Clostridium difficile cell wall protein CwpV undergoes enzyme-independent intramolecular autoproteolysis.

ABSTRACT: Clostridium difficile infection is a leading cause of antibiotic-associated diarrhea, placing considerable economic pressure on healthcare systems and resulting in significant morbidity and mortality. The pathogen produces a proteinaceous array on its cell surface known as the S-layer, consisting primarily of the major S-layer protein SlpA and a family of SlpA homologs. CwpV is the largest member of this family and is expressed in a phase-variable manner. The protein is post-translationally processed into two fragments that form a noncovalent, heterodimeric complex. To date, no specific proteases capable of cleaving CwpV have been identified. Using site-directed mutagenesis we show that CwpV undergoes intramolecular autoproteolysis, most likely facilitated by a N-O acyl shift, with Thr-413

SUBMITTER: Dembek M 

PROVIDER: S-EPMC3256870 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature