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An engineered eukaryotic protein glycosylation pathway in Escherichia coli.


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.

SUBMITTER: Valderrama-Rincon JD 

PROVIDER: S-EPMC3449280 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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An engineered eukaryotic protein glycosylation pathway in Escherichia coli.

Valderrama-Rincon Juan D JD   Fisher Adam C AC   Merritt Judith H JH   Fan Yao-Yun YY   Reading Craig A CA   Chhiba Krishan K   Heiss Christian C   Azadi Parastoo P   Aebi Markus M   DeLisa Matthew P MP  

Nature chemical biology 20120325 5


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  ...[more]

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