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Nature Research, Nature Communications, 1(7), 2016

DOI: 10.1038/ncomms13257

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T cell receptor recognition of CD1b presenting a mycobacterial glycolipid

Journal article published in 2016 by Stephanie Gras, Ildiko Van Rhijn ORCID, Adam Shahine, Tan-Yun Cheng, Mugdha Bhati, Li Lynn Tan ORCID, Hanim Halim, Kathryn D. Tuttle, Laurent Gapin, Jérôme Le Nours ORCID, D. Branch Moody, Jamie Rossjohn
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

AbstractCD1 proteins present microbial lipids to T cells. Germline-encoded mycolyl lipid-reactive (GEM) T cells with conserved αβ T cell receptors (TCRs) recognize CD1b presenting mycobacterial mycolates. As the molecular basis underpinning TCR recognition of CD1b remains unknown, here we determine the structure of a GEM TCR bound to CD1b presenting glucose-6-O-monomycolate (GMM). The GEM TCR docks centrally above CD1b, whereby the conserved TCR α-chain extensively contacts CD1b and GMM. Through mutagenesis and study of T cells from tuberculosis patients, we identify a consensus CD1b footprint of TCRs present among GEM T cells. Using both the TCR α- and β-chains as tweezers to surround and grip the glucose moiety of GMM, GEM TCRs create a highly specific mechanism for recognizing this mycobacterial glycolipid.