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Background  Acute gastroenteritis caused by the food-borne pathogen  Campylobacter jejuni  is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In  C. jejuni , the periplasmic protein HtrA is required for efficient binding to epithelial cells. HtrA has both protease and chaperone activity, and is important for virulence of several bacterial pathogens.    Results  The aim of this study was to determine the role of the dual activities of HtrA in host cell interaction of  C. jejuni  by comparing an  htrA  mutant lacking protease activity, but retaining chaperone activity, with a Δ htrA  mutant and the wild type strain. Binding of  C .  jejuni  to both epithelial cells and macrophages was facilitated mainly by HtrA chaperone activity that may be involved in folding of outer membrane adhesins. In contrast, HtrA protease activity played only a minor role in interaction with host cells.    Conclusion  We show that HtrA protease and chaperone activities contribute differently to  C. jejuni 's interaction with mammalian host cells, with the chaperone activity playing the major role in host cell binding.

HtrA chaperone activity contributes to host cell binding in Campylobacter jejuni