N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
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.
Wacker
Michael
M
Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
Linton
Dennis
D
Hitchen
Paul G
PG
Nita-Lazar
Mihai
M
Haslam
Stuart M
SM
North
Simon J
SJ
Panico
Maria
M
Morris
Howard R
HR
Dell
Anne
A
Wren
Brendan W
BW
Aebi
Markus
M
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
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