A "terminal" case of glycan catabolism: Structural and enzymatic characterization of the sialidases of Clostridium perfringens.

ABSTRACT: Sialic acids are commonly found on the terminal ends of biologically important carbohydrates, including intestinal mucin O-linked glycans. Pathogens such as Clostridium perfringens, the causative agent of necrotic enteritis in poultry and humans, have the ability to degrade host mucins and colonize the mucus layer, which involves removal of the terminal sialic acid by carbohydrate-active enzymes (CAZymes). Here, we present the structural and biochemical characterization of the GH33 catalytic domains of the three sialidases of C. perfringens and probe their substrate specificity. The catalytically active domains, which we refer to as NanH_GH33, NanJ_GH33, and NanI_GH33, displayed differential activity on various naturally occurring forms of sialic acid. We repo

SUBMITTER: Medley BJ 

PROVIDER: S-EPMC11525138 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature