logo image

HIV Molecular Immunology Database

Search Antibody Database

Found 3 matching records:

Displaying record number 465

Download this epitope record as JSON.

MAb ID 41.1 (ICR41.1i, ICR41. ICR 41.1i)
HXB2 Location Env Env Epitope Map
Author Location gp120( HXB10)
Research Contact J. Cordell, Institute for Cancer Research, Sutton, Surrey, UK
Epitope
Ab Type gp120 CD4i, gp120 V3 discontinuous
Neutralizing L (HXB2)
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 7 of 7 notes.

References

Showing 10 of 10 references.

Reitz1988 M. S. Reitz, Jr., C. Wilson, C. Naugle, and M. Robert-Guroff. Generation of a Neutralization-Resistant Variant of HIV-1 Is Due to Selection for a Point Mutation in the Envelope Gene. Cell, 54:57-63, 1988. Growth of HXB2 in the constant presence of a neutralizing antiserum yielded a viral population resistant to the same serum. gp41 mutation 582 (Ala to Thr) conferred the resistant phenotype. PubMed ID: 2838179. Show all entries for this paper.

McKeating1992a J. A. McKeating, J. Cordell, C. J. Dean, and P. Balfe. Synergistic Interaction between Ligands Binding to the CD4 Binding Site and V3 Domain of Human Immunodeficiency Virus Type I gp120. Virology, 191:732-742, 1992. PubMed ID: 1280382. Show all entries for this paper.

McKeating1993a J. A. McKeating, C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, S. C. Kayman, Z. Wu, A. Pinter, C. Dean, J. Sodroski, and R. A. Weiss. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol., 67:4932-4944, 1993. Substitutions in the V2 loop can result in complete dissociation of gp120 and gp41, suggesting alterations in V2 can affect subunit assembly. Other substitutions allowed gp120-gp41 association and expression, but inhibited viral entry or syncytia. Binding of some neutralizing MAbs was altered by V2 substitutions. For MAb CRA-4, changes at residues 191/192/193 (YSL/GSS), and for 11/68b, changes at residues 183/184 (PI/SG), within V2, and for both MAbs a position 435 (Y/H) change in C4, abrogate binding. These MAbs can bind to V1 and V2 domains in the absence of C4 domain, so the C4 substitution probably results in conformational change. PubMed ID: 7687306. Show all entries for this paper.

Klasse1993b P. Klasse, J. A. McKeating, M. Schutten, M. S. Reitz, Jr., and M. Robert-Guroff. An Immune-Selected Point Mutation in the Transmembrane Protein of Human Immunodeficiency Virus Type 1 (HXB2-Env:Ala 582(--> Thr)) Decreases Viral Neutralization by Monoclonal Antibodies to the CD4-Binding Site. Virology, 196:332-337, 1993. PubMed ID: 8356803. Show all entries for this paper.

McLain1994 L. McLain and N. J. Dimmock. Single- and Multi-Hit Kinetics of Immunoglobulin G Neutralization of Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies. J. Gen. Virol., 75:1457-1460, 1994. PubMed ID: 8207410. Show all entries for this paper.

Armstrong1996 S. J. Armstrong and N. J. Dimmock. Varying temperature-dependence of post-attachment neutralization of human immunodeficiency virus type 1 by monoclonal antibodies to gp120: identification of a very early fusion-independent event as a neutralization target. J. Gen. Virol., 77:1397-1402, 1996. PubMed ID: 8757979. Show all entries for this paper.

Armstrong1996a S. J. Armstrong, T. L. McInerney, L. McLain, B. Wahren, J. Hinkula, M. Levi, and N. J. Dimmock. Two neutralization anti-V3 monoclonal antibodies act by affecting different functions of human immunodeficiency virus type 1. J. Gen. Virol., 77:2931-2941, 1996. PubMed ID: 9000083. Show all entries for this paper.

Jeffs1996 S. A. Jeffs, J. McKeating, S. Lewis, H. Craft, D. Biram, P. E. Stephens, and R. L. Brady. Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein. J. Gen. Virol., 77:1403-1410, 1996. PubMed ID: 8757980. 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.

Heap2005a Caroline J. Heap, Steven A. Reading, and Nigel J. Dimmock. An Antibody Specific for the C-Terminal Tail of the gp41 Transmembrane Protein of Human Immunodeficiency Virus Type 1 Mediates Post-Attachment Neutralization, Probably Through Inhibition of Virus-Cell Fusion. J. Gen. Virol., 86(5):1499-1507, May 2005. PubMed ID: 15831963. Show all entries for this paper.


Displaying record number 625

Download this epitope record as JSON.

MAb ID ICR 39.13g (ICR39.13g, 39.13g, ICR39.13)
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Jackie Cordell and C. Dean
Epitope
Ab Type gp120 CD4bs
Neutralizing L
Species (Isotype) rat(IgG2b)
Patient  
Immunogen vaccine
Keywords dendritic cells, neutralization

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 14 of 14 notes.

