Identification and Functional Characterization of the Polymerizing Glycosyltransferase Required for the Transfer of d-Ribose to the d-Gal<i>f</i>NAc Moiety of the Capsular Polysaccharide of <i>Campylobacter jejuni</i>.

ABSTRACT: Campylobacter jejuni is the leading cause of food poisoning in the United States. The exterior surface of this bacterium is coated with a capsular polysaccharide (CPS) that helps protect the organism from the host immune system. In the HS:2 serotype of strain C. jejuni NCTC 11168, the minimal repeating trisaccharide consist of d-ribose, N-acetyl-d-galactosamine (GalNAc) and the serinol amide of d-glucuronic acid. Here we demonstrate that the C-terminal domain of Cj1432 (residues 574-914) is responsible for the transfer of d-ribose-5-P from phosphoribosyl pyrophosphate (PRPP) to C5 of the d-GalfNAc moiety of the growing polysaccharide chain. In the next step the middle domain of Cj1432 (residues 357-573) catalyzes the hydrolysis of phosphate from this product. Th

SUBMITTER: Xiang DF 

PROVIDER: S-EPMC12096443 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature