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Displaying record number 395

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MAb ID	polyclonal
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120( MN)
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L (MN ALA-1)
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords

Notes

Showing 1 of 1 note.

40% of antibody in serum that can bind to native viral proteins on MN-infected cells can be blocked by the peptide RKRIHIGPGRAFYTT, which can also block 75-95% of the complement activation on HIV infected cells. Spear1994

References

Showing 1 of 1 reference.

Spear1994 G. T. Spear, D. M. Takefman, S. Sharpe, M. Ghassemi, and S. Zolla-Pazner. Antibodies to the HIV-1 V3 Loop in Serum from Infected Persons Contribute a Major Proportion of Immune Effector Functions Including Complement Activation, Antibody Binding, and Neutralization. Virology, 204:609-615, 1994. PubMed ID: 7941328. Show all entries for this paper.

Displaying record number 455

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MAb ID	10F10
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120( MN)
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	mouse(IgG1)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	peptide
Vaccine strain	B clade MN
Vaccine component	gp120

Notes

Showing 1 of 1 note.

2C4: Putative epitope lies within IHIGPGRAFYT -- generated by multi-epitope polypeptide immunization -- recognize MN and SC (TRSIHIGPGRAFYTT) peptides, lower affinity for SF2. Duarte1994

References

Showing 1 of 1 reference.

Duarte1994 C. A. Duarte, M. Montero, A. Seralena, R. Valdes, V. Jimenez, J. Benitez, E. Narciandi, J. Madrazo, G. Padron, G. Sanchez, G. Gilljam, K. Persson, S. Ojeda, A. Caballero, A. Miranda, M. C. Dominguez, B. Wahren, and A. Menendez. Multiepitope Polypeptide of the HIV-1 Envelope Induces Neutralizing Monoclonal Antibodies against V3 Loop. AIDS Res. Hum. Retroviruses, 10:235-243, 1994. PubMed ID: 7517147. Show all entries for this paper.

Displaying record number 456

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MAb ID	2C4
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120( MN)
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L (MN)
Species (Isotype)	mouse(IgG2a)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	peptide
Vaccine strain	B clade MN

Notes

Showing 1 of 1 note.

2C4: Putative epitope lies within IHIGPGRAFYT -- neutralizes MN, not IIIB and SF2 -- generated by multi-epitope polypeptide immunization -- recognize MN and SC (TRSIHIGPGRAFYTT) peptides, lower affinity for SF2. Duarte1994

References

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Displaying record number 475

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MAb ID	412-D (412-10D, 412, 412D)
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120( MN)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Subtype	B
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	L
Species (Isotype)	human(IgG1κ)
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, antibody sequence, binding affinity, complement, kinetics, review, subtype comparisons, vaccine antigen design, variant cross-reactivity

Notes

Showing 12 of 12 notes.

412-D: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:3-33*01, IGHD:3-10, D-RF:1, 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)
412-D: Called 412: 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. Gorny2004 (antibody binding site)
412-D: 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. Gorny2003 (review)
412-D: 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 -- 412-D showed limited reactivity. Nyambi2000 (subtype comparisons)
412-D: MAb peptide-reactivity pattern clustered with immunological related MAbs: 391.5, 412 and 418, all selected with MN V3 peptide -- the core amino acids HIGPGR tended to be critical for reactivity in this group. Zolla-Pazner1999a (antibody binding site)
412-D: Review of clade specificity and anti-V3 HIV-1-Abs. Zolla-Pazner1999b (review, subtype comparisons)
412-D: 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 -- 412-D was bound only to B clade virions and to D clade MAL. Nyambi1998 (subtype comparisons)
412-D: Kinetic parameters were measured, and the association rates were similar, but dissociation rate constants were quite variable for V3 MAbs, 412-D has a relatively fast dissociation, thus low affinity among V3 MAbs. Gorny1998 (kinetics)
412-D: Called 412 -- The tip of the V3 loop was presented in a mucin backbone -- higher valency correlates with higher affinity constant. Fontenot1995 (vaccine antigen design, binding affinity)
412-D: Called 412-10D -- relatively rapid dissociation and weak homologous neutralization. VanCott1994 (binding affinity)
412-D: Mediated deposition of complement component C3 on HIV infected cells, enhanced by second Ab binding, rabbit anti-human IgG. Spear1993 (complement)
412-D: Neutralizes MN, does not bind SF2 or HXB2 -- not reactive with hexa or heptapeptides by Pepscan. Gorny1993 (antibody generation, variant cross-reactivity)

References

Showing 12 of 12 references.

Isolation 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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Displaying record number 1506

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MAb ID	D19
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120 (V3)( MN)
Research Contact	Paolo Lusso, Human Virology, San Raffaele Scientific Institute, Milan, Italy. paolo@hsr.it
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Ab Type	gp120 CD4i, gp120 V3 // V3 glycan (V3g)
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, genital and mucosal immunity, isotype switch, neutralization, subtype comparisons, variant cross-reactivity

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade BH8
Vaccine component	gp140

Notes

Showing 4 of 4 notes.