References

Showing 15 of 15 references.

Isolation Paper
Cordell1991 J. Cordell, J. P. Moore, C. J. Dean, P. J. Klasse, R. A. Weiss, and J. A. McKeating. Rat Monoclonal Antibodies to Nonoverlapping Epitopes of Human Immunodeficiency Virus Type I gp120 Block CD4 Binding In Vitro. Virology, 185:72-79, 1991. PubMed ID: 1718090. Show all entries for this paper.

McKeating1992a J. A. McKeating, J. Cordell, C. J. Dean, and P. Balfe. Synergistic Interaction between Ligands Binding to the CD4 Binding Site and V3 Domain of Human Immunodeficiency Virus Type I gp120. Virology, 191:732-742, 1992. PubMed ID: 1280382. Show all entries for this paper.

McKeating1992b J. A. McKeating, M. Thali, C. Furman, S. Karwowska, M. K. Gorny, J. Cordell, S. Zolla-Pazner, J. Sodroski, and R. A. Weiss. Amino Acid Residues of the Human Immunodeficiency Virus Type 1 gp120 Critical for the Binding of Rat and Human Neutralizing Antibodies That Block the gp120-sCD4 Interaction. Virology, 190:134-142, 1992. PubMed ID: 1382339. Show all entries for this paper.

McKeating1993a J. A. McKeating, C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, S. C. Kayman, Z. Wu, A. Pinter, C. Dean, J. Sodroski, and R. A. Weiss. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol., 67:4932-4944, 1993. Substitutions in the V2 loop can result in complete dissociation of gp120 and gp41, suggesting alterations in V2 can affect subunit assembly. Other substitutions allowed gp120-gp41 association and expression, but inhibited viral entry or syncytia. Binding of some neutralizing MAbs was altered by V2 substitutions. For MAb CRA-4, changes at residues 191/192/193 (YSL/GSS), and for 11/68b, changes at residues 183/184 (PI/SG), within V2, and for both MAbs a position 435 (Y/H) change in C4, abrogate binding. These MAbs can bind to V1 and V2 domains in the absence of C4 domain, so the C4 substitution probably results in conformational change. PubMed ID: 7687306. Show all entries for this paper.

Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.

Thali1993 M. Thali, J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski. Characterization of Conserved Human Immunodeficiency Virus Type 1 gp120 Neutralization Epitopes Exposed upon gp120-CD4 Binding. J. Virol., 67:3978-3988, 1993. Five regions are likely to contribute to the 48d and 17b discontinuous epitopes, either directly or through local conformational effects: the hydrophobic ring-like structure formed by the disulfide bond that links C3 and C4, the base of the stem-loop that contains V1 and V2, and the hydrophobic region in C2 from Arg 252 to Asp 262. Additionally changes in Glu 370, and Met 475 in C5, affected binding and neutralization. The hydrophobic character of these critical regions is consistent with the limited exposure on gp120 prior to CD4 binding. PubMed ID: 7685405. Show all entries for this paper.

Klasse1993b P. Klasse, J. A. McKeating, M. Schutten, M. S. Reitz, Jr., and M. Robert-Guroff. An Immune-Selected Point Mutation in the Transmembrane Protein of Human Immunodeficiency Virus Type 1 (HXB2-Env:Ala 582(--> Thr)) Decreases Viral Neutralization by Monoclonal Antibodies to the CD4-Binding Site. Virology, 196:332-337, 1993. PubMed ID: 8356803. Show all entries for this paper.

McLain1994 L. McLain and N. J. Dimmock. Single- and Multi-Hit Kinetics of Immunoglobulin G Neutralization of Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies. J. Gen. Virol., 75:1457-1460, 1994. PubMed ID: 8207410. Show all entries for this paper.

Beretta1994 A. Beretta and A.G. Dalgleish. B-Cell Epitopes. AIDS, 8(suppl 1):S133-S145, 1994. Show all entries for this paper.

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

Armstrong1996 S. J. Armstrong and N. J. Dimmock. Varying temperature-dependence of post-attachment neutralization of human immunodeficiency virus type 1 by monoclonal antibodies to gp120: identification of a very early fusion-independent event as a neutralization target. J. Gen. Virol., 77:1397-1402, 1996. PubMed ID: 8757979. Show all entries for this paper.

Klasse1996 P. J. Klasse and Q. J. Sattentau. Altered CD4 Interactions of HIV Type 1 LAI Variants Selected for the Capacity to Induce Membrane Fusion in the Presence of a Monoclonal Antibody to Domain 2 of CD4. AIDS Res. Hum. Retroviruses, 12:1015-1021, 1996. PubMed ID: 8827217. Show all entries for this paper.

