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Lookup NU author(s): Dr Jeong-Jin Lee, Professor Michael Kehoe, Professor John Robinson
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Bacterial superantigens are potent T-cell stimulatory protein molecules produced by Staphylococcus aureus and Streptococcus pyogenes. Their superantigenic activity can be attributed to their ability to cross-link major histocompatibility complex class II molecules with T-cell receptors (TCRs) to form a tri-molecular complex. Each superantigen is known to interact with a specific Vβ element of TCR. Staphylococcal enterotoxin B (SEB, a superantigen), a primary cause of food poisoning, is also responsible for a significant percentage of nonmenstrual associated toxic shock syndrome in patients with a variety of staphylococcal infections. Structural studies have elucidated a binding cavity on the toxin molecule essential for TCR binding. To understand the crucial residues involved in binding, mutagenesis analysis was performed. Our analysis suggest that mutation of a conserved residue Thr112 to Ser (T112S) in the binding cavity induces a selective reduction in the affinity for binding one TCR Vβ family and can be attributed to the structural differences in the native and mutant toxins. We present a detailed comparison of the mutant structure determined at 2.0 Å with the previously reported native SEB and SEB-TCR Vβ complex structures.
Author(s): Baker MD, Papageorgiou AC, Titball RW, Miller J, White S, Lingard B, Lee JJ, Cavanagh D, Kehoe MA, Robinson JH, Ravi Acharya K
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2002
Volume: 277
Issue: 4
Pages: 2756-2762
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
URL: http://dx.doi.org/10.1074/jbc.M109369200
DOI: 10.1074/jbc.M109369200
PubMed id: 11704673
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