Cell wall peptidolipids of Mycobacterium avium: from genetic prediction to exact structure of a nonribosomal peptide
Autor: | Frédéric Bonhomme, Judith R. Stabel, John P. Bannantine, Anne Lemassu, Franck Biet, Thierry Cochard, Maxime Branger, Gilles Etienne, Sylvie Bay, Françoise Laval, Darrell O. Bayles, Christelle Ganneau, Mamadou Daffé |
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Přispěvatelé: | USDA Agricultural Research Service [Maricopa, AZ] (USDA), United States Department of Agriculture - USDA (USA), Institut de pharmacologie et de biologie structurale (IPBS), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Chimie des Biomolécules, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Infectiologie Santé Publique (ISP-311), Université de Tours-Institut National de la Recherche Agronomique (INRA), F.B., M.B. and T.C. were supported by the Institut National de la Recherche Agronomique (INRA) and the Cluster de recherche en infectiologie de la région Centre. NMR experiments were performed on the PICT-Genotoul platform of Toulouse and funded by CNRS, Université de Toulouse-UPS, Ibisa, European structural funds and the Midi-Pyrénées region. This study was financially supported by the EMIDA-EraNet MYCOBACTDIAGNOSIS project and the USDA-Agricultural Research Service., United States Department of Agriculture (USDA), Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Chimie des Biomolécules - Chemistry of Biomolecules, Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Infectiologie et Santé Publique (UMR ISP), Institut National de la Recherche Agronomique (INRA)-Université de Tours (UT), Institut National de la Recherche Agronomique (INRA)-Université de Tours, Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0301 basic medicine
Sequence analysis 030106 microbiology peptide synthase non ribosomal prédiction génétique Paratuberculosis Tripeptide Microbiology Cell wall Membrane Lipids 03 medical and health sciences mycobacterium avium Nonribosomal peptide medicine Amino Acid Sequence caractérisation génétique Peptide Synthases Molecular Biology chemistry.chemical_classification biology Fatty acid Sequence Analysis DNA biology.organism_classification medicine.disease Amino acid 030104 developmental biology chemistry Biochemistry lipopeptide Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization cell wall [SDV.SPEE]Life Sciences [q-bio]/Santé publique et épidémiologie Peptides paroi cellulaire Mycobacterium |
Zdroj: | Molecular Microbiology Molecular Microbiology, Wiley, 2017, 105 (4), pp.525-539. ⟨10.1111/mmi.13717⟩ Molecular Microbiology, 2017, 105 (4), pp.525-539. ⟨10.1111/mmi.13717⟩ |
ISSN: | 0950-382X 1365-2958 |
Popis: | Summary Mycobacteria have a complex cell wall structure that includes many lipids; however, even within a single subspecies of Mycobacterium avium these lipids can differ. Total lipids from an M. avium subsp. paratuberculosis (Map) ovine strain (S-type) contained no identifiable glycopeptidolipids or lipopentapeptide, yet both lipids are present in other M. avium subspecies. We determined the genetic and phenotypic basis for this difference using sequence analysis as well as biochemical and physico-chemical approaches. This strategy showed that a nonribosomal peptide synthase, encoded by mps1, contains three amino acid specifying modules in ovine strains, compared to five modules in bovine strains (C-type). Sequence analysis predicted these modules would produce the tripeptide Phe-N-Methyl-Val-Ala with a lipid moiety, termed lipotripeptide (L3P). Comprehensive physico-chemical analysis of Map S397 extracts confirmed the structural formula of the native L3P as D-Phe-N-Methyl-L-Val-L-Ala-OMe attached in N-ter to a 20-carbon fatty acid chain. These data demonstrate that S-type strains, which are more adapted in sheep, produce a unique lipid. There is a dose-dependent effect observed for L3P on upregulation of CD25+ CD8 T cells from infected cows, while L5P effects were static. In contrast, L5P demonstrated a significantly stronger induction of CD25+ B cells from infected animals compared to L3P. This article is protected by copyright. All rights reserved. |
Databáze: | OpenAIRE |
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