Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens.

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Research Abstract Details 

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Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Abstract Text:

Jean-Nicholas P Brouillard,Sebastian ,Ashok K Varma,Irene Gryski,Christine A Herfst,A K M Nur-ur Rahman,Donald Y M Leung,Patrick M Schlievert, Madrenas,Eric J Sundberg,John K McCormick,

Superantigens (SAgs) are potent microbial toxins that bind simultaneously to T cell receptors (TCRs) and class II major histocompatibility complex molecules, resulting in the activation and expansion of large T cell subsets and the onset of numerous human diseases. Within the bacterial SAg family, streptococcal pyrogenic exotoxin I (SpeI) has been classified as belonging to the group V SAg subclass, which are characterized by a unique, relatively conserved approximately 15 amino acid extension (amino acid residues 154 to 170 in SpeI; herein referred to as the alpha3-beta8 loop), absent in SAg groups I through IV. Here, we report the crystal structure of SpeI at 1.56 A resolution. Although the alpha3-beta8 loop in SpeI is several residues shorter than that of another group V SAg, staphylococcal enterotoxin serotype I, the C-terminal portions of these loops, which are located adjacent to the putative TCR binding site, are structurally similar. Mutagenesis and subsequent functional analysis of SpeI indicates that TCR beta-chains are likely engaged in a similar general orientation as other characterized SAgs. We show, however, that the alpha3-beta8 loop length, and the presence of key glycine residues, are necessary for optimal activation of T cells. Based on Vbeta-skewing analysis of human T cells activated with SpeI and structural models, we propose that the alpha3-beta8 loop is positioned to form productive intermolecular contacts with the TCR beta-chain, likely in framework region 3, and that these contacts are required for optimal TCR recognition by SpeI, and likely all other group V SAgs.

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Publishing Authors By Initials

JN Brouillard,S ,AK Varma,I Gryski,CA Herfst,AK Rahman,DY Leung,PM Schlievert,J Madrenas,EJ Sundberg,JK McCormick,

For similar biological factors: antigens: superantigens research abstracts see: biological factors: antigens: superantigens research

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Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Journal Published:

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

Journal: Journal of molecular biology

VOLUME: 367

Page Numbers: 925-34

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 12

MONTH: 01

YEAR: 2007

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Keywords Mesh Terms:

KEYWORDS: Superantigens

MESH TERMS: physiology

Chemical & Substance for Abstract: Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens. Information

Substance Name: erythrogenic toxin

Registry Number: 0

Grant and Affiliation Information for Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by group V superantigens.

AFFILIATION: Department of Microbiology and Immunology, The University of Western Ontario, London, ON, Canada N6A 5B8.

Country: England

AGENCY: United States NIAID

GRANT: AI55882

ACRONYM: AI

MEDLINETA: J Mol Biol

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