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

• DOI: 10.1126/science.298.5599.1790
• Publication Date: 2002-11-29T15:32:06Z
• Authors: 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; Markus Aebi
• Keywords: N-linked glycosylation; Cloning (programming)

N-linked protein glycosylation is the most abundant posttranslation modification of secretory proteins in eukaryotes. A wide range functions are attributed to glycan structures covalently linked asparagine residues within asparagine-X-serine/threonine consensus sequence (Asn-Xaa-Ser/Thr). We found an system bacterium Campylobacter jejuni and demonstrate that a functional pathway could be transferred into Escherichia coli . Although bacterial N-glycan differs structurally from its eukaryotic counterparts, cloning universal cassette E. opens up possibility engineering permutations recombinant for research industrial applications.