Allelic polymorphism in the T cell receptor and its impact on immune responses

Gras, Stephanie, Chen, Zhenjun, Miles, John J., Liu, Yu Chih, Bell, Melissa J., Sullivan, Lucy C., Kjer-Nielsen, Lars, Brennan, Rebekah M., Burrows, Jacqueline M., Neller, Michelle A., Khanna, Rajiv, Purcell, Anthony W., Brooks, Andrew G., McCluskey, James, Rossjohn, Jamie and Burrows, Scott R. (2010) Allelic polymorphism in the T cell receptor and its impact on immune responses. Journal of Experimental Medicine, 207 7: 1555-1567. doi:10.1084/jem.20100603

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Author Gras, Stephanie
Chen, Zhenjun
Miles, John J.
Liu, Yu Chih
Bell, Melissa J.
Sullivan, Lucy C.
Kjer-Nielsen, Lars
Brennan, Rebekah M.
Burrows, Jacqueline M.
Neller, Michelle A.
Khanna, Rajiv
Purcell, Anthony W.
Brooks, Andrew G.
McCluskey, James
Rossjohn, Jamie
Burrows, Scott R.
Title Allelic polymorphism in the T cell receptor and its impact on immune responses
Journal name Journal of Experimental Medicine   Check publisher's open access policy
ISSN 0022-1007
Publication date 2010-07
Sub-type Article (original research)
DOI 10.1084/jem.20100603
Open Access Status File (Publisher version)
Volume 207
Issue 7
Start page 1555
End page 1567
Total pages 9
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Collection year 2011
Language eng
Formatted abstract
In comparison to human leukocyte antigen (HLA) polymorphism, the impact of allelic sequence variation within T cell receptor (TCR) loci is much less understood. Particular TCR loci have been associated with autoimmunity, but the molecular basis for this phenomenon is undefined. We examined the T cell response to an HLA-B*3501–restricted epitope (HPVGEADYFEY) from Epstein-Barr virus (EBV), which is frequently dominated by a TRBV9*01+ public TCR (TK3). However, the common allelic variant TRBV9*02, which differs by a single amino acid near the CDR2β loop (Gln55→His55), was never used in this response. The structure of the TK3 TCR, its allelic variant, and a nonnaturally occurring mutant (Gln55→Ala55) in complex with HLA-B*3501HPVGEADYFEY revealed that the Gln55→His55 polymorphism affected the charge complementarity at the TCR–peptide-MHC interface, resulting in reduced functional recognition of the cognate and naturally occurring variants of this EBV peptide. Thus, polymorphism in the TCR loci may contribute toward variability in immune responses and the outcome of infection. © 2010 Gras et al.
Keyword Epstein-barr-virus
Major histocompatibility complex
Allogeneic restriction
Amino acid substitution
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Medicine Publications
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Citation counts: TR Web of Science Citation Count  Cited 40 times in Thomson Reuters Web of Science Article | Citations
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Created: Sun, 18 Jul 2010, 00:04:45 EST