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

T. J. Palker, T. J. Matthews, M. E. Clark, G. J. Cianciolo, R. R. Randall, A. J. Langlois, G. C. White, B. Safai, R. Snyderman, D. P. Bolognesi

Research output: Contribution to journalArticle

Abstract

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-gp 120 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 react in RIA and neutralized HIV in vitro. Thus, ~ 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.

Original languageEnglish (US)
Pages (from-to)2479-2483
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number8
DOIs
StatePublished - Jul 21 1987
Externally publishedYes

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