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N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli

Science  29 Nov 2002:
Vol. 298, Issue 5599, pp. 1790-1793
DOI: 10.1126/science.298.5599.1790

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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 jejuniand 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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: aebi{at}micro.biol.ethz.ch

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