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Found 14 matching records:

Displaying record number 292

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MAb ID 11/65 (11/65a/5h)
HXB2 Location gp160(102-121)
DNA(6528..6587)
gp160 Epitope Map
Author Location gp120(311-321 HXB10)
Epitope EQMHEDIISLWDQSLKPCVK Epitope Alignment
EQMHEDIISLWDQSLKPCVK epitope logo
Ab Type gp120 C1
Neutralizing  
Species (Isotype) rat(IgG2b)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

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.

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.


Displaying record number 316

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MAb ID 11/4c (11/4c/1j/4j)
HXB2 Location gp160(162-170)
DNA(6708..6734)
gp160 Epitope Map
Author Location gp120(152-181)
Epitope STSIRGKVQ Epitope Alignment
STSIRGKVQ epitope logo
Ab Type gp120 V2 // V2 glycan(V2g) // V2 apex
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 5 of 5 notes.

References

Showing 4 of 4 references.

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.

Wu1995 Z. Wu, S. C. Kayman, W. Honnen, K. Revesz, H. Chen, S. V. Warrier, S. A. Tilley, J. McKeating, C. Shotton, and A. Pinter. Characterization of Neutralization Epitopes in the V2 Region of Human Immunodeficiency Virus Type 1 gp120: Role of Glycosylation in the Correct Folding of the V1/V2 Domain. J. Virol., 69:2271-2278, 1995. Most epitopes based only on numbering. PubMed ID: 7533854. Show all entries for this paper.

Shotton1995 C. Shotton, C. Arnold, Q. Sattentau, J. Sodroski, and J. A. McKeating. Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 69:222-230, 1995. Anti-V2 linear and conformation dependent MAbs were studied. All V2 Abs studied could bind IIIB, but failed to neutralize non-clonal stocks. Epitope exposure is different in rgp120 compared to native gp120. HXB2 V2-MAb neutralization escape mutants were sequenced. PubMed ID: 7527084. 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.


Displaying record number 1000

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MAb ID 55/1l
HXB2 Location gp160(300-315)
DNA(7122..7169)
gp160 Epitope Map
Author Location gp120(300-315)
Epitope NNNTRKRIRIQRGPGR? Epitope Alignment
NNNTRKRIRIQRGPGR? epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing  
Species (Isotype)  
Patient  
Immunogen  
Keywords  

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

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.


Displaying record number 381

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MAb ID 8/38c (8/38/1c, 8/38)
HXB2 Location gp160(300-315)
DNA(7122..7169)
gp160 Epitope Map
Author Location gp120(300-315 HXB10)
Research Contact C. Dean and C. Shotton, Institute for Cancer Research, Surrey, UK
Epitope NNNTRKRIRIQRGPGR Epitope Alignment
NNNTRKRIRIQRGPGR epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords antibody generation, dendritic cells, neutralization

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 7 of 7 notes.

References

Showing 6 of 6 references.

Isolation 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.

Sattentau1995a Q. J. Sattentau and J. P. Moore. Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer. J. Exp. Med., 182:185-196, 1995. This study suggests that antibodies specific for one of five different binding regions on gp120 are associated with viral neutralization: V2, V3, C4, the CD4 binding site, and a complex discontinuous epitope that does not interfere with CD4 binding. Kinetic binding properties of a set of MAbs that bind to these regions were studied, analyzing binding to both functional oligomeric LAI gp120 and soluble monomeric LAI BH10 gp120; neutralization ID$_50$s were also evaluated. It was found that the neutralization ID$_50$s was related to the ability to bind oligomeric, not monomeric, gp120, and concluded that with the exception of the V3 loop, regions of gp120 that are immunogenic will be poorly presented on cell-line-adapted virions. Further, the association rate, estimated as the t$_1/2$ to reach equilibrium binding to multimeric, virion associated, gp120, appears to be a major factor relating to affinity and potency of the neutralization response to cell-line-adapted virus. PubMed ID: 7540648. 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.

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.

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.

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 383

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MAb ID 8/64b
HXB2 Location gp160(300-315)
DNA(7122..7169)
gp160 Epitope Map
Author Location gp120(300-315 HXB10)
Epitope NNNTRKRIRIQRGPGR Epitope Alignment
NNNTRKRIRIQRGPGR epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) rat(IgM)
Patient  
Immunogen vaccine
Keywords dendritic cells, neutralization

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 4 of 4 notes.

References

Showing 3 of 3 references.

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.

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.

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 462

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MAb ID 10/36e
HXB2 Location gp160(311-321)
DNA(7155..7187)
gp160 Epitope Map
Author Location gp120(311-321 HXB10)
Epitope RGPGRAFVTIG Epitope Alignment
RGPGRAFVTIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L (HXB10)
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

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.

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.


