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Updated: May 23, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
An engineered eukaryotic protein glycosylation pathway in Escherichia coli
Juan D Valderrama-Rincon1, Adam C Fisher, Judith H Merritt
1School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, New York, USA.
Abstract:
We performed bottom-up engineering of a synthetic pathway in Escherichia coli for the production of eukaryotic trimannosyl chitobiose glycans and the transfer of these glycans to specific asparagine residues in target proteins. The glycan biosynthesis was enabled by four eukaryotic glycosyltransferases, including the yeast uridine diphosphate-N-acetylglucosamine transferases Alg13 and Alg14 and the mannosyltransferases Alg1 and Alg2. By including the bacterial oligosaccharyltransferase PglB from Campylobacter jejuni, we successfully transferred glycans to eukaryotic proteins.
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