T cell receptor recognition of CD1b presenting a mycobacterial glycolipid

Stephanie Gras, Ildiko Van Rhijn, Adam Shahine, Tan-Yun Cheng, Mugdha Bhati, Li Lynn Tan, Hanim Halim, Kathryn D. Tuttle, Laurent Gapin, Jérôme Le Nours, D. Branch Moody () and Jamie Rossjohn ()
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Stephanie Gras: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
Ildiko Van Rhijn: Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School
Adam Shahine: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
Tan-Yun Cheng: Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School
Mugdha Bhati: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
Li Lynn Tan: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
Hanim Halim: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
Kathryn D. Tuttle: University of Colorado Anschutz Medical Campus and National Jewish Health
Laurent Gapin: University of Colorado Anschutz Medical Campus and National Jewish Health
Jérôme Le Nours: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University
D. Branch Moody: Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School
Jamie Rossjohn: Infection and Immunity Program, Biomedicine Discovery Institute, Monash University

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract CD1 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.

Date: 2016
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DOI: 10.1038/ncomms13257

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