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Science 29 November 2002: Vol. 298. no. 5599, pp. 1790 - 1793 DOI: 10.1126/science.298.5599.1790
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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 Aebi1
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.
To whom correspondence should be addressed. E-mail:
aebi{at}micro.biol.ethz.ch
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