A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity

Elinor M. Schad, Anastassios C. Papageorgiou, L. Anders Svensson, K. Ravi Acharya

Research output: Contribution to journalArticle

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Staphylococcal enterotoxins and toxic shock syndrome toxin-1 are known as superantigens due to their ability to activate a large number of T-cells by crosslinking the major histocompatibility complex class II molecules with the T-cell receptor. Although superantigens seem to act by a common mechanism, they vary in many of their specific interactions and biological properties. A structural comparison of staphylococcal enterotoxins A and C2, members of the staphylococcal superantigens, has shown large conformational differences at the putative TcR interaction site (loops between αN-α2, α4-β9 and β10-α5 in staphylococcal enterotoxin A) that could explain the variability in their T-cell receptor specificity. A common Zn2+-binding site was identified in both staphylococcal enterotoxin A and C2 that is superimposable but differs somewhat in its coordination geometry between the two molecules.

Original languageEnglish
Pages (from-to)270-280
Number of pages11
JournalJournal of Molecular Biology
Issue number2
Publication statusPublished - 6 Jun 1997


  • MHC class II
  • Staphylococcal enterotoxins
  • Superantigen
  • T-cell receptor
  • X-ray crystallography

ASJC Scopus subject areas

  • Molecular Biology

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