ArticleThe Journal of biological chemistry2010
Characterization of the O-antigen polymerase (Wzy) of Francisella tularensis.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Immunosensors and Immunoassays to DetectBiosensors · 2026Review
- CRISPR-based mutagenesis of lipopolysaccharide biosynthesis genes in Leptospira interrogans reveals gene essentiality and confirms the role of an O-antigen polymerase.Scientific reports · 2026Article
- Recent insights into Wzy polymerases and lipopolysaccharide O-antigen biosynthesis.Journal of bacteriology · 2025Review
- Recent advances in understanding of enterobacterial common antigen synthesis and regulation.Open biology · 2025Review
- Construction and Validation of a Genome-Scale Metabolic Network of Thermotoga sp. Strain RQ7.Applied biochemistry and biotechnology · 2021Article
- Glycoconjugate vaccine using a genetically modified O antigen induces protective antibodies toProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Transcriptome and Comparative Genomics Analyses Reveal New Functional Insights on Key Determinants of Pathogenesis and Interbacterial Competition inApplied and environmental microbiology · 2019Article
- The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of theFrontiers in cellular and infection microbiology · 2017Article
- Chemoenzymatic synthesis of the bacterial polysaccharide repeating unit undecaprenyl pyrophosphate and its analogs.Nature protocols · 2016Article
- A Bacteriophage-Acquired O-Antigen Polymerase (Wzyβ) from P. aeruginosa Serotype O16 Performs a Varied Mechanism Compared to Its Cognate Wzyα.Frontiers in microbiology · 2016Article
- Characterization of Francisella tularensis Schu S4 mutants identified from a transposon library screened for O-antigen and capsule deficiencies.Frontiers in microbiology · 2015Article
- Mutational analysis of the Shigella flexneri O-antigen polymerase Wzy: identification of Wzz-dependent Wzy mutants.Journal of bacteriology · 2015Article
- O-antigen polymerase adopts a distributive mechanism for lipopolysaccharide biosynthesis.Applied microbiology and biotechnology · 2014Article
- Francisella tularensis Schu S4 lipopolysaccharide core sugar and O-antigen mutants are attenuated in a mouse model of tularemia.Infection and immunity · 2014Article
- Comparative review of Francisella tularensis and Francisella novicida.Frontiers in cellular and infection microbiology · 2014Review
- Haemophilus parainfluenzae expresses diverse lipopolysaccharide O-antigens using ABC transporter and Wzy polymerase-dependent mechanisms.International journal of medical microbiology : IJMM · 2013Article
- Bifidobacterium animalis subsp. lactis ATCC 27673 is a genomically unique strain within its conserved subspecies.Applied and environmental microbiology · 2013Article
- The atypical lipopolysaccharide of Francisella.Carbohydrate research · 2013Review
- Article
- Francisella is sensitive to insect antimicrobial peptides.Journal of innate immunity · 2013Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
The O-antigen polymerase of gram-negative bacteria has been difficult to characterize. Herein we report the biochemical and functional characterization of the protein product (Wzy) of the gene annotated as the putative O-antigen polymerase, which is located in the O-antigen biosynthetic locus of Francisella tularensis. In silico analysis (homology searching, hydropathy plotting, and codon usage assessment) strongly suggested that Wzy is an O-antigen polymerase whose function is to catalyze the addition of newly synthesized O-antigen repeating units to a glycolipid consisting of lipid A, inner core polysaccharide, and one repeating unit of the O-polysaccharide (O-PS). To characterize the function of the Wzy protein, a non-polar deletion mutant of wzy was generated by allelic replacement, and the banding pattern of O-PS was observed by immunoblot analysis of whole-cell lysates obtained by SDS-PAGE and stained with an O-PS-specific monoclonal antibody. These immunoblot analyses showed that O-PS of the wzy mutant expresses only one repeating unit of O-antigen. Further biochemical characterization of the subcellular fractions of the wzy mutant demonstrated that (as is characteristic of O-antigen polymerase mutants) the low molecular weight O-antigen accumulates in the periplasm of the mutant. Site-directed mutagenesis based on protein homology and topology, which was carried out to locate a catalytic residue of the protein, showed that modification of specific residues (Gly(176), Asp(177), Gly(323), and Tyr(324)) leads to a loss of O-PS polymerization. Topology models indicate that these amino acids most likely lie in close proximity on the bacterial surface.
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