The examination of the protease inhibitor ecotin and n-linked glycosylation in campylobacter species, an insight into cell protection in the protease rich environment of the human host

Protection from proteolysis is important for bacteria living in a competitive niche under attack by host defense mechanisms. Campylobacter species possess an N-linked protein glycosylation system, where an oligosaccharide is attached to asparagine residues or released as free oligosaccharide. The glycosylation of these proteins can stabilize proteins such as the multidrug efflux pump of C. jejuni that helps efflux antibiotics and toxic compounds.Glycosylation can also mask cleavage sites protecting against proteolytic activity. OralCampylobacter species have also developed an additional method for protection against proteases. Ecotin homologues have been identified in these non-thermophilic Campylobacter species. Ecotin is a generic serine-protease inhibitor that can bind and inhibit a wide range of proteases released by the host. The combination of N-glycosylation and ecotin helps provide Campylobacter species inhabiting the protease-rich oral cavity with additional mechanisms for bacterial fitness and survival in the human host.