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Displaying record number 847
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MAb ID |
Z13 |
HXB2 Location |
Env(671-676) DNA(8235..8252) |
Env Epitope Map
|
Author Location |
gp41(671-676 MN) |
Epitope |
NWFDIT
|
Epitope Alignment
|
Subtype |
B |
Ab Type |
gp41 MPER (membrane proximal external region) |
Neutralizing |
P View neutralization details |
Contacts and Features |
View contacts and features |
Species
(Isotype)
|
human(IgG1κ) |
Patient |
FDA2 |
Immunogen |
HIV-1 infection |
Keywords |
antibody binding site, antibody generation, antibody interactions, antibody sequence, assay or method development, binding affinity, broad neutralizer, contact residues, effector function, escape, germline, neutralization, review, SIV, structure, subtype comparisons, vaccine antigen design, variant cross-reactivity |
Notes
Showing 38 of
38 notes.
-
Z13: 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. The germline gene usage of PGZL1 was compared with other MPER antibodies: 4E10, VRC42.01, 10E8, DH511.2, DH517, Z13, and 2F5.
Zhang2019a
(neutralization, structure, contact residues, germline)
-
Z13: MHC Class II-restricted TH activation was shown to be a key determinant controlling nonneutralizing MPER Ab responses. TH H2d epitope KWASLWNWF, partially overlapping 2F5 MPER epitope, was required for MPER Ab induction.
Zhang2014
-
Z13: 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. Z13 is an MPER Ab, with breadth <20%, IC50 not reported, and its unique feature listed is WNWFDITN-peptide recognition derived from phage display.
Kwong2013
(review)
-
Z13: 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 are 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. Z13 has been referred as a bnAb directed to MPER.
Venditto2013
(antibody interactions, vaccine antigen design)
-
Z13: 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, WINWFDITN loop, Z13 class, Z13 family.
Kwong2012
(review, structure, broad neutralizer)
-
Z13: Crystal structure and mechanistic analysis of 2F5-gp41 complex is reported. Z13 has been referred as a BnAb directed against the transmembrane gp41 envelope glycoprotein.
Ofek2004
(antibody interactions, structure)
-
Z13: 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. Z13 has been referred as a positive control for epitope mapping and evaluating the anti-gp-41 antibodies.
Mouquet2011
(neutralization)
-
Z13: The capacity of Z13 to block completely the activity of the anti-HIV peptide T20 was investigated. T20 inhibited the fusion or syncytia formation between co-cultured CHO-WT cells expressing HIV-1 HXB2 envelope glycoprotein on their surface and HeLaT4 cells. Z13 was not able to block the anti-fusion effect of T20.
Vincent2012
(antibody interactions)
-
Z13: 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 the epitope of Z13 is located between those of 2F5 and 4E10 and closely overlaps that of 4E10 but the neutralizing capacity of MAb Z13 is weaker than those of 2F5 and 4E10.
Gonzalez2010
(neutralization, variant cross-reactivity, escape, review)
-
Z13: 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)
-
Z13: 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
(effector function, neutralization, review)
-
Z13: 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)
-
Z13: 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 Z13 are reviewed. Implications of the data for immunogen design is discussed.
Schief2009
(antibody binding site, review)
-
Z13: 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)
-
Z13: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:4-59*03, IGHD:3-16, D-RF:3, IGHJ:6. 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)
-
Z13: 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)
-
Z13: This review provides information on the HIV-1 glycoprotein properties that make it challenging to target with neutralizing Abs. Z13 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, are discussed. In addition, approaches to target cellular molecules, such as CD4, CCR5, CXCR4, and MHC molecules, with therapeutic Abs are reviewed.
Phogat2007
(review)
-
Z13: This review summarizes current knowledge on the various functional properties of antibodies in HIV-1 infection, including Z13 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)
-
Z13: Z13 structure, binding, neutralization, and strategies that can be used for vaccine antigen design to elicit anti-gp41 Abs, are reviewed in detail.
Lin2007
(review)
-
Z13: This review summarizes Z13 Ab epitope, properties and neutralization activity.
Kramer2007
(review)
-
Z13: Similarity level of the Z13 binding site pentapeptide NWFDI to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 1 time, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome.
Kanduc2008
-
Z13: The newly detected MAb m44 was shown to neutralize a panel of primary HIV-1 isolates with higher potency than Fab Z13. In binding assays, Z13 did not bind to 5Hb region, but did bind the 6HB with the same potency as m44. Z13 did not compete with m44 for binding. A fusion protein of gp41 constructed for alanine-scanning mutagenesis bound to Z13, indicating that its antigenic structure was intact.
Zhang2008
(neutralization)
-
Z13: 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. Plasma from 5 of 44 HIV-1 infected individuals reacted with a peptide that binds Z13, indicating that these patients mounted Z13-like Ab response.
Penn-Nicholson2008
-
Z13: The study compared Ab neutralization against the JR-FL primary isolate and trimer binding affinities judged by native PAGE. There was direct quantitative relationship between monovalent Fab-trimer binding and neutralization, implying that neutralization begins as each trimer is occupied by one Ab. In BN-PAGE, neutralizing Fabs, Z13 in particular, and sCD4 were able to shift JR-FL trimers. In contrast, most non-neutralizing Fabs bound to monomer, but their epitopes were conformationally occluded on trimers, confirming the exclusive relationship of trimer binding and neutralization.
