| DOI | Resolve DOI: https://doi.org/10.1128/JB.00861-09 |
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| Author | Search for: Twine, Susan M.1; Search for: Reid, Christopher W.1; Search for: Aubry, Annie1; Search for: McMullin, David R.1; Search for: Fulton, Kelly M.1; Search for: Austin, John; Search for: Logan, Susan M.1 |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Abstract | 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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| Publication date | 2009-09-11 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 15461141 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 1bddb470-b4b0-4743-a0ad-2af804f60024 |
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| Record created | 2010-08-16 |
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| Record modified | 2020-04-16 |
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