Journal article
A general protein O-glycosylation system within the Burkholderia cepacia complex is involved in motility and virulence
KV Lithgow, NE Scott, JA Iwashkiw, ELS Thomson, LJ Foster, MF Feldman, JJ Dennis
Molecular Microbiology | WILEY | Published : 2014
DOI: 10.1111/mmi.12540
Abstract
Bacteria of the Burkholderia cepacia complex (Bcc) are pathogens of humans, plants, and animals. Burkholderia cenocepacia is one of the most common Bcc species infecting cystic fibrosis (CF) patients and its carriage is associated with poor prognosis. In this study, we characterized a general O-linked protein glycosylation system in B.cenocepaciaK56-2. The PglLBc O-oligosaccharyltransferase (O-OTase), encoded by the cloned gene bcal0960, was shown to be capable of transferring a heptasaccharide from the Campylobacter jejuniN-glycosylation system to a Neisseria meningitides-derived acceptor protein in an Escherichia coli background, indicating that the enzyme has relaxed specificities for bot..
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Funding Acknowledgements
The authors thank Erin M. Dockery and Fatima Kamal of the Department of Biological Sciences, University of Alberta, and Sucharita Dutta and Julian Saba of Thermo Fisher Scientific for excellent technical assistance. The authors also thank Corey Wenzel and Brent Weber for editorial critique. All authors have no conflicts of interest to declare pertaining to pertinent commercial or other relationships. N.E.S. is supported by the National Health and Medical Research Council of Australia (NHMRC) Overseas (Biomedical) Fellow (APP1037373). M. F. F. is supported as a Canadian Institutes of Health Research (CIHR) New Investigator. This work was supported by grants to M. F. F. from the Alberta Glycomics Centre and the Natural Sciences and Engineering Research Council of Canada (NSERC). J.J.D. kindly acknowledges financial support in the form of operating grants from Cystic Fibrosis Canada (SFR1219) and NSERC (RES0001291).