Characterization of the Clostridioides difficile 630Δerm putative Pro-Pro endopeptidase CD1597.

ABSTRACT: Clostridioides difficile is the leading cause of antibiotic-associated infections worldwide. Within the host, C. difficile can transition from a sessile to a motile state by secreting PPEP-1, which releases the cells from the intestinal epithelium by cleaving adhesion proteins. PPEP-1 belongs to the group of Pro-Pro endopeptidases (PPEPs), which are characterized by their unique ability to cleave proline-proline bonds. Interestingly, another putative member of this group, CD1597, is present in C. difficile. Although it possesses a domain similar to other PPEPs, CD1597 displays several distinct features that suggest a markedly different role for this protein. We investigated the proteolytic activity of CD1597 by testing various potential substrates. In addition, we inve

SUBMITTER: Claushuis B 

PROVIDER: S-EPMC11460543 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature