ArticleMolecular & cellular proteomics : MCP2012
Characterization of protein glycosylation in Francisella tularensis subsp. holarctica: identification of a novel glycosylated lipoprotein required for virulence.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Review
- Virulence and genome analysis of three historicalFrontiers in cellular and infection microbiology · 2025Article
- Article
- Article
- HU protein is involved in intracellular growth and full virulence of Francisella tularensis.Virulence · 2018Article
- How Sweet Are Our Gut Beneficial Bacteria? A Focus on Protein Glycosylation in Lactobacillus.International journal of molecular sciences · 2018Review
- Role of Glycosylation/Deglycolysation Processes inFrontiers in cellular and infection microbiology · 2017Review
- Glycosylation of a Capsule-Like Complex (CLC) byFrontiers in microbiology · 2017Article
- Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum.Glycobiology · 2016Article
- From the Outside-In: The Francisella tularensis Envelope and Virulence.Frontiers in cellular and infection microbiology · 2015Review
- The post-translational modification of the Clostridium difficile flagellin affects motility, cell surface properties and virulence.Molecular microbiology · 2014Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- Uncovering the components of the Francisella tularensis virulence stealth strategy.Frontiers in cellular and infection microbiology · 2014Review
- Recent trends in analytical and structural glycobiology.Current opinion in chemical biology · 2013Review
- High-sensitivity analytical approaches for the structural characterization of glycoproteins.Chemical reviews · 2013Review
- Analytical glycobiology at high sensitivity: current approaches and directions.Glycoconjugate journal · 2013Review
- Roles forPathogens (Basel, Switzerland) · 2012Article
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
FTH_0069 is a previously uncharacterized strongly immunoreactive protein that has been proposed to be a novel virulence factor in Francisella tularensis. Here, the glycan structure modifying two C-terminal peptides of FTH_0069 was identified utilizing high resolution, high mass accuracy mass spectrometry, combined with in-source CID tandem MS experiments. The glycan observed at m/z 1156 was determined to be a hexasaccharide, consisting of two hexoses, three N-acetylhexosamines, and an unknown monosaccharide containing a phosphate group. The monosaccharide sequence of the glycan is tentatively proposed as X-P-HexNAc-HexNAc-Hex-Hex-HexNAc, where X denotes the unknown monosaccharide. The glycan is identical to that of DsbA glycoprotein, as well as to one of the multiple glycan structures modifying the type IV pilin PilA, suggesting a common biosynthetic pathway for the protein modification. Here, we demonstrate that the glycosylation of FTH_0069, DsbA, and PilA was affected in an isogenic mutant with a disrupted wbtDEF gene cluster encoding O-antigen synthesis and in a mutant with a deleted pglA gene encoding pilin oligosaccharyltransferase PglA. Based on our findings, we propose that PglA is involved in both pilin and general F. tularensis protein glycosylation, and we further suggest an inter-relationship between the O-antigen and the glycan synthesis in the early steps in their biosynthetic pathways.
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