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Membrane-associated lipoproteins have important functions in bacterial pathogenesis and physiology. According to the available genomic sequences, C. jejuni possesses multiple lipoproteins, but the majority of them have not yet been functionally characterized. To better understand the pathogenic mechanisms of C. jejuni, in this work we characterized a threegene operon (cj0089, cj0090, and cj0091) encoding a cluster of lipoproteins. It was shown that this lipoprotein-encoding operon is indirectly regulated by CmeR, a transcriptional regulator repressing the expression of the multidrug efflux pump CmeABC in C. jejuni. We determined that Cj0091 is an outer membrane associated protein, identified it as a new adhesin in C. jejuni, and demonstrated that this protein is involved in Campylobacter colonization in vivo. This study suggests that Cj0091 may be a promising candidate for the development of vaccines to reduce Campylobacter colonization in animal hosts.

Regulation and function of a cluster of lipoproteins in Campylobacter jejuni