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Displaying record number 255

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MAb ID M85
HXB2 Location Env(30-51)
DNA(6312..6377)
Env Epitope Map
Author Location gp120(30-51 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope ATEKLWVTVYYGVPVWKEATTT Epitope Alignment
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 5 of 5 notes.

References

Showing 7 of 7 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.

Koefoed2005 Klaus Koefoed, Lauge Farnaes, Meng Wang, Arne Svejgaard, Dennis R. Burton, and Henrik J. Ditzel. Molecular Characterization of the Circulating Anti-HIV-1 gp120-Specific B Cell Repertoire using Antibody Phage Display Libraries Generated from Pre-Selected HIV-1 gp120 Binding PBLs. J. Immunol. Methods, 297(1-2):187-201, Feb 2005. PubMed ID: 15777942. Show all entries for this paper.


Displaying record number 256

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MAb ID 7E2/4
HXB2 Location Env(31-50)
DNA(6315..6374)
Env Epitope Map
Author Location gp120(31-50 LAI)
Research Contact S. Ranjbar, NIBSC, UK
Epitope TEKLWVTVYYGVPVWKEATT Epitope Alignment
TEKLWVTVYYGVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 257

Download this epitope record as JSON.

MAb ID M92
HXB2 Location Env(41-50)
DNA(6345..6374)
Env Epitope Map
Author Location gp120(31-50 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope GVPVWKEATT Epitope Alignment
GVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) rat(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.


Displaying record number 258

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MAb ID 4D4#85
HXB2 Location Env(41-50)
DNA(6345..6374)
Env Epitope Map
Author Location gp120( LAI)
Research Contact S. Nigida and L. Arthur, NCI, Frederick, MD USA
Epitope GVPVWKEATT Epitope Alignment
GVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody polyreactivity, immunotherapy

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 6 of 6 notes.

References

Showing 7 of 7 references.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.


Displaying record number 260

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MAb ID M86
HXB2 Location Env(42-61)
DNA(6348..6407)
Env Epitope Map
Author Location gp120(42-61 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope VPVWKEATTTLFCASDAKAY Epitope Alignment
VPVWKEATTTLFCASDAKAY epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.


Displaying record number 263

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MAb ID 133/290
HXB2 Location Env(61-70)
DNA(6405..6434)
Env Epitope Map
Author Location gp120(61-70 LAI)
Research Contact M. Niedrig
Epitope YDTEVHNVWA Epitope Alignment
YDTEVHNVWA epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing L
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords vaccine antigen design

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 8 of 8 notes.

References

Showing 11 of 11 references.

Niedrig1992 M. Niedrig, H.-P. Harthus, M. Broker, H. Bickhard, G. Pauli, H. R. Gelderblom, and B. Wahren. Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120. J. Gen. Virol., 73:2451-2455, 1992. PubMed ID: 1383412. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Wyatt1995 R. Wyatt, J. Moore, M. Accola, E. Desjardin, J. Robinson, and J. Sodroski. Involvement of the V1/V2 Variable Loop Structure in the Exposure of Human Immunodeficiency Virus Type 1 gp120 Epitopes Induced by Receptor Binding. J. Virol., 69:5723-5733, 1995. Deletions in the V1/V2 loops of gp120 resulted in the loss of the ability of sCD4 to induce binding of the MAbs 17b, 48d, and A32. A32 can induce binding of 17b and 48d; this induction does not appear to involve the V1/V2 regions. PubMed ID: 7543586. 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.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.


Displaying record number 262

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MAb ID 133/237
HXB2 Location Env(61-70)
DNA(6405..6434)
Env Epitope Map
Author Location gp120(51-70 LAI)
Epitope YDTEVHNVWA Epitope Alignment
YDTEVHNVWA epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing L
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords vaccine antigen design

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Niedrig1992 M. Niedrig, H.-P. Harthus, M. Broker, H. Bickhard, G. Pauli, H. R. Gelderblom, and B. Wahren. Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120. J. Gen. Virol., 73:2451-2455, 1992. PubMed ID: 1383412. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.


