Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes

Eric J Sundberg; Hongmin Li; Andrea S Llera; John K McCormick; José Tormo; Patrick M Schlievert; Klaus Karjalainen; Roy A Mariuzza

doi:10.1016/S0969-2126(02)00759-1

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Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes

Journal article

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Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes

Eric J Sundberg, Hongmin Li, Andrea S Llera, John K McCormick, José Tormo, Patrick M Schlievert, Klaus Karjalainen and Roy A Mariuzza

Structure (London), Vol.10(5), pp.687-699

2002

DOI: 10.1016/S0969-2126(02)00759-1

PMID: 12015151

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Abstract

Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR β chain ligands that reveal distinct TCR binding modes. The SpeC-TCR β chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.

X-ray crystallography

T cell receptor

major histocompatibility complex

T cell activation

superantigen

protein-protein interactions

Details

Title: Subtitle: Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes
Creators: Eric J Sundberg - Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 USA
Hongmin Li - Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 USA
Andrea S Llera - Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 USA
John K McCormick - Department of Microbiology, University of Minnesota Medical School, Minneapolis, MN 55455 USA
José Tormo - Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 USA
Patrick M Schlievert - Department of Microbiology, University of Minnesota Medical School, Minneapolis, MN 55455 USA
Klaus Karjalainen - Basel Institute for Immunology, Grenzacherstrasse 487, CH-4005 Basel, Switzerland
Roy A Mariuzza - Center for Advanced Research in Biotechnology, W.M. Keck Laboratory for Structural Biology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850 USA
Resource Type: Journal article
Publication Details: Structure (London), Vol.10(5), pp.687-699
Publisher: Elsevier Inc
DOI: 10.1016/S0969-2126(02)00759-1
PMID: 12015151
ISSN: 0969-2126
eISSN: 1878-4186
Language: English
Date published: 2002
Academic Unit: Microbiology and Immunology; Internal Medicine
Record Identifier: 9984001111002771

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