specific Monoclonal Mucosal IgAs Derived from Highly Exposed but IgG-Seronegative Individuals Block HIV-1 Epithelial Transcytosis and Neutralize CD4+ Cell Infection: An IgA Gene and Functional Analysis. Mucosal Immunol., 2(5):412-426, Sep 2009. PubMed ID: 19587640. 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.

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.

Veiga2009 Ana S. Veiga, Leonard K. Pattenden, Jordan M. Fletcher, Miguel A. R. B. Castanho, and Marie Isabel Aguilar. Interactions of HIV-1 Antibodies 2F5 and 4E10 with a gp41 Epitope Prebound to Host and Viral Membrane Model Systems. ChemBioChem, 10(6):1032-1044, 17 Apr 2009. PubMed ID: 19283693. Show all entries for this paper.

Venditto2013 Vincent J. Venditto, Douglas S. Watson, Michael Motion, David Montefiori, and Francis C. Szoka, Jr. Rational Design of Membrane Proximal External Region Lipopeptides Containing Chemical Modifications for HIV-1 Vaccination. Clin Vaccine Immunol, 20(1):39-45, Jan 2013. PubMed ID: 23114698. Show all entries for this paper.

Vincent2008 Nadine Vincent, Amadou Kone, Blandine Chanut, Frédéric Lucht, Christian Genin, and Etienne Malvoisin. Antibodies Purified from Sera of HIV-1-Infected Patients by Affinity on the Heptad Repeat Region 1/Heptad Repeat Region 2 Complex of gp41 Neutralize HIV-1 Primary Isolates. AIDS, 22(16):2075-2085, 18 Oct 2008. PubMed ID: 18832871. 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.

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.

Walker2009b Laura M. Walker, Diana R. Bowley, and Dennis R. Burton. Efficient Recovery of High-Affinity Antibodies from a Single-Chain Fab Yeast Display Library. J. Mol. Biol., 389(2):365-375, 5 Jun 2009. PubMed ID: 19376130. 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.

Wallace2009 Aaron Wallace and Leonidas Stamatatos. Introduction of Exogenous Epitopes in the Variable Regions of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein: Effect on Viral Infectivity and the Neutralization Phenotype. J. Virol., 83(16):7883-7893, Aug 2009. PubMed ID: 19494007. Show all entries for this paper.

Wang2003 Lai-Xi Wang. Bioorganic Approaches towards HIV Vaccine Design. Curr. Pharm. Des., 9(22):1771-87, 2003. PubMed ID: 12871196. Show all entries for this paper.

Wang2011a Ji Wang, Pei Tong, Lu Lu, Leilei Zhou, Liling Xu, Shibo Jiang, and Ying-hua Chen. HIV-1 gp41 Core with Exposed Membrane-Proximal External Region Inducing Broad HIV-1 Neutralizing Antibodies. PLoS One, 6(3):e18233, 2011. PubMed ID: 21483871. Show all entries for this paper.

Wang2011b Suting Wang, Jianhui Nie, and Youchun Wang. Comparisons of the genetic and neutralization properties of HIV-1 subtype C and CRF07/08_BC env molecular clones isolated from infections in China. Virus Res, 155(1):137-46 doi, Jan 2011. PubMed ID: 20875470 Show all entries for this paper.

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.

Wang2013 Wenbo Wang, Jianhui Nie, Courtney Prochnow, Carolyn Truong, Zheng Jia, Suting Wang, Xiaojiang S. Chen, and Youchun Wang. A Systematic Study of the N-Glycosylation Sites of HIV-1 Envelope Protein on Infectivity and Antibody-Mediated Neutralization. Retrovirology, 10:14, 2013. PubMed ID: 23384254. 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.

Wen2010 Michael Wen, Reetakshi Arora, Huiqiang Wang, Lihong Liu, Jason T. Kimata, and Paul Zhou. GPI-Anchored Single Chain Fv---An Effective Way To Capture Transiently-Exposed Neutralization Epitopes on HIV-1 Envelope Spike. Retrovirology, 7:79, 2010. PubMed ID: 20923574. 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.

