Commonality and biosynthesis of the O-methyl phosphoramidate capsule modification in Campylobacter jejuni: J.Biol.Chem.

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TypeArticle
Journal titleJournal Of Biological Chemistry
Volume282
Issue39
Pages2856628576; # of pages: 11
SubjectAmides; angle; Animals; Bacteria; bacterial; Bacterial Capsules; Bacterial Proteins; biosynthesis; Bird Diseases; Campylobacter; Campylobacter coli; Campylobacter Infections; Campylobacter jejuni; Canada; capsular polysaccharide; capsule; Cecum; Chickens; CLUSTER; CPS; diagnosis; ELUCIDATION; Enteritis; Genetic Complementation Test; genetics; HIGH-RESOLUTION; Humans; Libraries; magic angle; magic angle spinning; Magnetic Resonance Spectroscopy; metabolism; METHYL; Microbiology; Miller Fisher Syndrome; Multigene Family; Multiple; MUTANT; MUTANTS; Mutation; NMR; NMR spectroscopy; NMR-spectroscopy; PATHWAY; Phosphoric Acids; POLYSACCHARIDE; Polysaccharides; Polysaccharides,Bacterial; Prevalence; RESOLUTION; SPECTROSCOPY; STRAIN; STRAINS; Syndrome; TARGET; therapy; transfer; transferase; Transferases; Typhlitis
AbstractIn this study we investigated the commonality and biosynthesis of the O-methyl phosphoramidate (MeOPN) group found on the capsular polysaccharide (CPS) of Campylobacter jejuni. High resolution magic angle spinning NMR spectroscopy was used as a rapid, high throughput means to examine multiple isolates, analyze the cecal contents of colonized chickens, and screen a library of CPS mutants for the presence of MeOPN. Sixty eight percent of C. jejuni strains were found to express the MeOPN with a high prevalence among isolates from enteritis, Guillain Barre, and Miller-Fisher syndrome patients. In contrast, MeOPN was not observed for any of the Campylobacter coli strains examined. The MeOPN was detected on C. jejuni retrieved from cecal contents of colonized chickens demonstrating that the modification is expressed by bacteria inhabiting the avian gastrointestinal tract. In C. jejuni 11168H, the cj1415-cj1418 cluster was shown to be involved in the biosynthesis of MeOPN. Genetic complementation studies and NMR/mass spectrometric analyses of CPS from this strain also revealed that cj1421 and cj1422 encode MeOPN transferases. Cj1421 adds the MeOPN to C-3 of the beta-d-GalfNAc residue, whereas Cj1422 transfers the MeOPN to C-4 of D-glycero-alpha-L-gluco-heptopyranose. CPS produced by the 11168H strain was found to be extensively modified with variable MeOPN, methyl, ethanolamine, and N-glycerol groups. These findings establish the importance of the MeOPN as a diagnostic marker and therapeutic target for C. jejuni and set the groundwork for future studies aimed at the detailed elucidation of the MeOPN biosynthetic pathway
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberMCNALLY2007
NPARC number9369723
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Record identifier25f3430f-cd95-4e86-bd59-8201d3ef28b6
Record created2009-07-10
Record modified2016-05-09
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