Abstract
N-linked protein glycosylation is the most abundant posttranslation modification of secretory proteins in eukaryotes. A wide range of functions are attributed to glycan structures covalently linked to asparagine residues within the asparagine-X-serine/threonine consensus sequence (Asn-Xaa-Ser/Thr). We found an N-linked glycosylation system in the bacterium Campylobacter jejuni and demonstrate that a functional N-linked glycosylation pathway could be transferred into Escherichia coli. Although the bacterial N-glycan differs structurally from its eukaryotic counterparts, the cloning of a universal N-linked glycosylation cassette in E. coli opens up the possibility of engineering permutations of recombinant glycan structures for research and industrial applications.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Campylobacter jejuni / genetics
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Campylobacter jejuni / metabolism*
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Carbohydrate Conformation
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Cloning, Molecular*
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Conjugation, Genetic
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Consensus Sequence
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Genes, Bacterial
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Genetic Complementation Test
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Glycoproteins / chemistry
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Glycoproteins / metabolism*
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Glycosylation
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Glycosyltransferases / genetics
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Glycosyltransferases / metabolism
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Lipoproteins / genetics
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Lipoproteins / isolation & purification
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Lipoproteins / metabolism
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Mass Spectrometry
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Membrane Transport Proteins
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Models, Biological
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Mutation
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Polysaccharides, Bacterial / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Transformation, Bacterial
Substances
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AcrA protein, E coli
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Bacterial Proteins
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Escherichia coli Proteins
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Glycoproteins
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Lipoproteins
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Membrane Transport Proteins
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Polysaccharides, Bacterial
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Recombinant Proteins
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Glycosyltransferases