DOI | Resolve DOI: https://doi.org/10.1128/JB.00438-11 |
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Author | Search for: Thomas, R.M.; Search for: Twine, S.M.1; Search for: Fulton, K.M.1; Search for: Tessier, L.1; Search for: Kilmury, S.L.N.1; Search for: Ding, W.1; Search for: Harmer, N.; Search for: Michell, S.L.; Search for: Oyston, P.C.F.; Search for: Titbal, R.W.; Search for: Prior, J.L. |
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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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Subject | bacterial protein; DsbA protein; hydronium ion; PilA protein; serine; threonine; unclassified drug; amino acid sequence; animal experiment; animal model; bacterial virulence; bacterium mutant; carboxy terminal sequence; female; Francisella tularensis; gene locus; liquid chromatography; mouse; nucleotide sequence; protein glycosylation; protein modification; protein structure; subcutaneous fat disorder; tandem mass spectrometry; tularemia; Bacterial Proteins; Electrophoresis, Gel, Two-Dimensional; Female; Francisella tularensis; Glycosylation; Mice; Mice, Inbred BALB C; Multigene Family; Reverse Transcriptase Polymerase Chain Reaction; Tularemia; Virulence; Virulence Factors; Francisella tularensis subsp. tularensis; Murinae |
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Abstract | In Francisella tularensis subsp. tularensis, DsbA has been shown to be an essential virulence factor and has been observed to migrate to multiple protein spots on two-dimensional electrophoresis gels. In this work, we show that the protein is modified with a 1,156-Da glycan moiety in O-linkage. The results of mass spectrometry studies suggest that the glycan is a hexasaccharide, comprised of N-acetylhexosamines, hexoses, and an unknown monosaccharide. Disruption of two genes within the FTT0789-FTT0800 putative polysaccharide locus, including a galE homologue (FTT0791) and a putative glycosyltransferase (FTT0798), resulted in loss of glycan modification of DsbA. The F. tularensis subsp. tularensis ΔFTT0798 and ΔFTT0791::Cm mutants remained virulent in the murine model of subcutaneous tularemia. This indicates that glycosylation of DsbA does not play a major role in virulence under these conditions. This is the first report of the detailed characterization of the DsbA glycan and putative role of the FTT0789-FTT0800 gene cluster in glycan biosynthesis. © 2011, American Society for Microbiology. |
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Publication date | 2011 |
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In | |
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Language | English |
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Peer reviewed | Yes |
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NPARC number | 21271529 |
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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 | ff4ea084-87c7-4727-8697-482df059dacf |
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Record created | 2014-03-24 |
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Record modified | 2020-04-21 |
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