title: N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
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.
authors.affiliation: Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
authors.forename: Michael
authors.initials: M
authors.lastname: Wacker
authors.forename: Dennis
authors.initials: D
authors.lastname: Linton
authors.forename: Paul G
authors.initials: PG
authors.lastname: Hitchen
authors.forename: Mihai
authors.initials: M
authors.lastname: Nita-Lazar
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Haslam
authors.forename: Simon J
authors.initials: SJ
authors.lastname: North
authors.forename: Maria
authors.initials: M
authors.lastname: Panico
authors.forename: Howard R
authors.initials: HR
authors.lastname: Morris
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
authors.forename: Brendan W
authors.initials: BW
authors.lastname: Wren
authors.forename: Markus
authors.initials: M
authors.lastname: Aebi
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D016123:Campylobacter jejuni / Q000235:genetics / Q000378:metabolism*; D002236:Carbohydrate Conformation; D003001:Cloning, Molecular; D003227:Conjugation, Genetic; D016384:Consensus Sequence; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D005816:Genetic Complementation Test; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D016695:Glycosyltransferases / Q000235:genetics / Q000378:metabolism; D008074:Lipoproteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013058:Mass Spectrometry; D026901:Membrane Transport Proteins; D008954:Models, Biological; D009154:Mutation; D011135:Polysaccharides, Bacterial / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014169:Transformation, Bacterial
chemical_list: C083497:AcrA protein, E coli; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006023:Glycoproteins; D008074:Lipoproteins; D026901:Membrane Transport Proteins; D011135:Polysaccharides, Bacterial; D011994:Recombinant Proteins; D016695:Glycosyltransferases