A Campylobacter jejuni glycosylation island important in cell charge, legionaminic acid biosynthesis and colonisation of chickens.


Howard, SL; Jagannathan, A; Soo, EC; Hui, JP; Aubry, AJ; Ahmed, I; Karlyshev, A; Kelly, JF; Jones, MA; Stevens, MP; Logan, SM; Wren, BW; (2009) A Campylobacter jejuni glycosylation island important in cell charge, legionaminic acid biosynthesis and colonisation of chickens. Infection and immunity, 77 (6). pp. 2544-56. ISSN 0019-9567 DOI: https://doi.org/10.1128/IAI.01425-08

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Abstract

Previously, we identified five genes (Cj1321 to Cj1326, of which Cj1325 and Cj1326 are a single gene) in the O-linked flagellin glycosylation island that are highly prevalent in Campylobacter jejuni isolates from chickens. We report mutagenesis, functional, and structural data to confirm that this locus, and Cj1324 in particular, has a significant contributory role in the colonization of chickens by C. jejuni. A motile DeltaCj1324 mutant with intact flagella was considerably less hydrophobic and less able to autoagglutinate and form biofilms than the parent strain, 11168H, suggesting that the surface charge of flagella of Cj1324-deficient strains was altered. The physical and functional attributes of the parent were restored upon complementation. Structural analysis of flagellin protein purified from the DeltaCj1324 mutant revealed the absence of two legionaminic acid glycan modifications that were present in the parent strain, 11168H. These glycoform modifications were shown to be prevalent in chicken isolates and confirm that differences in the highly variable flagellin glycosylation locus can relate to the strain source. The discovery of molecular mechanisms influencing the persistence of C. jejuni in poultry aids the rational design of approaches to control this problematic pathogen in the food chain.

Item Type: Article
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 19307210
Web of Science ID: 266182400032
URI: http://researchonline.lshtm.ac.uk/id/eprint/5683

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