Natural T Cell Epitope Containing Methyl Lysines on Mycobacterial Heparin-Binding Hemagglutinin
Autor: | Jérôme Segers, Emmanuelle Petit, Oleg Melnyk, Véronique Corbière, Sophie Lecher, Rémi Desmet, Françoise Mascart, Marc Loyens, Camille Locht |
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Přispěvatelé: | Hôpital Erasme [Bruxelles] (ULB), Faculté de Médecine [Bruxelles] (ULB), Université libre de Bruxelles (ULB)-Université libre de Bruxelles (ULB), Chemical Biology of Flatworms [Lille] (CBF), Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de La Rochelle (ULR), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), La Rochelle Université (ULR) |
Rok vydání: | 2020 |
Předmět: |
medicine.drug_class
T-Lymphocytes [SDV]Life Sciences [q-bio] T cell Mycobacterium smegmatis Immunology Epitopes T-Lymphocyte Hemagglutinin (influenza) Peptide Monoclonal antibody Methylation Epitope Interferon-gamma 03 medical and health sciences 0302 clinical medicine Antigen Lectins Immunologie medicine Humans [CHIM]Chemical Sciences Immunology and Allergy ComputingMilieux_MISCELLANEOUS chemistry.chemical_classification Antigens Bacterial biology Chemistry Lysine Mycobacterium tuberculosis biology.organism_classification Molecular biology Sciences biomédicales 3. Good health [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology medicine.anatomical_structure biology.protein [SDV.IMM]Life Sciences [q-bio]/Immunology Protein Processing Post-Translational 030215 immunology |
Zdroj: | The Journal of immunology, 204 (7 Journal of Immunology Journal of Immunology, Publisher : Baltimore : Williams & Wilkins, c1950-. Latest Publisher : Bethesda, MD : American Association of Immunologists, 2020, 204 (7), pp.1715-1723. ⟨10.4049/jimmunol.1901214⟩ Journal of Immunology, 2020, 204 (7), pp.1715-1723. ⟨10.4049/jimmunol.1901214⟩ |
ISSN: | 1550-6606 0022-1767 |
Popis: | T cell epitopes are mostly nonmodified peptides, although posttranslationally modified peptide epitopes have been described, but they originated from viral or self-proteins. In this study, we provide evidence of a bacterial methylated T cell peptide epitope. The mycobacterial heparin-binding hemagglutinin (HBHA) is a protein Ag with a complex C-terminal methylation pattern and is recognized by T cells from humans latently infected with Mycobacterium tuberculosis. By comparing native HBHAwith recombinant HBHA produced in Mycobacterium smegmatis (rHBHA-Ms), we could link antigenic differences to differences in the methylation profile. Peptide scan analyses led to the discovery of a peptide containing methyl lysines recognized by a mAb that binds to native HBHA ∼100-fold better than to rHBHA-Ms. This peptide was also recognized by T cells from latently infected humans, as evidenced by IFN-g release upon peptide stimulation. The nonmethylated peptide did not induce IFN-g, arguing that the methyl lysines are part of the T cell epitope. SCOPUS: ar.j info:eu-repo/semantics/published |
Databáze: | OpenAIRE |
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