Structural basis of supantigen action inferred from crystal structure of toxic-shock syndrome toxin-1

K. Ravi Acharya, Edward F. Passalacqua, E. Yvonne Jones, Karl Harlos, David I. Stuart, Rossalyn D. Brehm, Howard S. Tranter

Research output: Contribution to journalArticle

Abstract

SUPERANTIGENS stimulate T cells bearing particular T-cell receptor Vβ sequences1,2, so they are extremely potent polyclonal T-cell mitogens. T-cell activation is preceded by binding of superantigens to class II major histocompatibility complex (MHC) molecules3. To further the structural characterization of these interactions, the crystal structure of a toxin associated with toxic-shock syndrome, TSST-1, which is a microbial supantigen, has been determined at 2.5 Å resolution. The N- and C-terminal domains of the structure both contain regions involved in MHC class II association; the C-terminal domain is also implicated in binding the T-cell receptor. Despite low sequence conservation, the TSST-1 topology is similar to the structure reported for the supantigen staphylococcal enterotoxin B 4. But TSST 1 lacks several of the structural features highlighted as central to supantigen activity in the staphylococcal enterotoxin B and we therefore reappraise the structural basis of supantigen action.

Original languageEnglish
Pages (from-to)94-97
Number of pages4
JournalNature
Volume367
Issue number6458
DOIs
Publication statusPublished - 1 Jan 1994

ASJC Scopus subject areas

  • General

Cite this

Acharya, K. R., Passalacqua, E. F., Jones, E. Y., Harlos, K., Stuart, D. I., Brehm, R. D., & Tranter, H. S. (1994). Structural basis of supantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. Nature, 367(6458), 94-97. https://doi.org/10.1038/367094a0