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Nat Commun ; 10(1): 5403, 2019 11 27.
Article in English | MEDLINE | ID: mdl-31776333

ABSTRACT

Glycosylation of proteins profoundly impacts their physical and biological properties. Yet our ability to engineer novel glycoprotein structures remains limited. Established bacterial glycoengineering platforms require secretion of the acceptor protein to the periplasmic space and preassembly of the oligosaccharide substrate as a lipid-linked precursor, limiting access to protein and glycan substrates respectively. Here, we circumvent these bottlenecks by developing a facile glycoengineering platform that operates in the bacterial cytoplasm. The Glycoli platform leverages a recently discovered site-specific polypeptide glycosyltransferase together with variable glycosyltransferase modules to synthesize defined glycans, of bacterial or mammalian origin, directly onto recombinant proteins in the E. coli cytoplasm. We exploit the cytoplasmic localization of this glycoengineering platform to generate a variety of multivalent glycostructures, including self-assembling nanomaterials bearing hundreds of copies of the glycan epitope. This work establishes cytoplasmic glycoengineering as a powerful platform for producing glycoprotein structures with diverse future biomedical applications.


Subject(s)
Cytoplasm/metabolism , Glycoproteins/biosynthesis , Metabolic Engineering/methods , Benzazepines , Epitopes/metabolism , Escherichia coli/genetics , Escherichia coli/metabolism , Glucose/chemistry , Glucose/metabolism , Glucosyltransferases/metabolism , Glycoproteins/genetics , Glycoproteins/immunology , Glycosylation , Green Fluorescent Proteins/genetics , Green Fluorescent Proteins/metabolism , Monosaccharides , Polysaccharides/metabolism , Promoter Regions, Genetic , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics
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