Displaying record number 267

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MAb ID 4A7C6
HXB2 Location Env(81-90)
DNA(6465..6494)
Env Epitope Map
Author Location gp120(81-90 LAI)
Research Contact R. Tedder
Epitope PQEVVLVNVT Epitope Alignment
PQEVVLVNVT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 5 of 5 notes.

References

Showing 6 of 6 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. 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.

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.


Displaying record number 269

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MAb ID 1D10
HXB2 Location Env(81-100)
DNA(6465..6524)
Env Epitope Map
Author Location gp120(81-100 LAI)
Epitope PQEVVLVNVTENFDMWKNDM Epitope Alignment
PQEVVLVNVTENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing L
Species (Isotype) rat(IgG1)
Patient  
Immunogen vaccine
Keywords antibody generation

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 4 of 4 notes.

References

Showing 5 of 5 references.

Isolation Paper
Dowbenko1988 D. Dowbenko, G. Nakamura, C. Fennie, C. Shimasaki, L. Riddle, R. Harris, T. Gregory, and L. Lasky. Epitope mapping of the immunodeficiency virus type 1 gp120 with monoclonal antibodies. J. Virol., 62:4703-4711, 1988. PubMed ID: 2460639. Show all entries for this paper.

Berman1991 P. W. Berman, K. Rosenthal, G. Nakamura, L. Riddle, J. P. Porter, D. Dowbenko, M. Hobbes, R. Byrn, J. Groopman, T. Gregory, and B. Fendly. Monoclonal Antibodies to gp160 of HIV-1 That Neutralize HIV-1 Infectivity, Block the Binding of gp120 to CD4, and React with Diverse Isolates. J. Acquir. Immune Defic. Syndr., 4:306, 1991. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Nakamura1992 G. R. Nakamura, R. Byrn, K. Rosenthal, J. P. Porter, M. R. Hobbs, L. Riddle, D. J. Eastman, D. Dowbenko, T. Gregory, B. M. Fendly, and P. W. Berman. Monoclonal Antibodies to the Extracellular Domain of HIV-1 IIIB gp160 That Neutralize Infectivity, Block Binding to CD4 React with Diverse Isolates. AIDS Res. Hum. Retroviruses, 8:1875-1885, 1992. PubMed ID: 1283308. Show all entries for this paper.

Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.


Displaying record number 270

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MAb ID 133/192
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Research Contact Matthias Niedrig
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing L
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords vaccine antigen design

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 8 of 8 notes.

References

Showing 10 of 10 references.

Niedrig1992 M. Niedrig, H.-P. Harthus, M. Broker, H. Bickhard, G. Pauli, H. R. Gelderblom, and B. Wahren. Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120. J. Gen. Virol., 73:2451-2455, 1992. PubMed ID: 1383412. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.


Displaying record number 271

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MAb ID C6 (Ch6)
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 5 of 5 notes.

References

Showing 4 of 4 references.

Pincus1993 S. H. Pincus and J. McClure. Soluble CD4 Enhances the Efficacy of Immunotoxins Directed against gp41 of the Human Immunodeficiency Virus. Proc. Natl. Acad. Sci. U.S.A., 90:332-336, 1993. PubMed ID: 8419938. Show all entries for this paper.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.


Displaying record number 272

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MAb ID B2
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG2b)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 3 of 3 notes.

References

Showing 5 of 5 references.

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.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.


Displaying record number 278

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MAb ID B10
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site, binding affinity

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

MoorePerCom John P. Moore. Personal communication. Show all entries for this paper.


