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PMID: 2785644 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

High-affinity binding of staphylococcal enterotoxins A and B to HLA-DR.

Nature ·Vol. 339 ·No. 6221 ·1989-05-18 ·Pages 221-3

Fraser JD

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.

MeSH Terms
Binding Sites Cell Line Enterotoxins/metabolism HLA-DR Antigens/metabolism Humans Lymphocyte Activation T-Lymphocytes/immunology
Chemicals
Enterotoxins HLA-DR Antigens enterotoxin A, Staphylococcal enterotoxin B, staphylococcal
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Fraser J D
Department of Immunobiology, School of Medicine, University of Auckland, New Zealand.
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1989-05-18
Pages
221-3
Language
English
Region
England
NLM ID
0410462
Subset
IM
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