| Téléchargement | - Voir la version finale : The type B flagellin of hypervirulent clostridium difficile is modified with novel sulphonated Peptidylamido-glycans (PDF, 1.6 Mio)
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| DOI | Trouver le DOI : https://doi.org/10.1074/jbc.M116.749481 |
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| Auteur | Rechercher : Bouché, Laura; Rechercher : Panico, Maria; Rechercher : Hitchen, Paul; Rechercher : Binet, Daniel; Rechercher : Sastre, Federico; Rechercher : Faulds-pain, Alexandra; Rechercher : Valiente, Esmeralda; Rechercher : Vinogradov, Evgeny1; Rechercher : Aubry, Annie1; Rechercher : Fulton, Kelly1; Rechercher : Twine, Susan1; Rechercher : Logan, Susan m1; Rechercher : Wren, Brendan w; Rechercher : Dell, Anne; Rechercher : Morris, Howard r |
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| Affiliation | - Conseil national de recherches Canada. Thérapeutique en santé humaine
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| Format | Texte, Article |
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| Sujet | bacteria; glycosylation; gram-positive bacteria; mass spectrometry (MS); nuclear magnetic resonance (NMR); Clostridium difficile; flagellin; modification; sulphonated |
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| Résumé | Glycosylation of flagellins is a well recognized property of many bacterial species. In this study we describe the structural characterization of novel flagellar glycans from a number of hypervirulent strains of C. difficile. We used mass spectrometry (nano LC- MS and MS/MS analysis) to identify a number of putative glycopeptides which carried a variety of glycoform substitutions each of which was linked through an initial HexNAc residue to Ser or Thr. Detailed analysis of a LLDGSSTEIR glycopeptide released by tryptic digestion, which carried two variant structures, revealed that the glycopeptide contained, in addition to carbohydrate moieties, a novel structural entity. A variety of Electrospray-MS strategies using Q-TOF technology were used to define this entity, including positive- and negative-ion collisionally activated decomposition (CAD) MS/MS which produced unique fragmentation patterns, and high resolution accurate mass measurement to allow derivation of atomic compositions, leading to the suggestion of a Taurine-containing peptidylamido-glycan structure. Finally NMR analysis of flagellin glycopeptides provided complementary information. The glycan portion of the modification was assigned as α-Fuc3N-(1→3)-α-Rha-(1→2)-α-Rha3OMe-(1→3)-β-GlcNAc-(1→)Ser and the novel capping moiety was shown to be comprised of Taurine, Alanine, and Glycine. This is the first report of a novel O-linked sulphonated peptidylamido-glycan moiety decorating a flagellin protein. |
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| Date de publication | 2016-10 |
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| Maison d’édition | American Society for Biochemistry and Molecular Biology |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Numéro NPARC | 23000836 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 5ac353b2-654a-48eb-9fc4-c05458f7459d |
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| Enregistrement créé | 2016-10-17 |
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| Enregistrement modifié | 2020-06-02 |
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