NMR study and comparison of the antigenic properties of a peptide recognized by two HIV-1 neutralizing antibodies.

Important note: Information in this article was accurate in 1999. The state of the art may have changed since the publication date.

NMR study and comparison of the antigenic properties of a peptide recognized by two HIV-1 neutralizing antibodies.

J Mol Recognit. 1997 Nov-Dec;10(6):256-61. Unique Identifier : AIDSLINE MED/98443588
Tsang P; Mu X; Wu G; Durda PJ; Department of Chemistry, University of Cincinnati, OH 45221-0172,; USA.

Abstract: Fab-peptide complexes formed between a 15 residue peptide derived from the HIV-1 gp120 V3 loop and two of its cognate monoclonal antibodies, 5023A and 5025A, were studied using isotope-edited solution nuclear magnetic resonance (NMR) techniques. Since these antibodies neutralize HIV-1 virus with different strain specificities, this study was conducted to better understand the nature of these differences. The amide proton and nitrogen NMR resonances of specific residues were used to monitor the backbone of this peptide in these complexes. Three central residues of this peptide ('RAF') were found to be strongly affected by binding to both antibodies. Several other peptide residues were affected by binding to antibody 5023A but not 5025A. The antibody epitopes mapped by NMR are similar to those obtained previously via PEPSCAN at higher pH. One main difference between the PEPSCAN and NMR determined epitopes for 5023A involved two glycine residues of the peptide. By NMR, one of these glycines was more dramatically affected by antibody binding than predicted by PEPSCAN, while the other was much less so.

Keywords: JOURNAL ARTICLE Antibodies, Monoclonal Antibody Affinity *Antigen-Antibody Complex Binding Sites, Antibody/IMMUNOLOGY Enzyme-Linked Immunosorbent Assay Epitopes/*CHEMISTRY/IMMUNOLOGY Hydrogen-Ion Concentration HIV Antibodies/*IMMUNOLOGY/METABOLISM HIV Envelope Protein gp120/CHEMISTRY/*IMMUNOLOGY HIV-1/*IMMUNOLOGY Immunoglobulins, Fab/IMMUNOLOGY/METABOLISM Isotopes Neutralization Tests Nuclear Magnetic Resonance Peptide Fragments/CHEMISTRY/*IMMUNOLOGY Support, U.S. Gov't, P.H.S.
990228
A9920925

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