Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Structure of an anti‐HIV monoclonal Fab antibody fragment specific to a gp120 C‐4 region peptide

Structure of an anti‐HIV monoclonal Fab antibody fragment specific to a gp120 C‐4 region peptide <h1>Introduction.</h1> The structures of antibodies raised against peptides representing HIV‐1 epitopes are of intrinsic interest in the battle against AIDS. Antibodies that neutralize the virus, effectively stopping its reproduction, are of particular interest because the structure of a neutralizing antibody should contain information concerning the way neutralization can be accomplished. To that end, structures have been published describing neutralizing antibodies raised against representatives of the third hypervariable region (V3) of the HIV‐1 envelope glycoprotein subunit, gp120 (Fabs 59.1, 58.2, and 50.1, PDB accession numbers 1ACY, 1F58, and 1GGC). The subregion from which the peptides derive, amino acid residues 308–332, is known as the principal neutralization determinant (PND). Unfortunately, it is encoded by one of the most mutation prone sequences of the HIV genome, and the neutralizing capability of an antibody against the PND does not often generalize to mutated strains. The hope has been that structures would provide a basis for understanding how to completely neutralize the virus using antibodies, but this hope has not yet been realized. The neutralizing antibody investigated here, G3‐519, recognizes an epitope from the fourth conserved region (C4) of gp120 that plays an important role in interaction with CD4 (see details below). It http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Proteins: Structure Function and Bioinformatics Wiley

Structure of an anti‐HIV monoclonal Fab antibody fragment specific to a gp120 C‐4 region peptide

Download PDF
2 pages

Loading next page...
 
/lp/wiley/structure-of-an-anti-hiv-monoclonal-fab-antibody-fragment-specific-to-eWyUOZ215N

References (12)

Publisher
Wiley
Copyright
Copyright © 2001 Wiley Subscription Services
ISSN
0887-3585
eISSN
1097-0134
DOI
10.1002/prot.1148
Publisher site
See Article on Publisher Site

Abstract

<h1>Introduction.</h1> The structures of antibodies raised against peptides representing HIV‐1 epitopes are of intrinsic interest in the battle against AIDS. Antibodies that neutralize the virus, effectively stopping its reproduction, are of particular interest because the structure of a neutralizing antibody should contain information concerning the way neutralization can be accomplished. To that end, structures have been published describing neutralizing antibodies raised against representatives of the third hypervariable region (V3) of the HIV‐1 envelope glycoprotein subunit, gp120 (Fabs 59.1, 58.2, and 50.1, PDB accession numbers 1ACY, 1F58, and 1GGC). The subregion from which the peptides derive, amino acid residues 308–332, is known as the principal neutralization determinant (PND). Unfortunately, it is encoded by one of the most mutation prone sequences of the HIV genome, and the neutralizing capability of an antibody against the PND does not often generalize to mutated strains. The hope has been that structures would provide a basis for understanding how to completely neutralize the virus using antibodies, but this hope has not yet been realized. The neutralizing antibody investigated here, G3‐519, recognizes an epitope from the fourth conserved region (C4) of gp120 that plays an important role in interaction with CD4 (see details below). It

Journal

Proteins: Structure Function and Bioinformatics – Wiley

Published: Jan 15, 2001

There are no references for this article.