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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2008-2-15
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pubmed:databankReference |
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pubmed:abstractText |
Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A*0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1074-7613
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
171-82
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:18275829-Amino Acid Motifs,
pubmed-meshheading:18275829-Animals,
pubmed-meshheading:18275829-Crystallography, X-Ray,
pubmed-meshheading:18275829-HLA-A Antigens,
pubmed-meshheading:18275829-HLA-A2 Antigen,
pubmed-meshheading:18275829-Humans,
pubmed-meshheading:18275829-Immunodominant Epitopes,
pubmed-meshheading:18275829-Influenza A virus,
pubmed-meshheading:18275829-Models, Molecular,
pubmed-meshheading:18275829-Mutant Proteins,
pubmed-meshheading:18275829-Mutation,
pubmed-meshheading:18275829-Protein Structure, Tertiary,
pubmed-meshheading:18275829-Protein Subunits,
pubmed-meshheading:18275829-Receptors, Antigen, T-Cell, alpha-beta,
pubmed-meshheading:18275829-Structure-Activity Relationship,
pubmed-meshheading:18275829-T-Lymphocytes,
pubmed-meshheading:18275829-Viral Matrix Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain.
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pubmed:affiliation |
MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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