Wibmer2017 Constantinos Kurt Wibmer, Jason Gorman, Gabriel Ozorowski, Jinal N. Bhiman, Daniel J. Sheward, Debra H. Elliott, Julie Rouelle, Ashley Smira, M. Gordon Joyce, Nonkululeko Ndabambi, Aliaksandr Druz, Mangai Asokan, Dennis R. Burton, Mark Connors, Salim S. Abdool Karim, John R. Mascola, James E. Robinson, Andrew B. Ward, Carolyn Williamson, Peter D. Kwong, Lynn Morris, and Penny L. Moore. Structure and Recognition of a Novel HIV-1 gp120-gp41 Interface Antibody that Caused MPER Exposure through Viral Escape. PLoS Pathog., 13(1):e1006074, Jan 2017. PubMed ID: 28076415. 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.

Witt2017 Kristen C. Witt, Luis Castillo-Menendez, Haitao Ding, Nicole Espy, Shijian Zhang, John C. Kappes, and Joseph Sodroski. Antigenic Characterization of the Human Immunodeficiency Virus (HIV-1) Envelope Glycoprotein Precursor Incorporated into Nanodiscs. PLoS One, 12(2):e0170672, 2017. PubMed ID: 28151945. Show all entries for this paper.

Xu2001 W. Xu, B. A. Smith-Franklin, P. L. Li, C. Wood, J. He, Q. Du, G. J. Bhat, C. Kankasa, H. Katinger, L. A. Cavacini, M. R. Posner, D. R. Burton, T. C. Chou, and R. M. Ruprecht. Potent neutralization of primary human immunodeficiency virus clade C isolates with a synergistic combination of human monoclonal antibodies raised against clade B. J Hum Virol, 4(2):55--61, Mar-Apr 2001. PubMed ID: 11437315. Show all entries for this paper.

Xu2002 Weidong Xu, Regina Hofmann-Lehmann, Harold M. McClure, and Ruth M. Ruprecht. Passive Immunization with Human Neutralizing Monoclonal Antibodies: Correlates of Protective Immunity against HIV. Vaccine, 20(15):1956-1960, 6 May 2002. PubMed ID: 11983253. 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.

Yang2012 Lifei Yang, Yufeng Song, Xiaomin Li, Xiaoxing Huang, Jingjing Liu, Heng Ding, Ping Zhu, and Paul Zhou. HIV-1 Virus-Like Particles Produced by Stably Transfected Drosophila S2 Cells: A Desirable Vaccine Component. J. Virol., 86(14):7662-7676, Jul 2012. PubMed ID: 22553333. Show all entries for this paper.

Yang2013 Guang Yang, T. Matt Holl, Yang Liu, Yi Li, Xiaozhi Lu, Nathan I. Nicely, Thomas B. Kepler, S. Munir Alam, Hua-Xin Liao, Derek W. Cain, Leonard Spicer, John L. VandeBerg, Barton F. Haynes, and Garnett Kelsoe. Identification of Autoantigens Recognized by the 2F5 and 4E10 Broadly Neutralizing HIV-1 Antibodies. J. Exp. Med., 210(2):241-256, 11 Feb 2013. PubMed ID: 23359068. Show all entries for this paper.

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.

Yang2018 Zheng Yang, Xi Liu, Zehua Sun, Jingjing Li, Weiguo Tan, Weiye Yu, and Meiyun Zhang. Identification of a HIV gp41-Specific Human Monoclonal Antibody with Potent Antibody-Dependent Cellular Cytotoxicity. Front. Immunol., 9:2613, 2018. PubMed ID: 30519238. Show all entries for this paper.

Ye2006 Ling Ye, Yuliang Sun, Jianguo Lin, Zhigao Bu, Qingyang Wu, Shibo Jiang, David A. Steinhauer, Richard W. Compans, and Chinglai Yang. Antigenic Properties of a Transport-Competent Influenza HA/HIV Env Chimeric Protein. Virology, 352(1):74-85, 15 Aug 2006. PubMed ID: 16725170. Show all entries for this paper.

