Disulphide bond-forming enzymes in clostridial species.

ABSTRACT: Disulphide bond formation is critical for the folding and stability of proteins involved in bacterial cell envelope processes yet remains understudied in clostridial pathogens. While a few Clostridia-derived toxins and virulence factors are known to depend on disulphide bonds, the enzymes catalysing their formation are poorly characterized. Here, we performed a bioinformatic search to identify ten putative disulphide bond-forming enzymes in Clostridia. We cloned and codon-optimized these genes, testing their ability to complement Escherichia coli dsb mutants. Our analysis revealed a VKOR homologue, a VKOR-DsbA fusion and three DsbA homologues capable of complementing E. coli dsb mutants. Notably, Clostridium botulinum DsbA functioned independently of a regenerating par

SUBMITTER: Antonika C 

PROVIDER: S-EPMC12453122 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature