Functional analysis of Clostridium difficile sortase B reveals key residues for catalytic activity and substrate specificity.

ABSTRACT: Most of Gram-positive bacteria anchor surface proteins to the peptidoglycan cell wall by sortase, a cysteine transpeptidase that targets proteins displaying a cell wall sorting signal. Unlike other bacteria, Clostridium difficile, the major human pathogen responsible for antibiotic-associated diarrhea, has only a single functional sortase (SrtB). Sortase's vital importance in bacterial virulence has been long recognized, and C. difficile sortase B (Cd-SrtB) has become an attractive therapeutic target for managing C. difficile infection. A better understanding of the molecular activity of Cd-SrtB may help spur the development of effective agents against C. difficile infection. In this study, using site-directed mutagenesis, biochemical and biophysical tools, LC-M

SUBMITTER: Kang CY 

PROVIDER: S-EPMC7076211 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature