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dc.contributor.author
McCormick, John K.
dc.contributor.author
Tripp, Timothy J.
dc.contributor.author
Llera, Andrea Sabina
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dc.contributor.author
Sundberg, Eric J.
dc.contributor.author
Dinges, Martin M.
dc.contributor.author
Mariuzza, Roy A.
dc.contributor.author
Schlievert, Patrick M.
dc.date.available
2018-04-26T17:41:48Z
dc.date.issued
2003-07
dc.identifier.citation
McCormick, John K.; Tripp, Timothy J.; Llera, Andrea Sabina; Sundberg, Eric J.; Dinges, Martin M.; et al.; Functional Analysis of the TCR Binding Domain of Toxic Shock Syndrome Toxin-1 Predicts Further Diversity in MHC Class II/Superantigen/TCR Ternary Complexes; American Association of Immunologists; Journal of Immunology; 171; 3; 7-2003; 1385-1392
dc.identifier.issn
0022-1767
dc.identifier.uri
http://hdl.handle.net/11336/43551
dc.description.abstract
Superantigens (SAGs) aberrantly alter immune system function through simultaneous interaction with lateral surfaces of MHC class II molecules on APCs and with particular variable regions of the TCR beta-chain (Vbeta). To further define the interface between the bacterial SAG toxic shock syndrome toxin-1 (TSST-1) and the TCR, we performed alanine scanning mutagenesis within the putative TCR binding region of TSST-1 along the central alpha helix adjacent to the N-terminal alpha helix and the beta7-beta9 loop as well as with two universally conserved SAG residues (Leu(137) and Tyr(144) in TSST-1). Mutants were analyzed for multiple functional activities, and various residues appeared to play minor or insignificant roles in the TCR interaction. The locations of six residues (Gly(16), Trp(116), Glu(132), His(135), Gln(136), and Gln(139)), each individually critical for functional activity as well as direct interaction with the human TCR Vbeta2.1-chain, indicate that the interface occurs in a novel region of the SAG molecule. Based on these data, a model of the MHC/TSST-1/TCR ternary complex predicts similarities seen with other characterized SAGs, although the CDR3 loop of Vbeta2.1 is probably involved in direct SAG-TCR molecular interactions, possibly contributing to the TCR Vbeta specificity of TSST-1.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Association of Immunologists
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Tcr Receptor
dc.subject
Superantigens
dc.subject
Major Histocompatibility Complex
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Functional Analysis of the TCR Binding Domain of Toxic Shock Syndrome Toxin-1 Predicts Further Diversity in MHC Class II/Superantigen/TCR Ternary Complexes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-04-10T13:39:07Z
dc.identifier.eissn
1550-6606
dc.journal.volume
171
dc.journal.number
3
dc.journal.pagination
1385-1392
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda
dc.description.fil
Fil: McCormick, John K.. University of Minnesota; Estados Unidos
dc.description.fil
Fil: Tripp, Timothy J.. University of Minnesota; Estados Unidos
dc.description.fil
Fil: Llera, Andrea Sabina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. University of Maryland; Estados Unidos
dc.description.fil
Fil: Sundberg, Eric J.. University of Maryland; Estados Unidos
dc.description.fil
Fil: Dinges, Martin M.. University of Minnesota; Estados Unidos
dc.description.fil
Fil: Mariuzza, Roy A.. University of Maryland; Estados Unidos
dc.description.fil
Fil: Schlievert, Patrick M.. University of Minnesota; Estados Unidos
dc.journal.title
Journal of Immunology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jimmunol.org/content/171/3/1385.long
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.4049/jimmunol.171.3.1385
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