| DOI | Trouver le DOI : https://doi.org/10.1128/JB.00861-09 |
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| Auteur | Rechercher : Twine, Susan M.1; Rechercher : Reid, Christopher W.1; Rechercher : Aubry, Annie1; Rechercher : McMullin, David R.1; Rechercher : Fulton, Kelly M.1; Rechercher : Austin, John; Rechercher : Logan, Susan M.1 |
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| Affiliation | - Conseil national de recherches du Canada. Institut des sciences biologiques du CNRC
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| Format | Texte, Article |
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| Résumé | In this study intact flagellin proteins were purified from strains of C. difficile and analyzed using QTOF and linear ion trap mass spectrometers. Top-down studies showed the flagellin proteins to have a mass greater than that predicted from the corresponding gene sequence. These top down studies revealed marker ions characteristic of glycan modifications. Additionally, diversity in the observed masses of glycan modifications was seen between strains. Electron transfer dissociation mass spectrometry was used to demonstrate that the glycan was attached to the flagellin protein backbone in O-linkage via a HexNAc residue in all strains examined. Bioinformatics analysis of C. difficile genomes revealed diversity with respect to glycan biosythetic gene content within the flagellar biosynthetic locus likely reflected by the observed flagellar glycan diversity. Insertional inactivation of a glycosyltransfease gene (CD0240), which is present in all sequenced genomes, in strain C. difficile 630 resulted in an inability to produce flagella filaments at the cell surface and only minor amounts of unmodified flagellin protein. |
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| Date de publication | 2009-09-11 |
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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 | 15461141 |
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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 | 1bddb470-b4b0-4743-a0ad-2af804f60024 |
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| Enregistrement créé | 2010-08-16 |
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| Enregistrement modifié | 2020-04-16 |
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