Antibody recognition of amino acid divergence within an HIV-1 neutralization epitope.

Research in Virology
J GoudsmitF de Wolf

Abstract

Antibodies elicited by HIV-1 strains, and which neutralize such strains in vitro, bind to synthetic peptides of 5-8 amino acids in length. These amino acids, although variable, have a fixed location between two cysteines in the carboxyl terminus of the HIV-1 external envelope. Nine peptides of 9 amino acids corresponding to the gp120 domains of European and American (LAV-1, NY5, CDC4, SF2), Haitian (RF) and African (ELI, MAL, Z3, Z6) HIV-1 strains, were synthesized using LAV-1 and RF neutralization epitopes as models. Serum of chimpanzees infected with LAV-1, HTLV-IIIB or HTLV-IIIRF reacted predominantly with the homologous peptide, although cross-reactivity with heterologous peptides occurred: 8 out of 11 human sera with HTLV-IIIB-neutralizing activity bound the LAV-1/HTLV-IIIB peptide, and 6 out of 7 sera with HTLV-IIIRF-neutralizing activity bound the RF peptide. African sera reacted most frequently with the Z3 peptide (78%) while only 35% (p = 0.0001) of European and 20% (p less than 0.0001) of American sera recognized it. Recognition patterns of children from the USA and Europe were different. Although multiple reactivities were observed, blocking experiments favoured cross-reactivity as the explanation. Based on the antib...Continue Reading

References

Mar 15, 1979·Journal of Molecular Evolution·T MiyataT Yasunaga
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Jun 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·J GoudsmitD C Gajdusek

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Citations

Jun 17, 2000·Journal of Virological Methods·S C HsuW J Syu
Oct 27, 1998·AIDS Research and Human Retroviruses·J L MellquistS H Eshleman
Apr 1, 1991·Brain Pathology·C L AchimC A Wiley

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