Yee2011 Michael Yee, Krystyna Konopka, Jan Balzarini, and Nejat Düzgüneş. Inhibition of HIV-1 Env-Mediated Cell-Cell Fusion by Lectins, Peptide T-20, and Neutralizing Antibodies. Open Virol. J., 5:44-51, 2011. PubMed ID: 21660189. Show all entries for this paper.

Yu2015 Yongjiao Yu, Lu Fu, Yuhua Shi, Shanshan Guan, Lan Yang, Xin Gong, He Yin, Xiaoqiu He, Dongni Liu, Ziyu Kuai, Yaming Shan, Song Wang, and Wei Kong. Elicitation of HIV-1 Neutralizing Antibodies by Presentation of 4E10 and 10E8 Epitopes on Norovirus P particles. Immunol. Lett., 168(2):271-278, Dec 2015. PubMed ID: 26455781. 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.

Zhang2006a Mei-Yun Zhang, Vidita Choudhry, Igor A. Sidorov, Vladimir Tenev, Bang K Vu, Anil Choudhary, Hong Lu, Gabriela M. Stiegler, Hermann W. D. Katinger, Shibo Jiang, Christopher C. Broder, and Dimiter S. Dimitrov. Selection of a Novel gp41-Specific HIV-1 Neutralizing Human Antibody by Competitive Antigen Panning. J. Immunol. Methods, 317(1-2):21-30, 20 Dec 2006. PubMed ID: 17078964. Show all entries for this paper.

Zhang2007 Mei-Yun Zhang and Dimiter S. Dimitrov. Novel Approaches for Identification of Broadly Cross-Reactive HIV-1 Neutralizing Human Monoclonal Antibodies and Improvement of Their Potency. Curr. Pharm. Des., 13(2):203-212, 2007. PubMed ID: 17269928. Show all entries for this paper.

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.

Zhang2014 Jinsong Zhang, S. Munir Alam, Hilary Bouton-Verville, Yao Chen, Amanda Newman, Shelley Stewart, Frederick H. Jaeger, David C. Montefiori, S. Moses Dennison, Barton F. Haynes, and Laurent Verkoczy. Modulation of Nonneutralizing HIV-1 gp41 Responses by an MHC-Restricted TH Epitope Overlapping Those of Membrane Proximal External Region Broadly Neutralizing Antibodies. J. Immunol., 192(4):1693-1706, 15 Feb 2014. PubMed ID: 24465011. Show all entries for this paper.

Zhang2019a Lei Zhang, Adriana Irimia, Lingling He, Elise Landais, Kimmo Rantalainen, Daniel P. Leaman, Thomas Vollbrecht, Armando Stano, Daniel I. Sands, Arthur S. Kim, IAVI Protocol G Investigators, Pascal Poignard, Dennis R. Burton, Ben Murrell, Andrew B. Ward, Jiang Zhu, Ian A. Wilson, and Michael B. Zwick. An MPER Antibody Neutralizes HIV-1 Using Germline Features Shared Among Donors. Nat. Commun., 10(1):5389, 26 Nov 2019. PubMed ID: 31772165. 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.

Zhou2010a Nannan Zhou, Li Fan, Hsu-Tso Ho, Beata Nowicka-Sans, Yongnian Sun, Yingjie Zhu, Yanhua Hu, Brian McAuliffe, Burt Rose, Hua Fang, Tao Wang, John Kadow, Mark Krystal, Louis Alexander, Richard Colonno, and Pin-Fang Lin. Increased Sensitivity of HIV Variants Selected by Attachment Inhibitors to Broadly Neutralizing Antibodies. Virology, 402(2):256-261, 5 Jul 2010. PubMed ID: 20400170. Show all entries for this paper.

Zwick2001b M. B. Zwick, A. F. Labrijn, M. Wang, C. Spenlehauer, E. O. Saphire, J. M. Binley, J. P. Moore, G. Stiegler, H. Katinger, D. R. Burton, and P. W. Parren. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol., 75(22):10892--905, Nov 2001. URL: http://jvi.asm.org/cgi/content/full/75/22/10892. PubMed ID: 11602729. Show all entries for this paper.

