Journal article
Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation
JA Iwashkiw, A Seper, BS Weber, NE Scott, E Vinogradov, C Stratilo, B Reiz, SJ Cordwell, R Whittal, S Schild, MF Feldman
Plos Pathogens | PUBLIC LIBRARY SCIENCE | Published : 2012
Abstract
Acinetobacter baumannii is an emerging cause of nosocomial infections. The isolation of strains resistant to multiple antibiotics is increasing at alarming rates. Although A. baumannii is considered as one of the more threatening "superbugs" for our healthcare system, little is known about the factors contributing to its pathogenesis. In this work we show that A. baumannii ATCC 17978 possesses an O-glycosylation system responsible for the glycosylation of multiple proteins. 2D-DIGE and mass spectrometry methods identified seven A. baumannii glycoproteins, of yet unknown function. The glycan structure was determined using a combination of MS and NMR techniques and consists of a branched penta..
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Awarded by National Health and Medical Research Council
Funding Acknowledgements
This work was supported by grants from Alberta Innovates Technology Futures, the Natural Sciences and Engineering Research Council of Canada (NSERC), the Alberta Glycomics Centre to MFF, Austrian Science Fund (FWF) grants:F3005-B12 LIPOTOX, P229686 and W901 (DK Molecular Enzymology) to A. S. and S. S. NES is the recipient of a CJ Martin Overseas Biomedical Postdoctoral Research Fellow supported by The National Health and Medical Research Foundation of Australia (grant number: APP1037373). MFF is an Alberta Heritage Foundation for Medical Research (AHFMR) scholar and a Canadian Institutes of Health Research (CIHR) New Investigator. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.