Journal article
N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
- Wacker M Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
- Linton D
- Hitchen PG
- Nita-Lazar M
- Haslam SM
- North SJ
- Panico M
- Morris HR
- Dell A
- Wren BW
- Aebi M
- 2002-12-03
Published in:
- Science (New York, N.Y.). - 2002
Bacterial Proteins
Campylobacter jejuni
Carbohydrate Conformation
Cloning, Molecular
Conjugation, Genetic
Consensus Sequence
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Genetic Complementation Test
Glycoproteins
Glycosylation
Glycosyltransferases
Lipoproteins
Mass Spectrometry
Membrane Transport Proteins
Models, Biological
Mutation
Polysaccharides, Bacterial
Recombinant Proteins
Transformation, Bacterial
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
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- DOI 10.1126/science.298.5599.1790
- PMID 12459590
- Persistent URL
- https://sonar.ch/global/documents/67004
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