Discovery of a secreted Bacteroides fragilis mucinase that cleaves mucins with bis-T O-glycans through a carbohydrate binding module-dependent mechanism - PubMed
6 hours ago
- #Microbiome
- #O-glycans
- #Mucinase
- Discovery of nine CBM-bearing M60-like mucinases in gut commensals and opportunists, including Bacteroides fragilis mucinase HC11.
- Two functional classes of mucinases identified: BT4244 prefers bis-Tn O-glycans, HC11 prefers bis-T O-glycans.
- Carbohydrate-binding modules (CBM32) are essential for efficient cleavage of extended mucin substrates.
- Bacteroides fragilis secretes HC11 and degrades mucins only after sialic acid removal.
- CBM-catalytic cooperation suggested as a mechanism for controlling mucus turnover and barrier integrity.