A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope.

Journal Article

A highly immunogenic epitope from a conserved COOH-terminal region of the human immunodeficiency virus (HIV) gp120 envelope protein has been identified with antisera from HIV-seropositive subjects and a synthetic peptide (SP-22) containing 15 amino acids from this region (Ala-Pro-Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg-Glu-Lys-Arg). Peptide SP-22 absorbed up to 100% of anti-gp120 antibody reactivity from select HIV+ patient sera in immunoblot assays and up to 79% of serum anti-gp120 antibody reactivity in competition RIA. In RIA, 45% of HIV-seropositive subjects had antibodies that bound to peptide SP-22. Human anti-SP-22 antibodies that bound to and were eluted from an SP-22 affinity column reacted with gp120 in RIA and immunoblot assays but did not neutralize HIV or inhibit HIV-induced syncytium formation in vitro, even though these antibodies comprised 70% of all anti-gp120 antibodies in the test serum. In contrast, the remaining 30% of SP-22 nonreactive anti-gp120 antibodies did not react with gp120 in immunoblot assays but did not react in RIA and neutralized HIV in vitro. Thus, approximately 50% of HIV-seropositive patients make high titers of nonneutralizing antibodies to an immunodominant antigen on gp120 defined by SP-22. Moreover, the COOH terminus of gp120 contains the major antigen or antigens identified by human anti-gp120 antibodies in immunoblot assays.

Full Text

Duke Authors

Cited Authors

  • Palker, TJ; Matthews, TJ; Clark, ME; Cianciolo, GJ; Randall, RR; Langlois, AJ; White, GC; Safai, B; Snyderman, R; Bolognesi, DP

Published Date

  • April 1, 1987

Published In

Volume / Issue

  • 84 / 8

Start / End Page

  • 2479 - 2483

PubMed ID

  • 2436231

International Standard Serial Number (ISSN)

  • 0027-8424

Language

  • eng

Conference Location

  • United States