Found 14 matching records:
Download this epitope record as JSON.
MAb ID | 10/76b | |
---|---|---|
HXB2 Location | Env(162-170) DNA(6708..6734) |
Env Epitope Map |
Author Location | gp120(162-171 BH10) | |
Research Contact | Jane McKeating | |
Epitope |
STSIRGKVQ
|
Epitope Alignment
|
Ab Type | ||
Neutralizing | L (HXB10) | |
Species (Isotype) | rat(IgG2a) | |
Patient | ||
Immunogen | vaccine | |
Keywords | antibody binding site, antibody generation, variant cross-reactivity |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 8 of 8 notes.
Showing 7 of 7 references.
Isolation 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.
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.
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.
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.
Pinter2005 Abraham Pinter, William J. Honnen, Paul D'Agostino, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The C108g Epitope in the V2 Domain of gp120 Functions as a Potent Neutralization Target When Introduced into Envelope Proteins Derived from Human Immunodeficiency Virus Type 1 Primary Isolates. J. Virol., 79(11):6909-6917, Jun 2005. PubMed ID: 15890930. Show all entries for this paper.
Honnen2007 W. J. Honnen, C. Krachmarov, S. C. Kayman, M. K. Gorny, S. Zolla-Pazner, and A. Pinter. Type-Specific Epitopes Targeted by Monoclonal Antibodies with Exceptionally Potent Neutralizing Activities for Selected Strains of Human Immunodeficiency Virus Type 1 Map to a Common Region of the V2 Domain of gp120 and Differ Only at Single Positions from the Clade B Consensus Sequence. J. Virol., 81(3):1424-1432, Feb 2007. PubMed ID: 17121806. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 11/4c (11/4c/1j/4j) | |
---|---|---|
HXB2 Location | Env(162-170) DNA(6708..6734) |
Env Epitope Map |
Author Location | gp120(152-181) | |
Epitope |
STSIRGKVQ
|
Epitope Alignment
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L (HXB2) | |
Species (Isotype) | rat(IgG2a) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 5 of 5 notes.
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.
Download this epitope record as JSON.
MAb ID | 11/41e | |
---|---|---|
HXB2 Location | Env(162-170) DNA(6708..6734) |
Env Epitope Map |
Author Location | gp120(162-171) | |
Epitope |
STSIRGKVQ
|
Epitope Alignment
|
Ab Type | ||
Neutralizing | L (HXB10) | |
Species (Isotype) | rat(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 3 of 3 notes.
Showing 3 of 3 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.
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.
Download this epitope record as JSON.
MAb ID | 11/4b | |
---|---|---|
HXB2 Location | Env(162-170) DNA(6708..6734) |
Env Epitope Map |
Author Location | gp120(162-171) | |
Epitope |
STSIRGKVQ
|
Epitope Alignment
|
Ab Type | ||
Neutralizing | L (HXB10) | |
Species (Isotype) | rat(IgG2a) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 4 of 4 notes.
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.
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.
Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.
Download this epitope record as JSON.
MAb ID | 12b | |
---|---|---|
HXB2 Location | Env(162-181) DNA(6708..6767) |
Env Epitope Map |
Author Location | gp120(162-181) | |
Epitope |
STSIRGKVQKEYAFFYKLDI
|
Epitope Alignment
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L (HXB10) | |
Species (Isotype) | rat(IgG2a) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 3 of 3 notes.
Showing 3 of 3 references.
Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. 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.
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.
Download this epitope record as JSON.
MAb ID | 60b | |
---|---|---|
HXB2 Location | Env(172-181) DNA(6738..6767) |
Env Epitope Map |
Author Location | gp120(172-181 HXB2) | |
Epitope |
EYAFFYKLDI
|
Epitope Alignment
|
Subtype | B | |
Ab Type | ||
Neutralizing | no | |
Species (Isotype) | rat(IgG2b) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 1 of 1 note.
Showing 1 of 1 reference.
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.
Download this epitope record as JSON.
MAb ID | 74 | |
---|---|---|
HXB2 Location | Env(172-181) DNA(6738..6767) |
Env Epitope Map |
Author Location | gp120(172-181) | |
Epitope |
EYAFFYKLDI
|
Epitope Alignment
|
Ab Type | ||
Neutralizing | no | |
Species (Isotype) | rat(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 1 of 1 note.
Showing 1 of 1 reference.
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.
Download this epitope record as JSON.
