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. 2002 Nov 29;298(5599):1790-3.
doi: 10.1126/science.298.5599.1790.

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli

Michael Wacker  1 , Dennis Linton, Paul G Hitchen, Mihai Nita-Lazar, Stuart M Haslam, Simon J North, Maria Panico, Howard R Morris, Anne Dell, Brendan W Wren, Markus Aebi
Affiliations

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli

Michael Wacker et al. Science. .

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.

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