Crooks2008
(neutralization, binding affinity)
-
Z13: Competition of free gp120 89.6 with immobilized gp140 89.6 for binding to Z13 was assessed. The binding of this Ab to coated gp140 was decreased at the highest concentration of gp120. Neutralizing activity of Z13 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, binding affinity, subtype comparisons)
-
Z13: Epitope recognition sequences for Abs 2F5 and 4E10 were introduced into the corresponding region of SIVmac239. SIVmac239/4E10 and SIVmac239/2F5 were not neutralized by Z13 in spite of the overlap of Z13 and 4E10 sequences.
Yuste2006
(neutralization, SIV)
-
Z13: 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)
-
Z13: 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, review)
-
Z13: 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)
-
Z13: 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. Z13 is able to recognize both gp120-gp41 trimers and monomers, as well as trimeric and monomeric gp41 stumps. Z13 failed to bind to VLPs before treatment with detergent but did after the treatment, suggesting that Z13 epitope becomes fully available only after the Env trimers are liberated by detergent.
Moore2006
(antibody binding site)
-
Z13: This Ab was shown to infrequently neutralize cloned Envs (clades A, B, C, D, F1, CRF01_AE, CRF02_AG, CRF06_cpx and CRF11_cpx) derived from donors with and without broadly cross-reactive neutralizing antibodies.
Cham2006
(neutralization, variant cross-reactivity, subtype comparisons)
-
Z13: 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)
-
Z13: 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, and improved neutralization potency against sensitive HIV-1. Alanine scanning revealed that N671 and D674 residues are crucial for peptide recognition and neutralization of HIV-1 by this Fab. Z13e1 was shown to bind with high affinity to an epitope overlapping those of 2F5 and 4E10 with the minimal epitope WASLWNWFDITN, indicating that the limited neutralization potency results from the limited access to the epitope within the envelope trimer.
Nelson2007
(variant cross-reactivity)
-
Z13: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 Z13 epitope.
Luo2006
(vaccine antigen design)
-
Z13: This paper reviews MAbs and Fabs that bind to HIV-1 Env. Z13 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 MAb 4E10. Z13 is broadly neutralizing, neutralizing primary isolates from clades A, B, C, D and CRF01 (E).
Gorny2003
(antibody binding site, review)
-
Z13: 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)
-
Z13: Review of NAbs that notes Z13 is a phage display generated FAb fragment from a B clade infected individual and that illustrates gp41's conformational change and exposure of the 4E10/Z13 epitope in the transient pre-hairpin form.
Ferrantelli2002
(antibody binding site, review)
-
Z13: MAb 4E10 and FAb Z13 both bind proximally to 2F5 to a relatively 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 can neutralize some primary isolates from clades B, C, and E -- Z13 was selected using a phage display library with the MN gp41 peptide LLELDKWASLWNWFDITNWSW from an HIV infected donor who had an exceptionally broad NAb response -- different strains were refractive to neutralization by broadly neutralizing Abs IgG1b12, 2F5, Z13 and 4E10 -- epitope location noted here is by analogy to MAb 4E10.
Zwick2001b
(antibody binding site, antibody generation, variant cross-reactivity)
References
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Isolation Paper
Zwick2001b
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Crooks2008
Emma T. Crooks, Pengfei Jiang, Michael Franti, Sharon Wong, Michael B. Zwick, James A. Hoxie, James E. Robinson, Penny L. Moore, and James M. Binley. Relationship of HIV-1 and SIV Envelope Glycoprotein Trimer Occupation and Neutralization. Virology, 377(2):364-378, 1 Aug 2008. PubMed ID: 18539308.
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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.
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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.
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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.
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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.
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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.
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Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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Nadine Vincent and Etienne Malvoisin. Ability of Antibodies Specific to the HIV-1 Envelope Glycoprotein to Block the Fusion Inhibitor T20 in a Cell-Cell Fusion Assay. Immunobiology, 217(10):943-950, Oct 2012. PubMed ID: 22387075.
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Lai-Xi Wang. Bioorganic Approaches towards HIV Vaccine Design. Curr. Pharm. Des., 9(22):1771-87, 2003. PubMed ID: 12871196.
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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.
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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.
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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.
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Zhang2008
Mei-Yun Zhang, Bang K. Vu, Anil Choudhary, Hong Lu, Michael Humbert, Helena Ong, Munir Alam, Ruth M. Ruprecht, Gerald Quinnan, Shibo Jiang, David C. Montefiori, John R. Mascola, Christopher C. Broder, Barton F. Haynes, and Dimiter S. Dimitrov. Cross-Reactive Human Immunodeficiency Virus Type 1-Neutralizing Human Monoclonal Antibody That Recognizes a Novel Conformational Epitope on gp41 and Lacks Reactivity against Self-Antigens. J. Virol., 82(14):6869-6879, Jul 2008. PubMed ID: 18480433.
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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.
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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.
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