Multiple binding sites for bacterial superantigens on soluble class II MHC molecules

Haruo Kozono, David Parker, Janice White, Philippa Marrack, John Kappler

Research output: Contribution to journalArticle

99 Scopus citations

Abstract

We used surface plasmon resonance to study the binding of a set of soluble mouse I-E class II major histocompatibility molecules, each occupied by a different single peptide, to the staphylococcal enterotoxin superantigens, SEA and SEB. The rates of association and dissociation to SEA varied greatly depending on the I-E-bound peptide. By contrast, binding to SEB yielded fast association and dissociation rates, which were relatively peptide independent. The results also indicated nonoverlapping binding sites for SEB and SEA on class II and raised the possibility of enhanced SAg presentation to T cells by cross-linking of cell surface class II.

Original languageEnglish (US)
Pages (from-to)187-196
Number of pages10
JournalImmunity
Volume3
Issue number2
DOIs
StatePublished - Aug 1995

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology
  • Infectious Diseases

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