HIV molecular immunology database

 

Search Antibody Database

Found 1 matching record:

Displaying record number 262

Download this epitope record as JSON.

MAb ID 133/237
HXB2 Location gp160(61-70)
DNA(6405..6434)
gp160 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.


Questions or comments? Contact us at immuno@lanl.gov
 
Managed by Triad National Security, LLC for the U.S. Department of Energy’s National Nuclear Security Administration
Copyright © 2022 Triad National Security, LLC | Disclaimer/Privacy

Dept of Health & Human Services Los Alamos National Institutes of Health