High-affinity Binding of Staphylococcal Enterotoxins A and B to HLA-DR

Nature. 1989 May 18;339(6221):221-3. doi: 10.1038/339221a0.

Abstract

Staphylococcal enterotoxins A-E (refs 1-3), toxic shock toxin (TST-1) (ref. 1), a product of Mycoplasma arthritidis and the Mls antigens provoke dramatic T-cell responses. All are extremely potent polyclonal mitogens stimulating a large proportion of both murine and human CD4+ and CD8+T cells although activity is tightly restricted by major histocompatibility complex (MHC) class II antigens. The murine T-cell response to staphylococcal enterotoxin B (SEB) has recently been shown to involve only those T cells expressing T-cell receptor V beta 3, 8.1, 8.2 and 8.3 domains, a situation which closely mimics the response to Mls antigens. This paper examines the initial events in SEA and SEB T-cell activation and shows that MHC restriction results from a direct high affinity binding by intact SEA and SEB to the same site on MHC class II HLA-DR antigens.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Line
  • Enterotoxins / metabolism*
  • HLA-DR Antigens / metabolism*
  • Humans
  • Lymphocyte Activation
  • T-Lymphocytes / immunology*

Substances

  • Enterotoxins
  • HLA-DR Antigens
  • enterotoxin A, Staphylococcal
  • enterotoxin B, staphylococcal