Reinvestigation into the role of lipopolysaccharide Glycosyltransferases in Helicobacter pylori protein glycosylation.

ABSTRACT: Protein glycosylation has been considered as a fundamental phenomenon shared by all domains of life. In Helicobacter pylori, glycosylation of flagellins A and B with pseudaminic acid have been rigorously confirmed and shown to be essential for flagella assembly and bacterial colonization. In addition to flagellins, several other proteins including RecA, AlpA/B, and BabA/B in H. pylori have also been reported to be glycosylated and to be dependent on the lipopolysaccharide (LPS) biosynthetic pathway. However, these proteins have not been purified for sugar-specific staining or structural analysis to confirm the existence of carbohydrate motifs. Here, using a combined approach of genetics, protein purification, and sugar-specific staining, we demonstrate that RecA is not a glyc

SUBMITTER: Li H 

PROVIDER: S-EPMC12931685 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature