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Research Article Free access | 10.1172/JCI118122

Identification of an idiotypic peptide recognized by autoantibodies in human immunodeficiency virus-1-infected individuals.

Q L Wang, H T Wang, E Blalock, S Müller, and H Köhler

Markey Cancer Center, University of Kentucky Medical Center, Lexington 40536-0096, USA.

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Markey Cancer Center, University of Kentucky Medical Center, Lexington 40536-0096, USA.

Find articles by Wang, H. in: JCI | PubMed | Google Scholar

Markey Cancer Center, University of Kentucky Medical Center, Lexington 40536-0096, USA.

Find articles by Blalock, E. in: JCI | PubMed | Google Scholar

Markey Cancer Center, University of Kentucky Medical Center, Lexington 40536-0096, USA.

Find articles by Müller, S. in: JCI | PubMed | Google Scholar

Markey Cancer Center, University of Kentucky Medical Center, Lexington 40536-0096, USA.

Find articles by Köhler, H. in: JCI | PubMed | Google Scholar

First published August 1, 1995 - More info

Published in Volume 96, Issue 2 (August 1, 1995)
J Clin Invest. 1995;96(2):775–780. doi:10.1172/JCI118122.
Copyright © 1995, The American Society for Clinical Investigation.

Published August 1, 1995 ; Accepted: date unavailable
Abstract

Antibodies against HIV-1 proteins in HIV-1-infected individuals share a cross-reactive idiotype defined by the monoclonal antiidiotypic antibody 1F7 (5). Using a computer algorithm based on the molecular recognition theory, regions of inverse hydropathy between the variable sequence of 1F7 and human monoclonal anti-HIV-1 antibodies were identified, which are assumed to be involved in idiotype-antiidiotype contacts. A peptide was designed from the proposed contact in the variable heavy chain framework 3-complementarity determining region 3 (FR3-CDR3) of human antibodies and was synthesized. This peptide is recognized by the antiidiotype 1F7 and inhibits the binding of 1F7 to human anti-HIV-1 antibodies which express the 1F7 idiotype. A survey of normal and HIV-1-infected sera revealed the presence of antibodies in infected sera which bind to the FR3-CDR3 peptide. The biological relevance of autoantibodies against a self idiotope associated with HIV-1 infection is discussed in the context of the regulation of the antibody response to HIV-1.

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