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Nonoverlapping T and B cell determinants on an hepatitis B surface antigen pre-S(2) region synthetic peptide

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Overview

authors

  • Milich, D. R.
  • McLachlan, A.
  • Chisari, Francis
  • Thornton, G. B.

publication date

  • August 1986

journal

  • Journal of Experimental Medicine  Journal

abstract

  • We have examined T cell recognition of a hepatitis B surface antigen (HBsAg), pre-S(2)-region synthetic peptide, p120-145, in terms of fine specificity, H-2-linked genetic influences, comparison to antibody binding, and relevance to T cell recognition of the native protein. We showed that the immune response to the synthetic peptide is regulated by H-2-linked genes, but that the pattern of H-2 restriction differed from that observed for the native anti-pre-S(2) response. Dominant and nonoverlapping T cell and B cell recognition sites were identified on the synthetic peptide p120-145. T cell recognition is focussed on the NH2-terminal sequence, and antibody (B cell) recognition is focussed on the COOH-terminal sequence. The fine specificity of T cell recognition of p120-145 was defined by a single, subtype-dependent amino acid substitution. With respect to the immunogenicity of p120-145, the synthetic peptide containing both T and B cell determinants is highly immunogenic in responder strains, whereas separate T or B cell peptide determinants are minimally immunogenic. Furthermore, the synthetic T cell recognition site can prime T cell help for antibody production to the synthetic B cell site, which is crossreactive with the native pre-S(2) region of HBsAg/p33 particles. This system provides evidence that totally synthetic T cell and B cell recognition sites can be combined to yield a functional immunogen.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies, Viral
  • B-Lymphocytes
  • Cross Reactions
  • Epitopes
  • Female
  • H-2 Antigens
  • Hepatitis B Surface Antigens
  • Mice
  • Mice, Inbred C3H
  • Mice, Inbred C57BL
  • Peptide Fragments
  • T-Lymphocytes, Helper-Inducer
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.164.2.532

PubMed ID

  • 2425034
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Additional Document Info

start page

  • 532

end page

  • 547

volume

  • 164

issue

  • 2

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