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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Altman, John D. Ly, Dalam Roy, Sobhan Moody, D. Branch Li, Nan-sheng Piccirilli, Joseph A. Adams, Erin J. |
| Description | Author Affiliation: Roy S ( Departments of Biochemistry and Molecular Biology and.); Ly D ( Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, MA 02115); Li NS ( Departments of Biochemistry and Molecular Biology and.); Altman JD ( Emory Vaccine Center at Yerkes, Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30329.); Piccirilli JA ( Departments of Biochemistry and Molecular Biology and Chemistry and.); Moody DB ( Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Boston, MA 02115); Adams EJ ( Departments of Biochemistry and Molecular Biology and Committee on Immunology, University of Chicago, Chicago, IL 60637); |
| Abstract | CD1c is a member of the group 1 CD1 family of proteins that are specialized for lipid antigen presentation. Despite high cell surface expression of CD1c on key antigen-presenting cells and the discovery of its mycobacterial lipid antigen presentation capability, the molecular basis of CD1c recognition by T cells is unknown. Here we present a comprehensive functional and molecular analysis of ß T-cell receptor (TCR) recognition of CD1c presenting mycobacterial phosphomycoketide antigens. Our structure of CD1c with the mycobacterial phosphomycoketide (PM) shows similarities to that of CD1c-mannosyl-ß1-phosphomycoketide in that the A' pocket accommodates the mycoketide alkyl chain; however, the phosphate head-group of PM is shifted â ¼6 Å in relation to that of mannosyl-ß1-PM. We also demonstrate a bona fide interaction between six human TCRs and CD1c-mycoketide complexes, measuring high to moderate affinities. The crystal structure of the DN6 TCR and mutagenic studies reveal a requirement of five complementarity determining region (CDR) loops for CD1c recognition. Furthermore, mutagenesis of CD1c reveals residues in both the 1 and 2 helices involved in TCR recognition, yet not entirely overlapping among the examined TCRs. Unlike patterns for MHC I, no archetypical binding footprint is predicted to be shared by CD1c-reactive TCRs, even when recognizing the same or similar antigens. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 43 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antigen Presentation Immunology Antigens, Bacterial Antigens, CD1 Lipids Mycobacterium Receptors, Antigen, T-Cell, Alpha-beta Amino Acids Metabolism Chemistry Clone Cells Crystallography, X-Ray Glycosylation Models, Molecular Protein Binding Protein Footprinting Protein Structure, Secondary T-Lymphocytes Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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