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@ARTICLE{Azoury:167227,
      author       = {M. E. Azoury and M. Tarayrah and G. Afonso and A. Pais and
                      M. L. Colli and C. Maillard and C. Lavaud and L.
                      Alexandre-Heymann and S. Gonzalez-Duque and Y. Verdier and
                      J. Vinh and S. Pinto$^*$ and S. Buus and D. Dubois-Laforgue
                      and E. Larger and J.-P. Beressi and G. Bruno and D. L.
                      Eizirik and S. You and R. Mallone},
      title        = {{P}eptides {D}erived {F}rom {I}nsulin {G}ranule {P}roteins
                      {A}re {T}argeted by {CD}8+ {T} {C}ells {A}cross {MHC}
                      {C}lass {I} {R}estrictions in {H}umans and {NOD} {M}ice.},
      journal      = {Diabetes},
      volume       = {69},
      number       = {12},
      issn         = {1939-327X},
      address      = {Alexandria, Va},
      publisher    = {Assoc.},
      reportid     = {DKFZ-2021-00212},
      pages        = {2678 - 2690},
      year         = {2020},
      note         = {Division of Developmental Immunology},
      abstract     = {The antigenic peptides processed by β-cells and presented
                      through surface HLA class I molecules are poorly
                      characterized. Each HLA variant (e.g., the most common being
                      HLA-A2 and HLA-A3) carries some peptide-binding specificity.
                      Hence, features that, despite these specificities, remain
                      shared across variants may reveal factors favoring β-cell
                      immunogenicity. Building on our previous description of the
                      HLA-A2/A3 peptidome of β-cells, we analyzed the
                      HLA-A3-restricted peptides targeted by circulating CD8+ T
                      cells. Several peptides were recognized by CD8+ T cells
                      within a narrow frequency (1-50/106), which was similar in
                      donors with and without type 1 diabetes and harbored
                      variable effector/memory fractions. These epitopes could be
                      classified as conventional peptides or neoepitopes,
                      generated either via peptide cis-splicing or mRNA splicing
                      (e.g., secretogranin-5 [SCG5]-009). As reported for
                      HLA-A2-restricted peptides, several epitopes originated from
                      β-cell granule proteins (e.g., SCG3, SCG5, and
                      urocortin-3). Similarly, H-2Kd-restricted CD8+ T cells
                      recognizing the murine orthologs of SCG5, urocortin-3, and
                      proconvertase-2 infiltrated the islets of NOD mice and
                      transferred diabetes into NOD/scid recipients. The finding
                      of granule proteins targeted in both humans and NOD mice
                      supports their disease relevance and identifies the insulin
                      granule as a rich source of epitopes, possibly reflecting
                      its impaired processing in type 1 diabetes.},
      keywords     = {Adult / Alternative Splicing / Animals / CD8-Positive
                      T-Lymphocytes / Case-Control Studies / Chromogranins:
                      genetics / Chromogranins: metabolism / Computer Simulation /
                      Data Mining / Diabetes Mellitus, Type 1: genetics / Diabetes
                      Mellitus, Type 1: metabolism / Epitopes / Female / Gene
                      Expression Regulation / HLA-A3 Antigen / Humans / Insulin /
                      Male / Mice / Mice, Inbred NOD / Neuroendocrine Secretory
                      Protein 7B2: genetics / Neuroendocrine Secretory Protein
                      7B2: metabolism / Protein Binding / RNA, Messenger: genetics
                      / Urocortins: genetics / Urocortins: metabolism / Young
                      Adult / Chromogranins (NLM Chemicals) / Epitopes (NLM
                      Chemicals) / HLA-A3 Antigen (NLM Chemicals) / Insulin (NLM
                      Chemicals) / Neuroendocrine Secretory Protein 7B2 (NLM
                      Chemicals) / RNA, Messenger (NLM Chemicals) / Ucn3 protein,
                      mouse (NLM Chemicals) / Urocortins (NLM Chemicals)},
      cin          = {D090 ; D090},
      ddc          = {610},
      cid          = {I:(DE-He78)D090-20160331},
      pnm          = {314 - Tumor immunology (POF3-314)},
      pid          = {G:(DE-HGF)POF3-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32928873},
      doi          = {10.2337/db20-0013},
      url          = {https://inrepo02.dkfz.de/record/167227},
}