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Found 3 matching records:

Displaying record number 269

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MAb ID 1D10
HXB2 Location gp160(81-100)
DNA(6465..6524)
gp160 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 286

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MAb ID 5B3
HXB2 Location gp160(91-100)
DNA(6495..6524)
gp160 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 666

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MAb ID 6E10
HXB2 Location Env Env Epitope Map
Author Location gp120
Research Contact Phil Berman
Epitope
Ab Type  
Neutralizing L
Species (Isotype)  
Patient  
Immunogen  
Keywords binding affinity

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 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.

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.

Yu2010 Bin Yu, Dora P. A. J. Fonseca, Sara M. O'Rourke, and Phillip W. Berman. Protease Cleavage Sites in HIV-1 gp120 Recognized by Antigen Processing Enzymes Are Conserved and Located at Receptor Binding Sites. J. Virol., 84(3):1513-1526, Feb 2010. PubMed ID: 19939935. Show all entries for this paper.


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