Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.

ABSTRACT: Glycosyltransferases (GTs) catalyze the formation of new glycosidic bonds and thus are vital for synthesizing nature's vast repertoire of glycans and glycoconjugates and for engineering glycan-related medicines and materials. However, obtaining detailed structural and functional insights for the >750,000 known GTs is limited by difficulties associated with their efficient recombinant expression. Members of the GT-C fold, in particular, pose the most significant expression challenges due to the integration and folding requirements of their multiple membrane-spanning regions. Here, we address this challenge by engineering water-soluble variants of an archetypal GT-C fold enzyme, namely the oligosaccharyltransferase PglB from Campylobacter jejuni (CjPglB), which possesses 13 hyd

SUBMITTER: Kwon YH 

PROVIDER: S-EPMC12879670 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature