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Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):3016-21. Epub 2005 Feb 9.

Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli.

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Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, ETH-Hönggeberg, CH-8093 Zurich, Switzerland.


Campylobacter jejuni has a general N-linked protein glycosylation system that can be functionally transferred to Escherichia coli. In this study, we engineered E. coli cells in a way that two different pathways, protein N-glycosylation and lipopolysaccharide (LPS) biosynthesis, converge at the step in which PglB, the key enzyme of the C. jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB was the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer. The relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure was exploited to create novel N-glycan structures containing two distinct E. coli or Pseudomonas aeruginosa O antigens. PglB-mediated transfer of polysaccharides might be valuable for in vivo production of O polysaccharides-protein conjugates for use as antibacterial vaccines.

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