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Structural basis of a unique interferon-? signaling axis mediated via the receptor IFNAR1

de Weerd, N., Vivian, J., Nguyen, T., Mangan, N., Gould, J., Braniff, S., Zaker-Tabrizi, L., Fung, K., Forster, S., Beddoe, T., Reid, H., Rossjohn, Jamie and Hertzog, P. 2013. Structural basis of a unique interferon-? signaling axis mediated via the receptor IFNAR1. Nature Immunology 14 (9) , pp. 901-907. 10.1038/ni.2667

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Abstract

Human T cell antigen receptors (TCRs) pair in millions of combinations to create complex and unique T cell repertoires for each person. Through the use of tetramers to analyze TCRs reactive to the antigen-presenting molecule CD1b, we detected T cells with highly stereotyped TCR α-chains present among genetically unrelated patients with tuberculosis. The germline-encoded, mycolyl lipid-reactive (GEM) TCRs had an α-chain bearing the variable (V) region TRAV1-2 rearranged to the joining (J) region TRAJ9 with few nontemplated (N)-region additions. Analysis of TCRs by high-throughput sequencing, binding and crystallography showed linkage of TCRα sequence motifs to high-affinity recognition of antigen. Thus, the CD1-reactive TCR repertoire is composed of at least two compartments: high-affinity GEM TCRs, and more-diverse TCRs with low affinity for CD1b-lipid complexes. We found high interdonor conservation of TCRs that probably resulted from selection by a nonpolymorphic antigen-presenting molecule and an immunodominant antigen.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Systems Immunity Research Institute (SIURI)
Subjects: R Medicine > R Medicine (General)
R Medicine > RZ Other systems of medicine
Uncontrolled Keywords: Animals; Disease Models, Animal; Female; Interferon-beta; Lipopolysaccharides; Mice; Mice, Knockout; Models, Molecular; Multiprotein Complexes; Protein Binding; Protein Conformation; Protein Stability; Receptor, Interferon alpha-beta; Shock, Septic; Signal Transduction
Publisher: Nature Publishing Group
ISSN: 1529-2908
Date of Acceptance: 19 June 2013
Last Modified: 04 Jun 2017 08:20
URI: http://orca.cf.ac.uk/id/eprint/75928

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