Displaying record number 282

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MAb ID 489.1(961)
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Research Contact C. Bruck, SKB, Belgium
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 1 of 1 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 283

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MAb ID T1.1
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type vaccinia
Vaccine component gp160

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Broliden1990 P. A. Broliden, K. Ljunggren, J. Hinkula, E. Norrby, L. Akerblom, and B. Wahren. A monoclonal antibody to human immunodeficiency virus type 1 which mediates cellular cytotoxicity and neutralization. J. Virol., 64:936-940, 1990. PubMed ID: 2296090. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 284

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MAb ID T7.1
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 4 of 4 reference.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 285

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MAb ID T9
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(gp120 91-100 LAI)
Research Contact Lennart Akerblom, Britta Wahren and Jorma Hinkula
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 5 of 5 references.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.


Displaying record number 286

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MAb ID 5B3
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp160

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Berman1991 P. W. Berman, K. Rosenthal, G. Nakamura, L. Riddle, J. P. Porter, D. Dowbenko, M. Hobbes, R. Byrn, J. Groopman, T. Gregory, and B. Fendly. Monoclonal Antibodies to gp160 of HIV-1 That Neutralize HIV-1 Infectivity, Block the Binding of gp120 to CD4, and React with Diverse Isolates. J. Acquir. Immune Defic. Syndr., 4:306, 1991. Show all entries for this paper.

Nakamura1992 G. R. Nakamura, R. Byrn, K. Rosenthal, J. P. Porter, M. R. Hobbs, L. Riddle, D. J. Eastman, D. Dowbenko, T. Gregory, B. M. Fendly, and P. W. Berman. Monoclonal Antibodies to the Extracellular Domain of HIV-1 IIIB gp160 That Neutralize Infectivity, Block Binding to CD4 React with Diverse Isolates. AIDS Res. Hum. Retroviruses, 8:1875-1885, 1992. PubMed ID: 1283308. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 287

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MAb ID MF49.1
HXB2 Location Env(91-100)
DNA(6495..6524)
Env Epitope Map
Author Location gp120(91-100 LAI)
Epitope ENFDMWKNDM Epitope Alignment
ENFDMWKNDM epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 288

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MAb ID B20
HXB2 Location Env(101-110)
DNA(6525..6554)
Env Epitope Map
Author Location gp120(101-110 LAI)
Epitope VEQMHEDIIS Epitope Alignment
VEQMHEDIIS epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 289

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MAb ID B18
HXB2 Location Env(101-110)
DNA(6525..6554)
Env Epitope Map
Author Location gp120(101-110 LAI)
Epitope VEQMHEDIIS Epitope Alignment
VEQMHEDIIS epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 290

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MAb ID MF39.1 (39.1)
HXB2 Location Env(101-110)
DNA(6525..6554)
Env Epitope Map
Author Location gp120(101-110 LAI)
Epitope VEQMHEDIIS Epitope Alignment
VEQMHEDIIS epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 291

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MAb ID T2.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Research Contact Lennart Akerblom, Britta Wahren and Jorma Hinkula
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 4 of 4 reference.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 293

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MAb ID 6D8
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) rat
Patient  
Immunogen vaccine
Keywords antibody generation

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Isolation Paper
Dowbenko1988 D. Dowbenko, G. Nakamura, C. Fennie, C. Shimasaki, L. Riddle, R. Harris, T. Gregory, and L. Lasky. Epitope mapping of the immunodeficiency virus type 1 gp120 with monoclonal antibodies. J. Virol., 62:4703-4711, 1988. PubMed ID: 2460639. Show all entries for this paper.

Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Nakamura1992 G. R. Nakamura, R. Byrn, K. Rosenthal, J. P. Porter, M. R. Hobbs, L. Riddle, D. J. Eastman, D. Dowbenko, T. Gregory, B. M. Fendly, and P. W. Berman. Monoclonal Antibodies to the Extracellular Domain of HIV-1 IIIB gp160 That Neutralize Infectivity, Block Binding to CD4 React with Diverse Isolates. AIDS Res. Hum. Retroviruses, 8:1875-1885, 1992. PubMed ID: 1283308. Show all entries for this paper.


Displaying record number 294

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MAb ID M96
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 295

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MAb ID 37.1.1 (37.1, ARP 327, ARP327)
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Research Contact Claudine Bruck
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody interactions

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. 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.