Zwick2001c M. B. Zwick, M. Wang, P. Poignard, G. Stiegler, H. Katinger, D. R. Burton, and P. W. Parren. Neutralization synergy of human immunodeficiency virus type 1 primary isolates by cocktails of broadly neutralizing antibodies. J. Virol., 75(24):12198--208, Dec 2001. URL: http://jvi.asm.org/cgi/content/full/75/24/12198. PubMed ID: 11711611. Show all entries for this paper.

Zwick2005 Michael B. Zwick, Richard Jensen, Sarah Church, Meng Wang, Gabriela Stiegler, Renate Kunert, Hermann Katinger, and Dennis R. Burton. Anti-Human Immunodeficiency Virus Type 1 (HIV-1) Antibodies 2F5 and 4E10 Require Surprisingly Few Crucial Residues in the Membrane-Proximal External Region of Glycoprotein gp41 to Neutralize HIV-1. J. Virol., 79(2):1252-1261, Jan 2005. PubMed ID: 15613352. Show all entries for this paper.

Joshi2020 Vinita R. Joshi, Ruchi M. Newman, Melissa L. Pack, Karen A. Power, James B. Munro, Ken Okawa, Navid Madani, Joseph G. Sodroski, Aaron G. Schmidt, and Todd M. Allen. Gp41-targeted antibodies restore infectivity of a fusion-deficient HIV-1 envelope glycoprotein. PLoS Pathog, 16(5):e1008577 doi, May 2020. PubMed ID: 32392227 Show all entries for this paper.

Hutchinson2019 Jennie M. Hutchinson, Kathryn A. Mesa, David L. Alexander, Bin Yu, Sara M. O'Rourke, Kay L. Limoli, Terri Wrin, Steven G. Deeks, and Phillip W. Berman. Unusual Cysteine Content in V1 Region of gp120 from an Elite Suppressor That Produces Broadly Neutralizing Antibodies. Front. Immunol., 10:1021, 2019. PubMed ID: 31156622. Show all entries for this paper.

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Displaying record number 2119

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MAb ID	polyclonal
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	CRF01_AE
Ab Type	gp120 C1, gp120 C2
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	neutralization, vaccine-induced immune responses

Vaccine Details

Vaccine type	peptide
Vaccine strain	other
Adjuvant	Complete Freund's Adjuvant (CFA), Incomplete Freund's Adjuvant (IFA)

Notes

Showing 1 of 1 note.

• Mice were immunized with synthetic peptides representing aa 93-112 (C1E1 and C1E2) of C1 region and 218-239 (C2E) of C2 region. Mice immunized with C1E1 and C1E2 developed low titer Ab responses, while mice immunized with C2E induced higher titer Ab responses in a dose dependent matter. C2E immunized mouse antisera neutralized CRF01_AE laboratory strain NP03. Sreepian2009 (neutralization, vaccine-induced immune responses)

References

Showing 1 of 1 reference.

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.

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Displaying record number 2120

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MAb ID	C2EB5
HXB2 Location	Env	Env Epitope Map
Author Location	Env
Epitope
Subtype	CRF01_AE
Ab Type	gp120 C2
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords	antibody generation, binding affinity, neutralization, variant cross-reactivity

Vaccine Details

Vaccine type	peptide
Vaccine strain	other
Adjuvant	Complete Freund's Adjuvant (CFA), Incomplete Freund's Adjuvant (IFA)

Notes

Showing 1 of 1 note.

• C2EB5: This MAb was isolated from mice immunized with a peptide from C2 region. C2EB5 neutralized clades A, B, C, D and CRF01_AE. The MAb bound to clade B viruses with lowest affinity and to clade C with highest, which correlated with the neutralizing activity. It also bound to clade A, C, D and CRF01_AE. Sreepian2009 (antibody generation, neutralization, variant cross-reactivity, binding affinity)

References

Showing 1 of 1 reference.

Isolation 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.

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