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Cellular and humoral immune-responses to synthetic peptides deduced from the amino-acid-sequences of epstein-barr virus-encoded proteins in ebv-transformed cells

Academic Article
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Overview

authors

  • Dillner, J.
  • Szigeti, R.
  • Henle, W.
  • Henle, G.
  • Lerner, Richard
  • Klein, G.

publication date

  • October 1987

journal

  • International Journal of Cancer  Journal

abstract

  • Ten synthetic peptides containing 18-22 residues deduced from the amino-acid sequences of the EBV-encoded latent-infection-associated membrane protein (LMP) and the 2 principal nuclear antigens, EBNA-1 and EBNA-2, were tested for their ability to induce lymphokine release from sensitized T-cells of EBV-seropositive donors, as measured by the leukocyte migration inhibition assay (LMI). Only one of the 10 free peptides induced EBV-specific LMI. After Sepharose-coupling, 4 additional peptides were regularly active. In parallel, the sera of the same and other donors were screened for synthetic peptide-binding antibodies, as measured by an ELISA assay. Antibodies to 9 of the 10 peptides were detected in 25-80% of EBV-antibody-positive, but not in EBV-antibody-negative sera. A comparison of the two responses indicates that the humoral immune system tends to react with more epitopes on a given protein than the cellular immune system. Furthermore, the antibody reactivity pattern to different epitopes is more variable from individual to individual than the T-cell response. Also, the epitopes detected by antibodies and sensitized T-cells are often not identical.

subject areas

  • Amino Acid Sequence
  • Antibody Formation
  • Antigens, Viral
  • Cell Transformation, Viral
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes
  • Epstein-Barr Virus Nuclear Antigens
  • Herpesvirus 4, Human
  • Humans
  • Immunity, Cellular
  • Leukocyte Adherence Inhibition Test
  • Molecular Sequence Data
  • Peptide Fragments
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0020-7136

Digital Object Identifier (DOI)

  • 10.1002/ijc.2910400404

PubMed ID

  • 2444542
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Additional Document Info

start page

  • 455

end page

  • 460

volume

  • 40

issue

  • 4

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