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      CD1a-autoreactive T cells recognize natural skin oils that function as headless antigens.

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          Abstract

          T cells autoreactive to the antigen-presenting molecule CD1a are common in human blood and skin, but the search for natural autoantigens has been confounded by background T cell responses to CD1 proteins and self lipids. After capturing CD1a-lipid complexes, we gently eluted ligands while preserving non-ligand-bound CD1a for testing lipids from tissues. CD1a released hundreds of ligands of two types. Inhibitory ligands were ubiquitous membrane lipids with polar head groups, whereas stimulatory compounds were apolar oils. We identified squalene and wax esters, which naturally accumulate in epidermis and sebum, as autoantigens presented by CD1a. The activation of T cells by skin oils suggested that headless mini-antigens nest within CD1a and displace non-antigenic resident lipids with large head groups. Oily autoantigens naturally coat the surface of the skin; thus, this points to a previously unknown mechanism of barrier immunity.

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          Most cited references54

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          Phenotypic analysis of antigen-specific T lymphocytes.

          Identification and characterization of antigen-specific T lymphocytes during the course of an immune response is tedious and indirect. To address this problem, the peptide-major histocompatability complex (MHC) ligand for a given population of T cells was multimerized to make soluble peptide-MHC tetramers. Tetramers of human lymphocyte antigen A2 that were complexed with two different human immunodeficiency virus (HIV)-derived peptides or with a peptide derived from influenza A matrix protein bound to peptide-specific cytotoxic T cells in vitro and to T cells from the blood of HIV-infected individuals. In general, tetramer binding correlated well with cytotoxicity assays. This approach should be useful in the analysis of T cells specific for infectious agents, tumors, and autoantigens.
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            Structure of the complex between human T-cell receptor, viral peptide and HLA-A2.

            Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histocompatibility complex (MHC) molecule occurs through variable loops in the TCR structure which bury almost all the available peptide and a much larger area of the MHC molecule. The TCR fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and class II MHC molecules, providing evidence that the nature of binding is general. A broadly applicable binding mode has implications for the mechanism of repertoire selection and the magnitude of alloreactions.
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              • Record: found
              • Abstract: not found
              • Article: not found

              Phenotypic Analysis of Antigen-Specific T Lymphocytes

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                Author and article information

                Journal
                Nat. Immunol.
                Nature immunology
                Springer Nature
                1529-2916
                1529-2908
                Feb 2014
                : 15
                : 2
                Affiliations
                [1 ] 1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. [2] [3].
                [2 ] 1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. [2].
                [3 ] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
                [4 ] Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Australia.
                [5 ] 1] Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
                [6 ] Infectious Disease Department, Boston University, Boston, Massachusetts, USA.
                [7 ] Department of Gastrointestinal and General Surgery, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
                [8 ] Emory Vaccine Center, Atlanta, Georgia, USA.
                [9 ] 1] Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Australia. [2] Institute of Infection and Immunity, Cardiff University, School of Medicine, Heath Park, Cardiff, UK.
                Article
                ni.2790 NIHMS541955
                10.1038/ni.2790
                3932764
                24362891
                9ca855ff-901e-4974-8933-6e59bfd84b90
                History

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