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    Expression Patterns and Role of CadF protein in Campylobacter jejuni and Campylobacter coli (2007)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Krause-Gruszczynska, M.
    van Alphen, L.
    Oyarzabal, O.A.
    Alter, T. (WE 8)
    Hänel, I.
    Schliephake, A.
    König, W.
    van Putten, J.
    Konkel, M.
    Backert, S.
    Quelle
    FEMS microbiology letters; 274(1) — S. 9–16
    ISSN: 0378-1097
    Sprache
    Englisch
    Verweise
    DOI: 10.1111/j.1574-6968.2007.00802.x
    Pubmed: 17573935
    Kontakt
    Institut für Lebensmittelsicherheit und -hygiene

    Königsweg 69
    14163 Berlin
    Tel.+49 30 838 62550 Fax.+49 30 838 46029
    email:lebensmittelhygiene@vetmed.fu-berlin.de

    Abstract / Zusammenfassung

    Binding of Campylobacter jejuni and Campylobacter coli to host fibronectin is mediated by the 37 kDa outer membrane protein CadF. Immunoblot analysis of 58 C. jejuni and C. coli isolates of human and animal origin showed that CadF is expressed in every strain. In most C. jejuni isolates, a 37 kDa band (p37) and a less-prominent 32 kDa band (p32) reacted with the antibodies. In C. coli isolates, CadF was consistently larger with sizes of 39 kDa (p39) and 34 kDa (p34), respectively. PCR analysis and sequencing revealed the presence of a 39-bp insertion sequence in the cadF gene of C. coli strains, explaining the increased molecular size. Infection assays revealed that C. jejuni bound and invaded INT-407 epithelial cells much more efficiently than C. coli and that this difference was considerably reduced in isogenic cadF mutants. These results demonstrate that CadF is an important pathogenicity factor. The difference between CadF of C. jejuni and C. coli may potentially be exploited to discriminate these species in food and clinical specimens.