D19: Spatial relationships between V1V2 and V3 and the mechanisms of epitope masking were studied using mAbs 2182 and D19. Deletion of V1V2 region greatly enhanced neutralization by both mAbs. Using a functional strategy based on Env complementation system, it was shown that the influence of V1V2 on accessibility of the 2182 and D19 epitopes on V3 is manifested within the same promoter, rather than between adjacent promoters in the trimer. Liu2011b (antibody binding site)
D19: Several IgG MAbs were isotype switched to IgA and tested for their abilities to generate immune complexes with HIV-1 and be excreted from polarized epithelial cells from the basolateral to the apical surface via polymeric Ig receptor (pIgR) binding. IgA D19 was able to excrete HIV but it had lower level of binding to the virus, and as immune complex to the pIgR, than D10 and D47 MAbs. These results show that IgA Abs have potential to excrete HIV from mucosal lamina propria thus decreasing the viral burden and access to susceptible cells. Wright2008 (genital and mucosal immunity, isotype switch)
D19: By isotype switching, IgG and IgA variants of D19 were produced. Both D19 IgA and IgG neutralized virus in conventional neutralization assays, however, IgA performed better. D19 IgA was also internalized into the cells by the polymeric Ig receptor (pIgR) and showed capability of intracellular neutralization of HIV-1, while D19 IgG showed no such activity. Huang2005a (genital and mucosal immunity, isotype switch, neutralization)
D19: The epitope for D19 is conserved and embedded in V3. D19 is unique because for R5 viruses, it was cryptic and did not bind without exposure to sCD4, but for X4 and R5X4 isolates it was constitutively exposed. It had a similar overlapping binding region with MAbs 447-52D, B4e8, and 268-D, but different reactivity patterns and fine specificity; D19 binding to monomeric gp120 was independent of sCD4, the dependence was only seen in the context of native oligomeric Env. D19 reacted with 23/29 B clade Envs, but to only 2/14 viruses from other clades: one A and one F, but no C, D or E clade strains. D19 can neutralize X4 and R5X4 isolates, but could only neutralize R5 isolates in the presence of sCD4. The authors suggest that a more exposed V3 loop may facilitate CXCR4 coreceptor usage, but that this phenotype is limited in vivo by neutralizing antibodies until the onset of progressive disease. Lusso2005 (antibody binding site, antibody generation, variant cross-reactivity, subtype comparisons)

References

Showing 4 of 4 references.

Isolation 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.

Huang2005a Yung T. Huang, Alison Wright, Xing Gao, Lesya Kulick, Huimin Yan, and Michael E. Lamm. Intraepithelial Cell Neutralization of HIV-1 Replication by IgA. J. Immunol., 174(8):4828-4835, 15 Apr 2005. PubMed ID: 15814709. Show all entries for this paper.

Liu2011b Li Liu, Raffaello Cimbro, Paolo Lusso, and Edward A. Berger. Intraprotomer Masking of Third Variable loop (V3) Epitopes by the First and Second Variable Loops (V1V2) within the Native HIV-1 Envelope Glycoprotein Trimer. Proc. Natl. Acad. Sci. U.S.A, 108(50):20148-20153, 13 Dec 2011. PubMed ID: 22128330. Show all entries for this paper.

Wright2008 Alison Wright, Michael E. Lamm, and Yung T. Huang. Excretion of Human Immunodeficiency Virus Type 1 through Polarized Epithelium by Immunoglobulin A. J. Virol., 82(23):11526-11535, Dec 2008. PubMed ID: 18829757. Show all entries for this paper.

Displaying record number 2894

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MAb ID	CH22
HXB2 Location	gp160(304-320) DNA(7134..7184)	gp160 Epitope Map
Author Location	gp120
Epitope	`RKRIHIGPGRAFYTT`	Epitope Alignment
Subtype	B, CRF01_AE
Ab Type	gp120 V3 // V3 glycan (V3g)
Neutralizing	yes
Species (Isotype)	human(IgG1)
Patient
Immunogen	vaccine
Country	Thailand
Keywords	ADCC, antibody binding site, antibody generation, antibody polyreactivity, genital and mucosal immunity, immunoprophylaxis, review, SIV, structure, vaccine-induced immune responses

Notes

Showing 5 of 5 notes.

