Abstract
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 language | English |
|---|---|
| Pages (from-to) | 270-280 |
| Number of pages | 11 |
| Journal | Journal of Molecular Biology |
| Volume | 269 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 6 Jun 1997 |
Funding
We thank Don Wiley and his colleagues for providing the atomic coordinates of SEB-HLA-DR1 and TSSTHIGHL 1-HLA-DR1 complexes, Göran Carlström, Howard Tranter and Vasanta Subramanian for helpful discussions, Michael Hoffman for editing and Mikael Dohlsten and co-workers for supplying the protein material of SEA. This work is supported by the Medical Research Council, UK (K.R.A.) and the Swedish National Research Council (L.A.S.).
Keywords
- MHC class II
- Staphylococcal enterotoxins
- Superantigen
- T-cell receptor
- X-ray crystallography
ASJC Scopus subject areas
- Molecular Biology