Displaying record number 296

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MAb ID 187.2.1 (187.1)
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Research Contact Claudine Bruck and Clothilde Thiriart
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 4 of 4 notes.

References

Showing 5 of 5 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. 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.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 297

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MAb ID MF58.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

References

Showing 2 of 2 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 298

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MAb ID MF77.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 299

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MAb ID MF119.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 300

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MAb ID MF4.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 301

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MAb ID MF53.1
HXB2 Location Env(101-120)
DNA(6525..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope VEQMHEDIISLWDQSLKPCV Epitope Alignment
VEQMHEDIISLWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 309

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MAb ID W1
HXB2 Location Env(102-121)
DNA(6528..6587)
Env Epitope Map
Author Location gp120(102-121 LAI)
Research Contact D. Weiner, U. Penn.
Epitope EQMHEDIISLWDQSLKPCVK Epitope Alignment
EQMHEDIISLWDQSLKPCVK epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 307

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MAb ID 12G10
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.


Displaying record number 303

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MAb ID 135/9 (87-135/9)
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(111-120 LAI)
Research Contact Matthias Niedrig
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing L
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade IIIB
Vaccine component gp120

Notes

Showing 8 of 8 notes.

References

Showing 9 of 9 references.

Niedrig1992 M. Niedrig, H.-P. Harthus, M. Broker, H. Bickhard, G. Pauli, H. R. Gelderblom, and B. Wahren. Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120. J. Gen. Virol., 73:2451-2455, 1992. PubMed ID: 1383412. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. 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.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.


Displaying record number 304

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MAb ID MF46.1
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

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References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 305

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MAb ID C4
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Research Contact George Lewis
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 306

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MAb ID 11
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 308

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MAb ID 7C10
HXB2 Location Env(111-120)
DNA(6555..6584)
Env Epitope Map
Author Location gp120(101-120 LAI)
Epitope LWDQSLKPCV Epitope Alignment
LWDQSLKPCV epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

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References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 312

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MAb ID 6D5
HXB2 Location Env(122-141)
DNA(6588..6647)
Env Epitope Map
Author Location gp120(122-141 LAI)
Research Contact S. Nigida and L. Arthur, NCI, Frederick, MD USA
Epitope LTPLCVSLKCTDLKNDTNTN Epitope Alignment
LTPLCVSLKCTDLKNDTNTN epitope logo
Subtype B
Ab Type gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 348

Download this epitope record as JSON.

MAb ID 3D3.B8
HXB2 Location Env(211-221)
DNA(6855..6887)
Env Epitope Map
Author Location gp120(211-220 LAI)
Epitope EPIPIHYCAPA Epitope Alignment
EPIPIHYCAPA epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 349

Download this epitope record as JSON.

MAb ID 4C11.D8
HXB2 Location Env(211-221)
DNA(6855..6887)
Env Epitope Map
Author Location gp120(211-220 LAI)
Epitope EPIPIHYCAPA Epitope Alignment
EPIPIHYCAPA epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgM)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 350

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MAb ID 322-151
HXB2 Location Env(211-221)
DNA(6855..6887)
Env Epitope Map
Author Location gp120(201-220 LAI)
Research Contact G. Robey, Abbot Labs
Epitope EPIPIHYCAPA Epitope Alignment
EPIPIHYCAPA epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 352

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MAb ID 493-156
HXB2 Location Env(211-230)
DNA(6855..6914)
Env Epitope Map
Author Location gp120(211-230 LAI)
Research Contact G. Robey, Abbot Labs
Epitope EPIPIHYCAPAGFAILKCNN Epitope Alignment
EPIPIHYCAPAGFAILKCNN epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 354

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MAb ID J1
HXB2 Location Env(222-231)
DNA(6888..6917)
Env Epitope Map
Author Location gp120(222-231 LAI)
Research Contact J. Hoxie, U. Penn.
Epitope GFAILKCNNK Epitope Alignment
GFAILKCNNK epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain B clade LAI

