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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
New Series, Vol. 298, No. 5599 (Nov. 29, 2002), pp. 1790-1793
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/3833015
Page Count: 4
You can always find the topics here!Topics: Polysaccharides, Multigene family, Mass spectroscopy, Plasmids, Eukaryotic cells, Amino acids, Glycoproteins, Consensus sequence, Lectins, Antiserum
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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.
Science © 2002 American Association for the Advancement of Science