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Biophysical and structural characterization of antigen recognition by the alloreactive HCV1406 TCR
Author(s) -
Wang Yuan M,
Baker Brian M.
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.601.6
Subject(s) - t cell receptor , immunology , major histocompatibility complex , human leukocyte antigen , epitope , biology , t cell , antigen , mhc restriction , hepatitis c virus , computational biology , virology , immune system , virus
Alloreactivity occurs when organs are transplanted across MHC barriers, and results from T cell recognition of “foreign” MHC proteins. Although alloreactivity has been studied for decades, the underlying molecular mechanisms remain elusive. Previous research identified the capacity to generate allospecific T cell responses via liver transplantation across MHC barriers: the HCV1406 TCR, specific for the NS31406‐1415 epitope from the Hepatitis C virus (HCV) presented by HLA‐A2, expanded when an HLA‐A2−/− host received an HCV‐infected HLA‐A2+ liver. This system provides a model for understanding both general features of TCR‐pMHC specificity as well as the underpinnings of alloreactivity, and the role of the peptide vs MHC polymorphisms in driving alloreactivity. Here, a combination of protein biophysics and structural biology are used to investigate the HCV1406 TCR specificity and allogeneic TCR‐pMHC engagement.