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 355

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MAb ID J3
HXB2 Location Env(222-231)
DNA(6888..6917)
Env Epitope Map
Author Location gp120(222-231 LAI)
Research Contact J. Hoxie, U. Penn.
Epitope GFAILKCNNK Epitope Alignment
GFAILKCNNK epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain B clade LAI

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 references.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 356

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MAb ID MF87.1
HXB2 Location Env(252-261)
DNA(6978..7007)
Env Epitope Map
Author Location gp120(242-261 LAI)
Epitope RPVVSTQLLL Epitope Alignment
RPVVSTQLLL epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 357

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MAb ID MF169.1
HXB2 Location Env(252-261)
DNA(6978..7007)
Env Epitope Map
Author Location gp120(242-261 LAI)
Epitope RPVVSTQLLL Epitope Alignment
RPVVSTQLLL epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 3 of 3 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 358

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MAb ID MF170.1
HXB2 Location Env(252-261)
DNA(6978..7007)
Env Epitope Map
Author Location gp120(242-261 LAI)
Epitope RPVVSTQLLL Epitope Alignment
RPVVSTQLLL epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 3 of 3 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.


Displaying record number 363

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MAb ID 213.1
HXB2 Location Env(252-261)
DNA(6978..7007)
Env Epitope Map
Author Location gp120(242-261 LAI)
Research Contact Claudine Bruck
Epitope RPVVSTQLLL Epitope Alignment
RPVVSTQLLL epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 364

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MAb ID M89
HXB2 Location Env(252-271)
DNA(6978..7037)
Env Epitope Map
Author Location gp120(252-271 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.


Displaying record number 365

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MAb ID B12
HXB2 Location Env(252-271)
DNA(6978..7037)
Env Epitope Map
Author Location gp120(252-271 LAI)
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody generation

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 4 of 4 notes.

References

Showing 3 of 3 references.

Isolation Paper
Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 375

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MAb ID C13
HXB2 Location Env(252-271)
DNA(6978..7037)
Env Epitope Map
Author Location gp120(252-271 LAI)
Research Contact George Lewis
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 5 of 5 notes.

References

Showing 4 of 4 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

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.

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 376

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MAb ID 110.E
HXB2 Location Env(262-281)
DNA(7008..7067)
Env Epitope Map
Author Location gp120(262-281 LAI)
Research Contact F. Traincard
Epitope NGSLAEEEVVIRSVNFTDNA Epitope Alignment
NGSLAEEEVVIRSVNFTDNA epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 377

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MAb ID 110.C
HXB2 Location Env(271-280)
DNA(7035..7064)
Env Epitope Map
Author Location gp120(271-280 LAI)
Research Contact F. Traincard, Hybridolabs, Institut Pasteur
Epitope VIRSVNFTDN Epitope Alignment
VIRSVNFTDN epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 438

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MAb ID 110.I
HXB2 Location Env(316-322)
DNA(7170..7190)
Env Epitope Map
Author Location gp120(316-322)
Research Contact F. Traincard, Pasteur Institute, France
Epitope AFVTIGK Epitope Alignment
AFVTIGK epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing L
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component gp120

Notes

Showing 6 of 6 notes.

References

Showing 7 of 7 references.

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. 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.

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.

Poignard1996b P. Poignard, T. Fouts, D. Naniche, J. P. Moore, and Q. J. Sattentau. Neutralizing antibodies to human immunodeficiency virus type-1 gp120 induce envelope glycoprotein subunit dissociation. J. Exp. Med., 183:473-484, 1996. Binding of Anti-V3 and the CD4I neutralizing MAbs induces shedding of gp120 on cells infected with the T-cell line-adapted HIV-1 molecular clone Hx10. This was shown by significant increases of gp120 in the supernatant, and exposure of a gp41 epitope that is masked in the oligomer. MAbs binding either to the V2 loop or to CD4BS discontinuous epitopes do not induce gp120 dissociation. This suggests HIV neutralization probably is caused by several mechanisms, and one of the mechanisms may involve gp120 dissociation. PubMed ID: 8627160. Show all entries for this paper.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. 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.


