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

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          Abstract

          CD1a autoreactive T cells 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 unliganded CD1a for testing lipids from tissues. CD1a released hundreds of ligands of two types. Inhibitory ligands were ubiquitous membrane lipids with polar headgroups, whereas stimulatory compounds were apolar oils. CD1a autoantigens naturally accumulate in epidermis and sebum, where they were identified as squalene and skin waxes. T cell activation by skin oils suggests that headless mini-antigens nest within CD1a and displace non-antigenic resident lipids with large head groups. Oily autoantigens naturally coat the skin's surface, pointing to a new mechanism of barrier immunity.

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          Most cited references 54

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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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              Phenotypic Analysis of Antigen-Specific T Lymphocytes

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                Author and article information

                Journal
                100941354
                21750
                Nat Immunol
                Nat. Immunol.
                Nature immunology
                1529-2908
                1529-2916
                28 January 2014
                22 December 2013
                February 2014
                01 August 2014
                : 15
                : 2
                : 177-185
                Affiliations
                [1 ]Division of Rheumatology, Immunology and Allergy
                [2 ]Department of Gastrointestinal and General Surgery, Brigham and Women’s Hospital, Harvard Medical School
                [3 ]Boston University, Boston MA
                [4 ]Emory Vaccine Center, Atlanta GA
                [5 ]Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, Australia
                [6 ]Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands
                [7 ]Institute of Infection and Immunity, Cardiff University, School of Medicine, Heath Park, Cardiff CF14 4XN, UK
                Author notes
                [9 ]Correspondence should be addressed to D.B.M ( bmoody@ 123456partners.org ) or AdJ ( ad2952@ 123456columbia.edu )
                [8]

                These authors contributed equally to this work

                Current affiliation AdJ: Department of Dermatology, Columbia University Medical Center, New York NY

                Article
                NIHMS541955
                10.1038/ni.2790
                3932764
                24362891

                Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms

                Funding
                Funded by: National Institute of Arthritis and Musculoskeletal and Skin Diseases : NIAMS
                Award ID: R01 AR048632 || AR
                Funded by: National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID
                Award ID: R01 AI049313 || AI
                Funded by: National Institute of Allergy and Infectious Diseases Extramural Activities : NIAID
                Award ID: K08 AI089858 || AI
                Categories
                Article

                Immunology

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