Journal article

Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1.

Beenu Moza, Ashok K Varma, Rebecca A Buonpane, Penny Zhu, Christine A Herfst, Melissa J Nicholson, Anne-Kathrin Wilbuer, Nilufer P Seth, Kai W Wucherpfennig, John K McCormick, David M Kranz, Eric J Sundberg

EMBO J | Published : 2007


Superantigens (SAGs) bind simultaneously to major histocompatibility complex (MHC) and T-cell receptor (TCR) molecules, resulting in the massive release of inflammatory cytokines that can lead to toxic shock syndrome (TSS) and death. A major causative agent of TSS is toxic shock syndrome toxin-1 (TSST-1), which is unique relative to other bacterial SAGs owing to its structural divergence and its stringent TCR specificity. Here, we report the crystal structure of TSST-1 in complex with an affinity-matured variant of its wild-type TCR ligand, human T-cell receptor beta chain variable domain 2.1. From this structure and a model of the wild-type complex, we show that TSST-1 engages TCR ligands i..

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University of Melbourne Researchers