Displaying record number 523

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MAb ID 4D7/4
HXB2 Location Env(360-380)
DNA(7302..7364)
Env Epitope Map
Author Location gp120(361-380 LAI)
Research Contact S. Ranjbar, NIBSC, UK
Epitope IFKQSSGGDPEIVTHSFNCGG Epitope Alignment
Subtype B
Ab Type gp120 V4
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 1 of 1 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 524

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MAb ID 36.1(ARP 329)
HXB2 Location Env(361-381)
DNA(7305..7367)
Env Epitope Map
Author Location gp120(362-381 LAI)
Epitope FKQSSGGDPEIVTHSFNCGGE Epitope Alignment
Subtype B
Ab Type gp120 V4
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 525

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MAb ID C12
HXB2 Location Env(361-381)
DNA(7305..7367)
Env Epitope Map
Author Location gp120(362-381 LAI)
Research Contact George Lewis
Epitope FKQSSGGDPEIVTHSFNCGGE Epitope Alignment
Subtype B
Ab Type gp120 CD4i, gp120 V4
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody sequence, co-receptor, review

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 8 of 8 notes.

References

Showing 9 of 9 references.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Choe2003 Hyeryun Choe, Wenhui Li, Paulette L. Wright, Natalya Vasilieva, Miro Venturi, Chih-Chin Huang, Christoph Grundner, Tatyana Dorfman, Michael B. Zwick, Liping Wang, Eric S. Rosenberg, Peter D. Kwong, Dennis R. Burton, James E. Robinson, Joseph G. Sodroski, and Michael Farzan. Tyrosine Sulfation of Human Antibodies Contributes to Recognition of the CCR5 Binding Region of HIV-1 gp120. Cell, 114(2):161-170, 25 Jul 2003. PubMed ID: 12887918. Show all entries for this paper.

Dorfman2006 Tatyana Dorfman, Michael J. Moore, Alexander C. Guth, Hyeryun Choe, and Michael Farzan. A Tyrosine-Sulfated Peptide Derived from the Heavy-Chain CDR3 Region of an HIV-1-Neutralizing Antibody Binds gp120 and Inhibits HIV-1 Infection. J. Biol. Chem., 281(39):28529-28535, 29 Sep 2006. PubMed ID: 16849323. Show all entries for this paper.

Lin2007 George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.

Liao2013a Hongyan Liao, Jun-tao Guo, Miles D. Lange, Run Fan, Michael Zemlin, Kaihong Su, Yongjun Guan, and Zhixin Zhang. Contribution of V(H) Replacement Products to the Generation of Anti-HIV Antibodies. Clin. Immunol., 146(1):46-55, Jan 2013. PubMed ID: 23220404. Show all entries for this paper.


Displaying record number 526

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MAb ID 110.D
HXB2 Location Env(380-393)
DNA(7362..7403)
Env Epitope Map
Author Location gp120(380-393 LAI)
Research Contact F. Traincard, Pasteur Institute, France
Epitope GEFFYCNSTQLFNS Epitope Alignment
GEFFYCNSTQLFNS epitope logo
Subtype B
Ab Type gp120 C3
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 527

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MAb ID B32
HXB2 Location Env(380-393)
DNA(7362..7403)
Env Epitope Map
Author Location gp120(380-393 LAI)
Epitope GEFFYCNSTQLFNS Epitope Alignment
GEFFYCNSTQLFNS epitope logo
Subtype B
Ab Type gp120 C3
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.


Displaying record number 561

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MAb ID M91
HXB2 Location Env(461-470)
DNA(7605..7634)
Env Epitope Map
Author Location gp120(451-470 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope SNNESEIFRL Epitope Alignment
SNNESEIFRL epitope logo
Subtype B
Ab Type gp120 V5-C5
Neutralizing no
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords antibody interactions

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 7 of 7 notes.

