N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
Wacker, Michael;
Linton, Dennis;
Hitchen, Paul G;
Nita-Lazar, Mihai;
Haslam, Stuart M;
North, Simon J;
Panico, Maria;
Morris, Howard R;
Dell, Anne;
Wren, Brendan W;
+1 more...Aebi, Markus;
(2002)
N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.
Science (New York, NY), 298 (5599).
pp. 1790-1793.
ISSN 0036-8075
DOI: https://doi.org/10.1126/science.298.5599.1790
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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.