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Displaying record number 779

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MAb ID	D61
HXB2 Location	gp160(592-608) DNA(7998..8048)	gp160 Epitope Map
Author Location	gp41(592-608 HXB2)
Research Contact	Patricia Earl and Christopher Broder, NIH
Epitope	LLGIWGCSGKLICTTAV	Epitope Alignment
Subtype	B
Ab Type	gp41 cluster I
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody binding site, antibody generation, antibody interactions, genital and mucosal immunity, isotype switch

Vaccine Details

Vaccine type	protein
Vaccine component	Env dimers

Notes

Showing 8 of 8 notes.

• D61: D61 was used in competition assays with gp41 Abs cloned from B cells from patients with broadly neutralizing sera. Abs that competed with D61 for binding were assigned to be directed to gp41 cluster I. Pietzsch2010 (antibody interactions)
• D61: D61 did not compete with the newly defined neutralizing MAb m44 for binding to gp41. Zhang2008
• D61: 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. Unlike IgA D10, D47, D19, and D25, IgA D61 was not able to excrete HIV. D61 bound weakly to HIV but the produced immune complex failed to associate with pIgR. These results show that some 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)
• D61: The fusion process was slowed by using a suboptimal temperature (31.5 C) to re-evaluate the potential of Abs targeting fusion intermediates to block HIV entry -- preincubation of E/T cells at 31.5 C enabled polyclonal anti-N-HR Ab and anti-six-helix bundle Abs to inhibit fusion, indicating six-helix bundles form prior to fusion -- the preincubation 31.5 C step did not alter the inhibitory activity of neutralizing Abs anti-gp41 2F5, or anti-gp120 2G12, IG1b12, 48d, and 17b -- nor did it alter two gp41 MAbs, T9 and D61, inability to inhibit fusion. Database note: First author "GoldingH" is distinct from another author found as both "GoldingB" & "Golding" on annotated papers in this database. GoldingH2002 (antibody binding site)
• D61: Binding maps to region 597-613: WGCSGKLICTTAVPWNA -- immunodominant region containing two Cys residues -- this antibody, along with human MAb 246-D, can be blocked by any of a group of 8 conformational MAbs (M10, D41, D54, T4, T6, T9, T10 and T35) -- members of this competition group are blocked by sera from HIV-1+ individuals. Earl1997 (antibody binding site)
• D61: Does not precipitate gp41(21-166), but due to a structural difference in the disulfide bonding region near the two cysteines -- the authors propose that this region may change conformation during the activation of the membrane fusion state of the HIV-1 glycoprotein. Weissenhorn1996 (antibody binding site)
• D61: Linear gp41 epitope in the cluster I region -- human sera blocked binding in oligomeric ELISA assay to a similar extent for gp41 MAbs D20, D43, D61, and T4. Richardson1996 (antibody binding site)
• D61: Generated during a study of the influence of the oligomeric structure of Env in determining the repertoire of the Ab response. Earl1994 (antibody generation)

References

Showing 8 of 8 references.

Isolation Paper
Earl1994 P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157. Show all entries for this paper.

Earl1997 P. L. Earl, C. C. Broder, R. W. Doms, and B. Moss. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol., 71:2674-84, 1997. PubMed ID: 9060620. Show all entries for this paper.

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

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.

Richardson1996 T. M. Richardson, Jr., B. L. Stryjewski, C. C. Broder, J. A. Hoxie, J. R. Mascola, P. L. Earl, and R. W. Doms. Humoral response to oligomeric human immunodeficiency virus type 1 envelope protein. J. Virol., 70:753-62, 1996. An Env antigen capture enzyme-linked immunosorbent assay using a soluble, oligomeric form of HIV-1IIIB Env (gp140) that contains gp120 and the gp41 ectodomain was developed. The gp140, captured by various monoclonal antibodies (MAbs), retained its native oligomeric structure: it bound CD4 and was recognized by MAbs to conformational epitopes in gp120 and gp41, including oligomer-specific epitopes in gp41. PubMed ID: 8551612. Show all entries for this paper.

Weissenhorn1996 W. Weissenhorn, S. A. Wharton, L. J. Calder, P. L. Earl, B. Moss, E. Aliprandis, J. J. Skehel, and D. C. Wiley. The Ectodomain of HIV-1 Env Subunit gp41 Forms a Soluble, alpha-Helical, Rod-Like Oligomer in the Absence of gp120 and the N-Terminal Fusion Peptide. EMBO J., 15:1507-1514, 1996. PubMed ID: 8612573. 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.

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.

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Displaying record number 780

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MAb ID	D49
HXB2 Location	gp160(592-608) DNA(7998..8048)	gp160 Epitope Map
Author Location	gp41(597-613)
Research Contact	Pat Earl
Epitope	LLGIWGCSGKLICTTAV	Epitope Alignment
Ab Type	gp41 cluster I
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody interactions, kinetics

Vaccine Details

Vaccine type	protein
Vaccine component	Env dimers

Notes

Showing 6 of 6 notes.