References

Showing 8 of 8 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.

Zwick2003a Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015. Show all entries for this paper.


Displaying record number 562

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MAb ID CRA1 (CRA-1, CRA1, ARP 323, ARP323)
HXB2 Location Env(461-470)
DNA(7605..7634)
Env Epitope Map
Author Location gp120(451-470 LAI)
Research Contact M. Page, NIBSC, UK
Epitope SNNESEIFRL Epitope Alignment
SNNESEIFRL epitope logo
Subtype B
Ab Type gp120 V5-C5
Neutralizing no
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody interactions

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 9 of 9 notes.

References

Showing 8 of 8 references.

Koefoed2005 Klaus Koefoed, Lauge Farnaes, Meng Wang, Arne Svejgaard, Dennis R. Burton, and Henrik J. Ditzel. Molecular Characterization of the Circulating Anti-HIV-1 gp120-Specific B Cell Repertoire using Antibody Phage Display Libraries Generated from Pre-Selected HIV-1 gp120 Binding PBLs. J. Immunol. Methods, 297(1-2):187-201, Feb 2005. PubMed ID: 15777942. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. 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.

Yang2000 Xinzhen Yang, Michael Farzan, Richard Wyatt, and Joseph Sodroski. Characterization of Stable, Soluble Trimers Containing Complete Ectodomains of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins. J. Virol., 74(12):5716-5725, Jun 2000. PubMed ID: 10823881. Show all entries for this paper.


Displaying record number 563

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MAb ID 9301
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact Dupont, commercial
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 5 of 5 references.

Skinner1988 M. A. Skinner, R. Ting, A. J. Langlois, K. J. Weinhold, H. K. Lyerly, K. Javaherian, and T. J. Matthews. Characteristics of a Neutralizing Monoclonal Antibody to the HIV Envelope Glycoprotein. AIDS Res. Hum. Retroviruses, 4:187-197, 1988. PubMed ID: 2456088. 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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Wagner1996 R. Wagner, L. Deml, R. Schirmbeck, M. Niedrig, J. Reimann, and H. Wolf. Construction, Expression, and Immunogenicity of Chimeric HIV-1 Virus-Like Particles. Virology, 220:128-140, 1996. PubMed ID: 8659105. Show all entries for this paper.


Displaying record number 567

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MAb ID 1C1
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact Repligen Inc, Cambridge, MA, commercial
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody interactions

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 5 of 5 notes.

References

Showing 5 of 5 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

VanCott1995 T. C. VanCott, F. R. Bethke, D. S. Burke, R. R. Redfield, and D. L. Birx. Lack of Induction of Antibodies Specific for Conserved, Discontinuous Epitopes of HIV-1 Envelope Glycoprotein by Candidate AIDS Vaccines. J. Immunol., 155:4100-4110, 1995. The Ab response in both HIV-1 infected and uninfected volunteers immunized with HIV-1 rec envelope subunit vaccines (Genentech gp120IIIB, MicroGeneSys gp160IIIB, or ImmunoAG gp160IIIB) preferentially induced Abs reactive only to the denatured form of gp120. This may explain the inability of the vaccinee sera to neutralize primary HIV-1 isolates. PubMed ID: 7561123. 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.

Zwick2003a Michael B. Zwick, Robert Kelleher, Richard Jensen, Aran F. Labrijn, Meng Wang, Gerald V. Quinnan, Jr., Paul W. H. I. Parren, and Dennis R. Burton. A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12. J. Virol., 77(12):6965-6978, Jun 2003. PubMed ID: 12768015. Show all entries for this paper.


Displaying record number 568

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MAb ID B221 (221)
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact Rod Daniels
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody interactions, dendritic cells, neutralization

Vaccine Details

Vaccine type protein
Vaccine strain B clade NL43
Vaccine component gp160

Notes

Showing 8 of 8 notes.

References

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.

