ArticleThe Journal of biological chemistry2008
Flagellin glycosylation in Pseudomonas aeruginosa PAK requires the O-antigen biosynthesis enzyme WbpO.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
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- Identification of theFrontiers in cellular and infection microbiology · 2025Article
- The O-glycan is essential for the induction of protective antibodies against lethal infection by flagella A-bearingInfection and immunity · 2024Article
- Characterization of PglJ, a Glycosyltransferase in theBiochemistry · 2024Article
- Molecular characterisation of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation.PLoS neglected tropical diseases · 2023Article
- Flagella, Chemotaxis and Surface Sensing.Advances in experimental medicine and biology · 2022Article
- Article
- Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion.Nature communications · 2020Article
- Antibody Binding to the O-Specific Antigen of Pseudomonas aeruginosa O6 Inhibits Cell Growth.Antimicrobial agents and chemotherapy · 2020Article
- Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Flashy flagella: flagellin modification is relatively common and highly versatile among the Enterobacteriaceae.BMC genomics · 2016Article
- High Yield Overexpression, Refolding, Purification and Characterization of Pseudomonas aeruginosa Type B-Flagellin: An Improved Method Without Sonication.International journal of molecular and cellular medicine · 2016Article
- Polar Glycosylated and Lateral Non-Glycosylated Flagella from Aeromonas hydrophila Strain AH-1 (Serotype O11).International journal of molecular sciences · 2015Article
- O-Glycosylation of the N-terminal region of the serine-rich adhesin Srr1 of Streptococcus agalactiae explored by mass spectrometry.Molecular & cellular proteomics : MCP · 2014Article
- Gram-negative flagella glycosylation.International journal of molecular sciences · 2014Review
- Developing an international Pseudomonas aeruginosa reference panel.MicrobiologyOpen · 2013Article
- Posttranslational modification of flagellin FlaB in Shewanella oneidensis.Journal of bacteriology · 2013Article
- Variation in the complex carbohydrate biosynthesis loci of Acinetobacter baumannii genomes.PloS one · 2013Article
- Biosynthesis of UDP-GlcNAc, UndPP-GlcNAc and UDP-GlcNAcA involves three easily distinguished 4-epimerase enzymes, Gne, Gnu and GnaB.PloS one · 2013Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa PAK (serotype O6) produces a single polar, glycosylated flagellum composed of a-type flagellin. To determine whether or not flagellin glycosylation in this serotype requires O-antigen genes, flagellin was isolated from the wild type, three O-antigen-deficient mutants wbpL, wbpO, and wbpP, and a wbpO mutant complemented with a plasmid containing a wild-type copy of wbpO. Flagellin from the wbpO mutant was smaller (42 kDa) than that of the wild type (45 kDa), or other mutants strains, and exhibited an altered isoelectric point (pI 4.8) when compared with PAK flagellin (pI 4.6). These differences were because of the truncation of the glycan moiety in the wbpO-flagellin. Thus, flagellin glycosylation in P. aeruginosa PAK apparently requires a functional WbpO but not WbpP. Because WbpP was previously proposed to catalyze a metabolic step in the biosynthesis of B-band O-antigen that precedes the action of WbpO, these results prompted us to reevaluate the two-step pathway catalyzed by WbpO and WbpP. Results from WbpO-WbpP-coupled enzymatic assays showed that either WbpO or WbpP is capable of initiating the two-step pathway; however, the kinetic parameters favored the WbpO reaction to occur first, converting UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-glucuronic acid prior to the conversion to UDP-N-acetyl-D-galacturonic acid by WbpP. This is the first report to show that a C4 epimerase could utilize UDP-N-acetylhexuronic acid as a substrate.
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