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Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.


ABSTRACT: Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR ? chain (mV?8.2) and staphylococcal enterotoxin G (SEG) at 2.0 Å resolution revealed a binding site that does not conserve the "hot spots" present in mV?8.2-SEC2, mV?8.2-SEC3, mV?8.2-SEB, and mV?8.2-SPEA complexes. Analysis of the mV?8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mV?8.2 by SEG. This mode of interaction between SEG and mV?8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host.

SUBMITTER: Fernandez MM 

PROVIDER: S-EPMC3020726 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.

Fernández Marisa M MM   Cho Sangwoo S   De Marzi Mauricio C MC   Kerzic Melissa C MC   Robinson Howard H   Mariuzza Roy A RA   Malchiodi Emilio L EL  

The Journal of biological chemistry 20101108 2


Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the de  ...[more]

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