• D49: Intrinsic reactivity of HIV-1, a new property regulating the level of both entry and sensitivity to Abs has been reported. This activity dictates the level of responsiveness of Env protein to co-receptor, CD4 engagement and Abs. D49 was used as a control. Haim2011 (antibody interactions)
• D49: Unlike the MPER MAbs tested, D49 did not show any Env-independent virus capture in the conventional or in the modified version of the virus capture assay. Leaman2010
• D49: Immobilized D49 was able to capture infectious HIV-1 whole virions in a standard virus capture assay, unlike mAbs 8K8 and D5. Nelson2008
• D49: In contrast to a decrease of 2F5 and 4E10 binding upon triggering of HIV-1 Env-expressing cells with target cells, binding of D49 to it epitope in the immunodominant loop of gp41 remains unchanged, indicating that the decrease seen for 2F5 and 4E10 is not due to removal of gp41 from the surface. Dimitrov2007 (kinetics)
• D49: Binding maps to region 597-613: WGCSGKLICTTAVPWNA -- immunodominant region containing two Cys residues. Earl1997
• D49: Generated during a study of the influence of the oligomeric structure of Env in determining the repertoire of the Ab response. Earl1994

References

Showing 6 of 6 references.

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.

Earl1994 P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157. Show all entries for this paper.

Earl1997 P. L. Earl, C. C. Broder, R. W. Doms, and B. Moss. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol., 71:2674-84, 1997. PubMed ID: 9060620. 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.

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.

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

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Displaying record number 781

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MAb ID	T32
HXB2 Location	gp160(592-608) DNA(7998..8048)	gp160 Epitope Map
Author Location	gp41(597-613)
Research Contact	Patricia Earl and Christopher Broder, NIH
Epitope	LLGIWGCSGKLICTTAV	Epitope Alignment
Ab Type	gp41 cluster I
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords	antibody generation, antibody interactions, binding affinity, viral fitness and reversion

Vaccine Details

Vaccine type	tetrameric Env
Vaccine component	Env

Notes

Showing 4 of 4 notes.

• T32: 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)
• T32: The capacity of T32 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. T32 was not able to block the anti-fusion effect of T20. Vincent2012 (antibody interactions)
• T32: Binding maps to region 597-613: WGCSGKLICTTAVPWNA -- immunodominant region containing two Cys residues. Earl1997 (binding affinity)
• T32: Generated during a study of the influence of the oligomeric structure of Env in determining the repertoire of the Ab response. Earl1994 (antibody generation)

References

Showing 4 of 4 references.

Isolation Paper
Earl1994 P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157. Show all entries for this paper.

Earl1997 P. L. Earl, C. C. Broder, R. W. Doms, and B. Moss. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol., 71:2674-84, 1997. PubMed ID: 9060620. Show all entries for this paper.

Vincent2012 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. 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.

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Displaying record number 782

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MAb ID	T34
HXB2 Location	gp160(592-608) DNA(7998..8048)	gp160 Epitope Map
Author Location	gp41(597-613)
Research Contact	Patricia Earl and Christopher Broder, NIH
Epitope	LLGIWGCSGKLICTTAV	Epitope Alignment
Ab Type	gp41 cluster I
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	tetrameric Env
Vaccine component	Env

Notes

Showing 2 of 2 notes.

• T34: Binding maps to region 597-613: WGCSGKLICTTAVPWNA -- immunodominant region containing two Cys residues. Earl1997
• T34: Generated during a study of the influence of the oligomeric structure of Env in determining the repertoire of the Ab response -- an oligomer with no gp120/gp41 cleavage site was used as the immunogen. Earl1994

References

Showing 2 of 2 references.

Earl1994 P. L. Earl, C. C. Broder, D. Long, S. A. Lee, J. Peterson, S. Chakrabarti, R. W. Doms, and B. Moss. Native oligomeric human immunodeficiency virus type 1 Envelope glycoprotein elicits diverse monoclonal antibody reactivities. J. Virol., 68:3015-3026, 1994. In a study of the repertoire of response to oligomeric versus monomeric Env protein, 138 murine MAbs were generated in response to an immunogen that was a gp120/bp41 oligomeric molecule that was not cleaved due to a mutation in the cleavage site. The oligomeric molecule was found to elicit a response that was very different than the monomer. Most MAbs were conformational, many were to gp41 or if in gp120, to the CD4 BS. Few MAbs to linear V3 epitopes were produced in response to oligomeric protein, though this was a common specificity in response to immunization with gp120 monomeric protein. PubMed ID: 7512157. Show all entries for this paper.

Earl1997 P. L. Earl, C. C. Broder, R. W. Doms, and B. Moss. Epitope map of human immunodeficiency virus type 1 gp41 derived from 47 monoclonal antibodies produced by immunization with oligomeric envelope protein. J. Virol., 71:2674-84, 1997. PubMed ID: 9060620. Show all entries for this paper.

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