Peet1998 N. M. Peet, J. A. McKeating, J. B. de Souza, I. M. Roitt, P. J. Delves, and T. Lund. The Effect of Low-Profile Serine Substitutions in the V3 Loop of HIV-1. Virology, 251:59-70, 1998. PubMed ID: 9813203. Show all entries for this paper.

Vella2002 Cherelyn Vella, Natalie N. Zheng, Philippa Easterbrook, and Rod S. Daniels. Herpesvirus saimiri-Immortalized Human Lymphocytes: Novel Hosts for Analyzing HIV Type 1 in Vitro Neutralization. AIDS Res. Hum. Retroviruses, 18(13):933-946, 1 Sep 2002. PubMed ID: 12230936. 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.


Displaying record number 626

Download this epitope record as JSON.

MAb ID ICR 39.3b (39.3, 39.3b, ICR39.3b)
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact J. Cordell and C. Dean
Epitope
Ab Type gp120 CD4bs
Neutralizing L
Species (Isotype) rat(IgG2b)
Patient  
Immunogen vaccine
Keywords review, vaccine antigen design

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 8 of 8 notes.

References

Showing 9 of 9 references.

Isolation Paper
Cordell1991 J. Cordell, J. P. Moore, C. J. Dean, P. J. Klasse, R. A. Weiss, and J. A. McKeating. Rat Monoclonal Antibodies to Nonoverlapping Epitopes of Human Immunodeficiency Virus Type I gp120 Block CD4 Binding In Vitro. Virology, 185:72-79, 1991. PubMed ID: 1718090. Show all entries for this paper.

McKeating1992b J. A. McKeating, M. Thali, C. Furman, S. Karwowska, M. K. Gorny, J. Cordell, S. Zolla-Pazner, J. Sodroski, and R. A. Weiss. Amino Acid Residues of the Human Immunodeficiency Virus Type 1 gp120 Critical for the Binding of Rat and Human Neutralizing Antibodies That Block the gp120-sCD4 Interaction. Virology, 190:134-142, 1992. PubMed ID: 1382339. Show all entries for this paper.

Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.

Moore1993c J. P. Moore, M. Thali, B. A. Jameson, F. Vignaux, G. K. Lewis, S.-W. Poon, M. S. Fung, P. J. Durda, L. Akerblom, B. Wahren, D. D. Ho, Q. J. Sattentau, and J. Sodroski. Immunochemical Analysis of the gp120 Surface Glycoprotein of Human Immunodeficiency Virus Type 1: Probing the Structure of the C4 and V4 Domains and the Interaction of the C4 Domain with the V3 Loop. J. Virol., 73:4785-4796, 1993. General observations: C4 and V3 MAbs are sensitive to the way the epitopes are presented, and this sensitivity cannot be correlated to peptide binding. Some V3-C4 domain interaction was indicated based on mutation and interference studies. PubMed ID: 7687303. Show all entries for this paper.

McLain1994 L. McLain and N. J. Dimmock. Single- and Multi-Hit Kinetics of Immunoglobulin G Neutralization of Human Immunodeficiency Virus Type 1 by Monoclonal Antibodies. J. Gen. Virol., 75:1457-1460, 1994. PubMed ID: 8207410. Show all entries for this paper.

Armstrong1996 S. J. Armstrong and N. J. Dimmock. Varying temperature-dependence of post-attachment neutralization of human immunodeficiency virus type 1 by monoclonal antibodies to gp120: identification of a very early fusion-independent event as a neutralization target. J. Gen. Virol., 77:1397-1402, 1996. PubMed ID: 8757979. Show all entries for this paper.

Jeffs1996 S. A. Jeffs, J. McKeating, S. Lewis, H. Craft, D. Biram, P. E. Stephens, and R. L. Brady. Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein. J. Gen. Virol., 77:1403-1410, 1996. PubMed ID: 8757980. Show all entries for this paper.

Wyatt1998 R. Wyatt, P. D. Kwong, E. Desjardins, R. W. Sweet, J. Robinson, W. A. Hendrickson, and J. G. Sodroski. The Antigenic Structure of the HIV gp120 Envelope Glycoprotein. Nature, 393:705-711, 1998. Comment in Nature 1998 Jun 18;393(6686):630-1. The spatial organization of the neutralizing epitopes of gp120 is described, based on epitope maps interpreted in the context of the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody. PubMed ID: 9641684. 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.


This is a legacy search page. It is deprecated, will receive no more updates, and will eventually be removed. Please use the new search pages.

Questions or comments? Contact us at immuno@lanl.gov
 
Managed by Triad National Security, LLC for the U.S. Department of Energy's National Nuclear Security Administration
Copyright Triad National Security, LLC | Disclaimer/Privacy

Dept of Health & Human Services LANL logo National Institutes of Health logo