CH22: 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. Three non-nAb combinations were assayed: 7B2/CH58/CH90, 7B2/CH58/CH22, and F240/M785-U1/N10-U1; ; A32, 7B2, CH90, and CH22 contained the AAA mutations (S298A, E333A, and K334A) optimized for binding to Fc RIIIa (CD16) and to augment antibody ADCC activity. Cheeseman2017 (genital and mucosal immunity, immunoprophylaxis)
CH22: In a passive antibody infusion-rhesus macaque challenge model, non-neutralizing mAbs were seen to limit virus acquisition and infection. 7B2, which recognizes both virus particles and infected cells as well as A32, recognizing only infected cells, together were able to decrease transmitted/founder viruses in in vivo rectal mucosal high-dose transmission of SHIV-BaL by 50% though they did not prevent infection or reduce viral load. CH22, a V3-loop bNAb was able to eliminate all transmission of SHIV by intra-rectal route in 4/6 subjects. Santra2015 (genital and mucosal immunity, SIV, structure)
CH22: A panel of Env-specific mAbs was isolated from 6 HIV1-infected lactating women. Antibodies in colostrum may help prevent mucosal infection of the infant, so this study aimed to define milk IgGs for future vaccination strategies to reduce HIV transmission during lactation. Despite the high rate of VH 1-69 usage among colostrum Env specific B cells, it did not correlate with distinct gp120 epitope specificity or function. CH22 was compared to the newly-derived mAbs; it had no cross-reactivity with gut bacteria, and tested negative in onje test of autoreactivity. Jeffries2016 (antibody polyreactivity)
CH22: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. CH22, generated by a vaccine recipient of phase II RV135 clinical trial, is discussed as the V3 region-targeting, neutralizing anti-gp120 mAb exhibiting ADCC activity and having a linear epitope. Pollara2013 (ADCC, review)
CH22: NAb response was compared in 2 HIV-1 vaccine efficacy trials in which either partial protection (RV144) or no protection (Vax003) was seen. The peak NAb response in RV144 was substantially weaker than the peak response in Vax003, suggesting that either weak neutralizing antibody responses can be partially protective in low-risk heterosexual populations or that the modest efficacy seen in RV144 was mediated by other immune responses. MAb CH22 was vaccine-induced antibody, isolated from subject T141485 in RV144 trial. CH22 used V-gene segment, had no detectable neutralizing activity against tier 2 viruses, but neutralized subtype B tier 1 viruses, and mapped to V3 linear peptide KRIHIGPGRAFYTT. Montefiori2012 (antibody binding site, antibody generation, vaccine-induced immune responses)

References

Showing 5 of 5 references.

Isolation Paper
Montefiori2012 David C. Montefiori, Chitraporn Karnasuta, Ying Huang, Hasan Ahmed, Peter Gilbert, Mark S. de Souza, Robert McLinden, Sodsai Tovanabutra, Agnes Laurence-Chenine, Eric Sanders-Buell, M. Anthony Moody, Mattia Bonsignori, Christina Ochsenbauer, John Kappes, Haili Tang, Kelli Greene, Hongmei Gao, Celia C. LaBranche, Charla Andrews, Victoria R. Polonis, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayaphan, Jaranit Kaewkungwal, Steve G. Self, Phillip W. Berman, Donald Francis, Faruk Sinangil, Carter Lee, Jim Tartaglia, Merlin L. Robb, Barton F. Haynes, Nelson L. Michael, and Jerome H. Kim. Magnitude and Breadth of the Neutralizing Antibody Response in the RV144 and Vax003 HIV-1 Vaccine Efficacy Trials. J. Infect. Dis., 206(3):431-441, 1 Aug 2012. PubMed ID: 22634875. 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.

Jeffries2016 T. L. Jeffries, Jr., C. R. Sacha, J. Pollara, J. Himes, F. H. Jaeger, S. M. Dennison, E. McGuire, E. Kunz, J. A. Eudailey, A. M. Trama, C. LaBranche, G. G. Fouda, K. Wiehe, D. C. Montefiori, B. F. Haynes, H.-X. Liao, G. Ferrari, S. M. Alam, M. A. Moody, and S. R. Permar. The Function and Affinity Maturation of HIV-1 gp120-Specific Monoclonal Antibodies Derived from Colostral B Cells. Mucosal. Immunol., 9(2):414-427, Mar 2016. PubMed ID: 26242599. 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.

Santra2015 Sampa Santra, Georgia D Tomaras, Ranjit Warrier, Nathan I. Nicely, Hua-Xin Liao, Justin Pollara, Pinghuang Liu, S. Munir Alam, Ruijun Zhang, Sarah L. Cocklin, Xiaoying Shen, Ryan Duffy, Shi-Mao Xia, Robert J. Schutte, Charles W. Pemble, IV, S. Moses Dennison, Hui Li, Andrew Chao, Kora Vidnovic, Abbey Evans, Katja Klein, Amit Kumar, James Robinson, Gary Landucci, Donald N. Forthal, David C. Montefiori, Jaranit Kaewkungwal, Sorachai Nitayaphan, Punnee Pitisuttithum, Supachai Rerks-Ngarm, Merlin L. Robb, Nelson L. Michael, Jerome H. Kim, Kelly A. Soderberg, Elena E. Giorgi, Lily Blair, Bette T. Korber, Christiane Moog, Robin J. Shattock, Norman L. Letvin, Joern E. Schmitz, M. A. Moody, Feng Gao, Guido Ferrari, George M. Shaw, and Barton F. Haynes. Human Non-Neutralizing HIV-1 Envelope Monoclonal Antibodies Limit the Number of Founder Viruses during SHIV Mucosal Infection in Rhesus Macaques. PLoS Pathog., 11(8):e1005042, Aug 2015. PubMed ID: 26237403. Show all entries for this paper.