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

Michael Wacker, Dennis Linton, Paul G. Hitchen, Mihai Nita-Lazar, Stuart M. Haslam, Simon J. North, Maria Panico, Howard R. Morris, Anne Dell, Brendan W. Wren and Markus Aebi
Science
New Series, Vol. 298, No. 5599 (Nov. 29, 2002), pp. 1790-1793
Stable URL: http://www.jstor.org/stable/3833015
Page Count: 4
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N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
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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 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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