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Alloantibodies can discriminate class I major histocompatibility complex molecules associated with various endogenous peptides

Academic Article
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Overview

authors

  • Sherman, Linda
  • Chattopadhyay, S.
  • Biggs, J. A.
  • Dick, R. F.
  • Bluestone, J. A.

publication date

  • August 1993

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Molecules encoded by a single major histocompatibility complex class I gene can associate with any one of a large number of peptide ligands. T-cell receptors have the capacity to discriminate among these peptide-class I complexes and in many cases bind only a single peptide-class I complex with sufficient affinity to trigger effector function. In contrast, it is generally assumed that class I-specific alloantibodies are indifferent to peptide heterogeneity, being directed toward allele-specific determinants on the molecule. In this report, three monoclonal antibodies were used to precipitate Kb molecules from cell lysates. Surprisingly, in each case a different set of peptides was found to be associated with Kb as detected by peptide-dependent Kb-specific alloreactive cytolytic T lymphocytes or by biochemical resolution. These results demonstrate that the affinity of binding by alloantibodies can be affected by the endogenous peptide ligand.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antigens
  • Cytotoxicity, Immunologic
  • H-2 Antigens
  • Immunity, Cellular
  • In Vitro Techniques
  • Isoantibodies
  • Macromolecular Substances
  • Mice
  • Mice, Inbred C57BL
  • Peptides
  • T-Lymphocytes, Cytotoxic
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Identity

PubMed Central ID

  • PMC47052

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.90.15.6949

PubMed ID

  • 8346201
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Additional Document Info

start page

  • 6949

end page

  • 6951

volume

  • 90

issue

  • 15

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