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, Randall R Reed, 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 - 1987
Externally publishedYes

Fingerprint

Human Immunodeficiency Virus env Gene Products
Immunodominant Epitopes
HIV
Anti-Idiotypic Antibodies
Antibodies
Peptides
Serum
Antigens
Giant Cells
Immune Sera
Epitopes
Amino Acids

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope. / Palker, T. J.; Matthews, T. J.; Clark, M. E.; Cianciolo, G. J.; Reed, Randall R; Langlois, A. J.; White, G. C.; Safai, B.; Snyderman, R.; Bolognesi, D. P.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, No. 8, 1987, p. 2479-2483.

Research output: Contribution to journalArticle

Palker, T. J. ; Matthews, T. J. ; Clark, M. E. ; Cianciolo, G. J. ; Reed, Randall R ; Langlois, A. J. ; White, G. C. ; Safai, B. ; Snyderman, R. ; Bolognesi, D. P. / A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope. In: Proceedings of the National Academy of Sciences of the United States of America. 1987 ; Vol. 84, No. 8. pp. 2479-2483.
@article{cbcca75cbe7b4c74b28351e24cf2efa7,
title = "A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope",
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.",
author = "Palker, {T. J.} and Matthews, {T. J.} and Clark, {M. E.} and Cianciolo, {G. J.} and Reed, {Randall R} and Langlois, {A. J.} and White, {G. C.} and B. Safai and R. Snyderman and Bolognesi, {D. P.}",
year = "1987",
doi = "10.1073/pnas.84.8.2479",
language = "English (US)",
volume = "84",
pages = "2479--2483",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "8",

}

TY - JOUR

T1 - A conserved region at the COOH terminus of human immunodeficiency virus gp120 envelope protein contains an immunodominant epitope

AU - Palker, T. J.

AU - Matthews, T. J.

AU - Clark, M. E.

AU - Cianciolo, G. J.

AU - Reed, Randall R

AU - Langlois, A. J.

AU - White, G. C.

AU - Safai, B.

AU - Snyderman, R.

AU - Bolognesi, D. P.

PY - 1987

Y1 - 1987

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0011993562&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0011993562&partnerID=8YFLogxK

U2 - 10.1073/pnas.84.8.2479

DO - 10.1073/pnas.84.8.2479

M3 - Article

C2 - 2436231

AN - SCOPUS:0011993562

VL - 84

SP - 2479

EP - 2483

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 8

ER -