The fidelity, occasional promiscuity, and versatility of T cell receptor recognition.
Although there are multiple structures showing how alphabeta T cell receptors (TCRs) specifically recognize antigenic peptides bound to the major histocompatibility complex (MHC) molecules (pMHC-I and pMHC-II), we have little data on how TCRs interact with lipid-based antigens presented by members of the CD1 family. Here, we review recent findings in the field of TCR recognition, including TCR-pMHC complexes and the structure of a TCR in complex with CD1d-glycolipid. Collectively, these studies have revealed the versatility of the TCR in recognizing the distinct yet evolutionarily related proteinaceous and lipid-presenting molecules of the immune system.
Godfrey
Dale I
DI
Department of Microbiology and Immunology, University of Melbourne, Parkville, Victoria 3010, Australia. godfrey@unimelb.edu.au
Rossjohn
Jamie
J
McCluskey
James
J
D000818:Animals; D017951:Antigen Presentation / Q000276:immunology*; D018949:Antigens, CD1 / Q000276:immunology; D055610:Antigens, CD1d; D006017:Glycolipids / Q000276:immunology; D006801:Humans; D008213:Lymphocyte Activation / Q000276:immunology*; D008285:Major Histocompatibility Complex / Q000276:immunology; D011948:Receptors, Antigen, T-Cell / Q000276:immunology* / Q000378:metabolism; D013601:T-Lymphocytes / Q000276:immunology* / Q000378:metabolism
D018949:Antigens, CD1; D055610:Antigens, CD1d; C526877:CD1D protein, human; D006017:Glycolipids; D011948:Receptors, Antigen, T-Cell