N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
École Polytechnique Fédérale de Lausanne · University of London · +2 more institutions
Abstract
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…
Citation impact
- FWCI
- 8.63
- Percentile
- 100%
- References
- 20
Authors
11- MWMichael WackerCorresponding
École Polytechnique Fédérale de Lausanne
- DLDennis LintonCorresponding
University of London, London School of Hygiene & Tropical Medicine
- PGPaul G. Hitchen
Imperial College London
- MNMihai Niţă‐Lazăr
École Polytechnique Fédérale de Lausanne
- SMStuart M. Haslam
Imperial College London
Topics & keywords
- Glycosylation
- Campylobacter jejuni
- Asparagine
- Glycan
- Threonine
- Escherichia coli
- Serine
- Biology