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Adherence of  Campylobacter jejuni  to its particular host cells is mediated by several pathogen proteins. We screened a transposon-based mutant library of  C. jejuni  in order to identify clones with an invasion deficient phenotype towards Caco2 cells and detected a mutant with the transposon insertion in gene  cj0268c .  In vitro  characterization of a generated non-random mutant, the mutant complemented with an intact copy of  cj0268c  and parental strain NCTC 11168 confirmed the relevance of Cj0268c in the invasion process, in particular regarding adherence to host cells. Whereas Cj0268c does not impact autoagglutination or motility of  C. jejuni , heterologous expression in  E. coli  strain DH5α enhanced the potential of the complemented  E. coli  strain to adhere to Caco2 cells significantly and, thus, indicates that Cj0268c does not need to interact with other  C. jejuni  proteins to develop its adherence-mediating phenotype. Flow cytometric measurements of  E. coli  expressing Cj0268c indicate a localization of the protein in the periplasmic space with no access of its C-terminus to the bacterial surface. Since a respective knockout mutant possesses clearly reduced resistance to Triton X-100 treatment, Cj0268c contributes to the stability of the bacterial cell wall. Finally, we could show that the presence of  cj0268c  seems to be ubiquitous in isolates of  C. jejuni  and does not correlate with specific clonal groups regarding pathogenicity or pathogen metabolism.

The Campylobacter jejuni Cj0268c Protein Is Required for Adhesion and Invasion In Vitro