Bristow1994 R. G. W. Bristow, A. R. Douglas, J. J. Skehel, and R. S Daniels. Analysis of murine antibody responses to baculovirus-expressed human immunodeficiency virus type 1 envelope glycoproteins. J. Gen. Virol., 75:2089-2095, 1994. BALB/c mice were immunized with baculovirus expressed gp160 or gp120, and 15 MAbs were generated. No MAbs generated in this study neutralized reference strains, using a tetrazolium-based cytotoxicity assay to test for neutralization. Ten of the Mabs were mapped by peptide ELISA, and seven reacted with the C1 region, one with V2, one with V4, and one with the C-terminal end. PubMed ID: 7519249. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. 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.

Billington2007 J. Billington, T. P. Hickling, G. H. Munro, C. Halai, R. Chung, G. G. Dodson, and R. S. Daniels. Stability of a Receptor-Binding Active Human Immunodeficiency Virus Type 1 Recombinant gp140 Trimer Conferred by Intermonomer Disulfide Bonding of the V3 Loop: Differential Effects of Protein Disulfide Isomerase on CD4 and Coreceptor Binding. J. Virol., 81(9):4604-4614, May 2007. PubMed ID: 17301129. 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.


Displaying record number 569

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MAb ID 660-178
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact G. Robey, Abbott Labs
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 570

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MAb ID 8C6/1
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact S. Ranjbar, NIBSC, UK
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 V5-C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI

Notes

Showing 2 of 2 notes.

References

Showing 1 of 1 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 571

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MAb ID 5F4/1
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact S. Ranjbar, NIBSC, UK
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain HIV-2 ROD

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 572

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MAb ID 3F5
HXB2 Location Env(471-490)
DNA(7635..7694)
Env Epitope Map
Author Location gp120(471-490 LAI)
Research Contact S. Nigida, NCI, USA
Epitope GGGDMRDNWRSELYKYKVVK Epitope Alignment
GGGDMRDNWRSELYKYKVVK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 576

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MAb ID W2
HXB2 Location Env(472-491)
DNA(7638..7697)
Env Epitope Map
Author Location gp120(472-491 LAI)
Research Contact D. Weiner, U. Penn., USA
Epitope GGDMRDNWRSELYKYKVVKI Epitope Alignment
GGDMRDNWRSELYKYKVVKI epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 1 of 1 note.

References

Showing 1 of 1 reference.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 580

Download this epitope record as JSON.

MAb ID RV110026
HXB2 Location Env(491-500)
DNA(7695..7724)
Env Epitope Map
Author Location gp120(491-500 LAI)
Research Contact Commercial, Olympus Inc
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) human
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain B clade LAI

Notes

Showing 2 of 2 notes.

References

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.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.


Displaying record number 581

Download this epitope record as JSON.

MAb ID 110.1 (110-1)
HXB2 Location Env(491-500)
DNA(7695..7724)
Env Epitope Map
Author Location gp120(491-500 LAI)
Research Contact Genetic Systems Corp, Seattle WA, E. Kinney-Thomas
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing no
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, immunotoxin

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade BRU
Vaccine component HIV-1

Notes

Showing 11 of 11 notes.

References

Showing 12 of 12 references.

Isolation Paper
Gosting1987 L. H. Gosting, J. McClure, E. S. Dickinson, S. M. Watanabe, K. Shriver, and L. C. Goldstein. Monoclonal antibodies to gp110 and gp41 of human immunodeficiency virus. J. Clin. Microbiol., 25:845-848, 1987. PubMed ID: 2438302. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Linsley1988 P. S. Linsley, J. A. Ledbetter, E. Kinney-Thomas, and S.-L. Hu. Effects of Anti-gp120 Monoclonal Antibodies on CD4 Receptor Binding by the env Protein of Human Immunodeficiency Virus Type 1. J. Virol., 62:3695-3702, 1988. PubMed ID: 2458487. Show all entries for this paper.

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.

McDougal1996 J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.


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