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Science 29 November 2002:
Vol. 298. no. 5599, pp. 1790 - 1793
DOI: 10.1126/science.298.5599.1790

Reports

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

Michael Wacker,1* Dennis Linton,2* Paul G. Hitchen,3 Mihai Nita-Lazar,1 Stuart M. Haslam,3 Simon J. North,3 Maria Panico,3 Howard R. Morris,34 Anne Dell,3 Brendan W. Wren,2 Markus Aebi1dagger

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.

1 Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, Zürich, CH-8092 Zürich, Switzerland.
2 Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London WC1E 7HT, UK.
3 Department of Biological Sciences, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK.
4 M-SCAN Mass Spectrometry Research and Training Centre, Silwood Park, Ascot SL5 7PZ, UK.
*   These authors contributed equally to this work.

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


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