| Literature DB >> 21803994 |
Rebecca M Thomas1, Susan M Twine, Kelly M Fulton, Luc Tessier, Sara L N Kilmury, Wen Ding, Nicholas Harmer, Stephen L Michell, Petra C F Oyston, Richard W Titball, Joann L Prior.
Abstract
In Francisella tularensis subsp. tularensis, DsbA has been shown to be an essential virulence factor and has been observed to migrate to multiple protein spots on two-dimensional electrophoresis gels. In this work, we show that the protein is modified with a 1,156-Da glycan moiety in O-linkage. The results of mass spectrometry studies suggest that the glycan is a hexasaccharide, comprised of N-acetylhexosamines, hexoses, and an unknown monosaccharide. Disruption of two genes within the FTT0789-FTT0800 putative polysaccharide locus, including a galE homologue (FTT0791) and a putative glycosyltransferase (FTT0798), resulted in loss of glycan modification of DsbA. The F. tularensis subsp. tularensis ΔFTT0798 and ΔFTT0791::Cm mutants remained virulent in the murine model of subcutaneous tularemia. This indicates that glycosylation of DsbA does not play a major role in virulence under these conditions. This is the first report of the detailed characterization of the DsbA glycan and putative role of the FTT0789-FTT0800 gene cluster in glycan biosynthesis.Entities:
Mesh：
Substances：
Year: 2011 PMID： 21803994 PMCID： PMC3187430 DOI： 10.1128/JB.00438-11
Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490