MAb ID | CRA-3 (CRA3) | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Research Contact | Mark Page, NIBSC AIDS reagent project, Potters Bar, Herts, UK | |
Epitope |
|
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | ||
Species (Isotype) | mouse(IgG2a) | |
Patient | ||
Immunogen | vaccine | |
Keywords | dendritic cells, neutralization |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 6 of 6 notes.
Showing 7 of 7 references.
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.
Moore1993b J. P. Moore, Q. J. Sattentau, H. Yoshiyama, M. Thali, M. Charles, N. Sullivan, S.-W. Poon, M. S. Fung, F. Traincard, M. Pinkus, G. Robey, J. E. Robinson, D. D. Ho, and J. Sodroski. Probing the Structure of the V2 Domain of Human Immunodeficiency Virus Type 1 Surface Glycoprotein gp120 with a Panel of Eight Monoclonal Antibodies: Human Immune Response to the V1 and V2 domains. J. Virol., 67:6136-6151, 1993. PubMed ID: 7690418. 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.
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.
Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.
Ditzel1997 H. J. Ditzel, P. W. Parren, J. M. Binley, J. Sodroski, J. P. Moore, C. F. Barbas, III, and D. R. Burton. Mapping the Protein Surface of Human Immunodeficiency Virus Type 1 gp120 Using Human Monoclonal Antibodies from Phage Display Libraries. J. Mol. Biol., 267:684-695, 1997. (Genbank: U82767 U82768 U82769 U82770 U82771 U82772 U82942 U82943 U82944 U82945 U82946 U82947 U82948 U82949 U82950 U82951 U82952 U82961 U82962) Recombinant monoclonal antibodies from phage display libraries provide a method for Env surface epitope mapping. Diverse epitopes are accessed by presenting gp120 to the library in different forms, such as sequential masking of epitopes with existing MAbs or sCD4 prior to selection or by selection on peptides. Fabs identified by these methods have specificities associated with epitopes presented poorly on native multimeric envelope. PubMed ID: 9126846. 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.
Download this epitope record as JSON.
MAb ID | CRA-6 (CRA6) | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Epitope |
|
|
Ab Type | gp120 V1-V2 | |
Neutralizing | ||
Species (Isotype) | mouse | |
Patient | ||
Immunogen | ||
Keywords |
Showing 1 of 1 note.
Showing 1 of 1 reference.
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.
Download this epitope record as JSON.
MAb ID | CRA-4 (CRA4) | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Research Contact | Mark Page, NIBS, MRC AIDS reagent repository, ARP 325 | |
Epitope |
|
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L (HXB2) | |
Species (Isotype) | mouse(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords | dendritic cells, neutralization |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 7 of 7 notes.
Showing 7 of 7 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.
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.
Moore1993b J. P. Moore, Q. J. Sattentau, H. Yoshiyama, M. Thali, M. Charles, N. Sullivan, S.-W. Poon, M. S. Fung, F. Traincard, M. Pinkus, G. Robey, J. E. Robinson, D. D. Ho, and J. Sodroski. Probing the Structure of the V2 Domain of Human Immunodeficiency Virus Type 1 Surface Glycoprotein gp120 with a Panel of Eight Monoclonal Antibodies: Human Immune Response to the V1 and V2 domains. J. Virol., 67:6136-6151, 1993. PubMed ID: 7690418. 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.
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.
Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. 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.
Download this epitope record as JSON.
MAb ID | 66a | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Epitope |
|
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L (HXB2) | |
Species (Isotype) | mouse(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 2 of 2 notes.
Showing 1 of 1 references.
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.
Download this epitope record as JSON.
MAb ID | 66c | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Epitope |
|
|
Ab Type | gp120 V2 // V2 glycan(V2g) // V2 apex | |
Neutralizing | L (HXB2) | |
Species (Isotype) | mouse(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 1 of 1 note.
Showing 1 of 1 reference.
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.
Download this epitope record as JSON.
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 type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 6 of 6 notes.
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.
Download this epitope record as JSON.
MAb ID | 62c | |
---|---|---|
HXB2 Location | Env | Env Epitope Map |
Author Location | gp120 | |
Epitope |
|
|
Ab Type | gp120 V1-V2 | |
Neutralizing | no | |
Species (Isotype) | rat(IgG1) | |
Patient | ||
Immunogen | vaccine | |
Keywords | dendritic cells, neutralization |
Vaccine type | protein |
---|---|
Vaccine strain | B clade BH10 |
Vaccine component | gp120 |
Showing 3 of 3 notes.
Showing 2 of 2 references.
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.
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.
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