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The chemistry of site-directed serology for HIV infections

Academic Article
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Overview

authors

  • Norrby, E.
  • Biberfeld, G.
  • Johnson, P. R.
  • Parks, D. E.
  • Houghten, R. A.
  • Lerner, Richard

publication date

  • October 1989

journal

  • AIDS Research and Human Retroviruses  Journal

abstract

  • The advent of site-directed serology has provided a specific and simplified means of distinguishing antibody responses to the two types of human immunodeficiency virus (HIV) in an outbred population. Remarkably, human sera containing HIV antibodies and simian sera containing simian immunodeficiency virus (SIV) antibodies had a very narrow amino acid dependence in the 23 residue long peptide, 582Ala-604Cys, used as antigen. A single dominating antigenic site was demonstrated in the C-terminal part of the peptide--596Trp-602Gln for HIV-2 and SIV antibodies and 597Gly-602Leu for HIV-1. A minor fraction of HIV-1 antibodies also reacted with a second site, 588Lys and 589Asp. These data define the precise amino acid dependence of a uniquely immunogenic site in the folded transmembrane protein of HIV and facilitate the optimizing of peptide antigens for site-directed serology.

subject areas

  • Acquired Immunodeficiency Syndrome
  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Glycine
  • HIV
  • HIV Antibodies
  • HIV-1
  • HIV-2
  • Haplorhini
  • Humans
  • Simian Immunodeficiency Virus
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Identity

International Standard Serial Number (ISSN)

  • 0889-2229

Digital Object Identifier (DOI)

  • 10.1089/aid.1989.5.487

PubMed ID

  • 2480152
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Additional Document Info

start page

  • 487

end page

  • 493

volume

  • 5

issue

  • 5

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