Source:http://linkedlifedata.com/resource/pubmed/id/19167249
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2009-2-25
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pubmed:databankReference | |
pubmed:abstractText |
During selection of the T cell repertoire, the immune system navigates the subtle distinction between self-restriction and self-tolerance, yet how this is achieved is unclear. Here we describe how self-tolerance toward a trans-HLA (human leukocyte antigen) allotype shapes T cell receptor (TCR) recognition of an Epstein-Barr virus (EBV) determinant (FLRGRAYGL). The recognition of HLA-B8-FLRGRAYGL by two archetypal TCRs was compared. One was a publicly selected TCR, LC13, that is alloreactive with HLA-B44; the other, CF34, lacks HLA-B44 reactivity because it arises when HLA-B44 is coinherited in trans with HLA-B8. Whereas the alloreactive LC13 TCR docked at the C terminus of HLA-B8-FLRGRAYGL, the CF34 TCR docked at the N terminus of HLA-B8-FLRGRAYGL, which coincided with a polymorphic region between HLA-B8 and HLA-B44. The markedly contrasting footprints of the LC13 and CF34 TCRs provided a portrait of how self-tolerance shapes the specificity of TCRs selected into the immune repertoire.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1097-4180
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pubmed:author |
pubmed-author:BellMelissa JMJ,
pubmed-author:BrooksAndrew GAG,
pubmed-author:BurrowsScott RSR,
pubmed-author:ClementsCraig SCS,
pubmed-author:GrasStephanieS,
pubmed-author:Kjer-NielsenLarsL,
pubmed-author:LiuYu ChihYC,
pubmed-author:McCluskeyJamesJ,
pubmed-author:PurcellAnthony WAW,
pubmed-author:RossjohnJamieJ,
pubmed-author:SullivanLucy CLC
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-203
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pubmed:dateRevised |
2009-6-8
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pubmed:meshHeading |
pubmed-meshheading:19167249-Amino Acid Sequence,
pubmed-meshheading:19167249-Antigens, Viral,
pubmed-meshheading:19167249-Crystallography, X-Ray,
pubmed-meshheading:19167249-HLA-B8 Antigen,
pubmed-meshheading:19167249-Herpesvirus 4, Human,
pubmed-meshheading:19167249-Humans,
pubmed-meshheading:19167249-Models, Molecular,
pubmed-meshheading:19167249-Peptides,
pubmed-meshheading:19167249-Protein Structure, Quaternary,
pubmed-meshheading:19167249-Receptors, Antigen, T-Cell,
pubmed-meshheading:19167249-Self Tolerance,
pubmed-meshheading:19167249-Structural Homology, Protein,
pubmed-meshheading:19167249-Surface Plasmon Resonance
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pubmed:year |
2009
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pubmed:articleTitle |
The shaping of T cell receptor recognition by self-tolerance.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, The Protein Crystallography Unit, Monash University, Clayton, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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