Displaying record number 461

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MAb ID 10/54 (10/54ow/6i/6i)
HXB2 Location gp160(311-321)
DNA(7155..7187)
gp160 Epitope Map
Author Location gp120(311-321 HXB10)
Epitope RGPGRAFVTIG Epitope Alignment
RGPGRAFVTIG epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L (HXB10)
Species (Isotype) rat(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

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.

McKeating1993b J. A. McKeating, J. Bennett, S. Zolla-Pazner, M. Schutten, S. Ashelford, A. Leigh-Brown, and P. Balfe. Resistance of a Human Serum-Selected Human Immunodeficiency Virus Type 1 Escape Mutant to Neutralization by CD4 Binding Site Monoclonal Antibodies Is Conferred by a Single Amino Acid Change in gp120. J. Virol., 67:5216-5225, 1993. PubMed ID: 7688820. 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.

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.


Displaying record number 545

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MAb ID ICR38.1a (38.1a, 388/389, ARP388/389)
HXB2 Location gp160(429-438)
DNA(7509..7538)
gp160 Epitope Map
Author Location gp120(427-436 BRU)
Epitope EVGKAMYAPP (Discontinuous epitope) Epitope Alignment
EVGKAMYAPP epitope logo
Ab Type gp120 C3, gp120 C4
Neutralizing L
Species (Isotype) rat(IgG2b)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, dendritic cells

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 10 of 10 notes.

References

Showing 12 of 12 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.

McKeating1992 J. A. McKeating, J. P. Moore, M. Ferguson, H. S. Marsden, S. Graham, J. W. Almond, D. J. Evans, and R. A. Weiss. Monoclonal Antibodies to the C4 Region of Human Immunodeficiency Virus Type 1 gp120: Use in Topological Analysis of a CD4 Binding Site. AIDS Res. Hum. Retroviruses, 8:451-459, 1992. Antibodies were generated using an antigen poliovirus chimera, expressing aa430-446 of gp120. Results suggest that WQEVGKAMYA may be exposed on the surface of rec gp120. PubMed ID: 1376134. 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.

McKeating1993b J. A. McKeating, J. Bennett, S. Zolla-Pazner, M. Schutten, S. Ashelford, A. Leigh-Brown, and P. Balfe. Resistance of a Human Serum-Selected Human Immunodeficiency Virus Type 1 Escape Mutant to Neutralization by CD4 Binding Site Monoclonal Antibodies Is Conferred by a Single Amino Acid Change in gp120. J. Virol., 67:5216-5225, 1993. PubMed ID: 7688820. 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.

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.

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.

Kropelin1998 M. Kropelin, C. Susal, V. Daniel, and G. Opelz. Inhibition of HIV-1 rgp120 Binding to CD4+ T Cells by Monoclonal Antibodies Directed against the gp120 C1 or C4 Region. Immunol. Lett., 63:19-25, 1998. PubMed ID: 9719434. 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 1002

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MAb ID 55/68b
HXB2 Location Env Env Epitope Map
Author Location gp120(300-315)
Epitope
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing  
Species (Isotype)  
Patient  
Immunogen  
Keywords  

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

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.


Displaying record number 600

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MAb ID 10/46c
HXB2 Location Env Env Epitope Map
Author Location gp120
Epitope
Ab Type gp120 CD4BS
Neutralizing  
Species (Isotype) rat
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component gp120

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 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.

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.

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.


Displaying record number 625

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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 698

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MAb ID 11/68b
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Shotton and Dean
Epitope
Ab Type gp120 V1-V2
Neutralizing L (HXB2)
Species (Isotype) rat(IgG1)
Patient  
Immunogen vaccine
Keywords dendritic cells, neutralization

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 6 of 6 notes.

References

Showing 4 of 4 references.

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.

Shotton1995 C. Shotton, C. Arnold, Q. Sattentau, J. Sodroski, and J. A. McKeating. Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 69:222-230, 1995. Anti-V2 linear and conformation dependent MAbs were studied. All V2 Abs studied could bind IIIB, but failed to neutralize non-clonal stocks. Epitope exposure is different in rgp120 compared to native gp120. HXB2 V2-MAb neutralization escape mutants were sequenced. PubMed ID: 7527084. 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.

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 999

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MAb ID 11/75a/21/41
HXB2 Location Env Env Epitope Map
Author Location gp120
Epitope
Ab Type gp120 V3 discontinuous
Neutralizing  
Species (Isotype)  
Patient  
Immunogen  
Keywords  

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

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.

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.


Displaying record number 1001

Download this epitope record as JSON.

MAb ID 55/45a/1l
HXB2 Location Env Env Epitope Map
Author Location gp120
Epitope
Ab Type gp120 V3 discontinuous
Neutralizing  
Species (Isotype)  
Patient  
Immunogen  
Keywords  

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

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.


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