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Mimicking the alloantigenicity of proteins with chemically synthesized peptides differing in single amino acids.

Authors
  • Alexander, H
  • Johnson, D A
  • Rosen, J
  • Jerabek, L
  • Green, N
  • Weissman, I L
  • Lerner, R A
Type
Published Article
Journal
Nature
Publication Date
Jan 01, 1983
Volume
306
Issue
5944
Pages
697–699
Identifiers
PMID: 6656870
Source
Medline
License
Unknown

Abstract

Recent studies have shown that short chemically synthesized peptides very often induce antibodies which react with the cognate sequence in the intact folded protein. Since such antibodies react with known regions of proteins, they are of predetermined specificity and offer a precision not previously possible with immunological probes. A basic concept emerging from the use of such antibodies in viral systems is that the differential immunogenicity of closely related proteins can be mimicked by short peptides which span the regions of sequence variation. To generalize this concept, we have studied the two Thy-1 proteins which vary by only a single amino acid. Chemically synthesized peptides differing in only one out of 19 amino acids were able to induce allospecific antisera. Thus, single amino acid changes have similar effects on the immunogenicity of proteins and small peptides, even though the latter are free from constraints provided by neighbouring structures in the tertiary configuration of the intact folded proteins.

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