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N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
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 glycan structures for research and industrial applications.
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Citations
Cited by
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
“To cite just a few examples, the following glycans were mostly unknown when the previous version of this review was being written: functional sialylation in the fly nervous system (181); O-fucose and O-glucose glycans on Notch (182-184), and O-fucose on thrombospondin repeats (185) ; mucin type O-glycosylation in prot…”
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
Self-citationCarbohydrate-active enzymes (CAZymes) in the gut microbiome
Wardman, J. F., Bains, R. K., Rahfeld, P., & Withers, S. G. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00712-1 · Cited by 597
Major findings and recent advances in virus–like particle (VLP)-based vaccines
Mohsen, M. O., Zha, L., Cabral-Miranda, G., & Bachmann, M. F. (2017) · Seminars in Immunology · doi:10.1016/j.smim.2017.08.014 · Cited by 555
Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall
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Metadata
- Authors
- Wacker, M., Linton, D., Hitchen, P. G., Nita-Lazar, M., Haslam, S. M., North, S. J., Panico, M., Morris, H. R., Dell, A., Wren, B. W., & Aebi, M.
- Venue
- Science
- Published
- 2002-11-29
- Volume
- 298
- Issue
- 5599
- Pages
- 1790-1793
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2161171034
- Cited by
- 777
- References
- 0
- FWCI
- 8.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli. https://app.cochat.ai/papers/10.1126/science.298.5599.1790
- The paper
- Wacker, M., Linton, D., Hitchen, P. G., Nita-Lazar, M., Haslam, S. M., North, S. J., Panico, M., Morris, H. R., Dell, A., Wren, B. W., & Aebi, M. (2002). N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli. Science. https://doi.org/10.1126/science.298.5599.1790
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
