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

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

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

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,

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 in a markedly different way than do other SAGs. We provide a structural basis for the high TCR specificity of TSST-1 and present a model of the TSST-1-dependent MHC-SAG-TCR T-cell signaling complex that is structurally and energetically unique relative to those formed by other SAGs. Our data also suggest that protein plasticity plays an exceptionally significant role in this affinity maturation process that results in more than a 3000-fold increase in affinity.

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

B Moza,AK Varma,RA Buonpane,P Zhu,CA Herfst,MJ Nicholson,AK Wilbuer,NP Seth,KW Wucherpfennig,JK McCormick,DM Kranz,EJ Sundberg,

For similar biological phenomena, cell phenomena, and immunity: immunity: t-cell antigen receptor specificity research abstracts see: biological phenomena, cell phenomena, and immunity: immunity: t-cell antigen receptor specificity research

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MEDLINE DATE:

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The EMBO journal

VOLUME: 26

Page Numbers: 1187-97

Journal Abbreviation: EMBO J.

ISSN: 0261-4189

DAY: 1

MONTH: 02

YEAR: 2007

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

Number of References:

LANGUAGE: eng

NlmUniqueID: 8208664

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

KEYWORDS: T-Cell Antigen Receptor Specificity

MESH TERMS: genetics

Chemical & Substance for Abstract: Structural basis of T-cell specificity and activation by the bacterial superantigen TSST-1. Information

Substance Name: enterotoxin F, Staphylococcal

Registry Number: 0

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

AFFILIATION: Boston Biomedical Research Institute, Watertown, MA 02472, USA.

Country: England

AGENCY: United States NIGMS

GRANT: T32 GM 07283

ACRONYM: GM

MEDLINETA: EMBO J

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