Abstract:
:Trehalose is a disaccharide formed from two glucose molecules. This sugar molecule can be isolated from a range of organisms including bacteria, fungi, plants and invertebrates. Trehalose has a variety of functions including a role as an energy storage molecule, a structural component of glycolipids and plays a role in the virulence of some microorganisms. There are many metabolic pathways that control the biosynthesis and degradation of trehalose in different organisms. The enzyme trehalase forms part of a pathway that converts trehalose into glucose. In this study we set out to investigate whether trehalase plays a role in both stress adaptation and virulence of Burkholderia pseudomallei. We show that a trehalase deletion mutant (treA) had increased tolerance to thermal stress and produced less biofilm than the wild type B. pseudomallei K96243 strain. We also show that the ΔtreA mutant has reduced ability to survive in macrophages and that it is attenuated in both Galleria mellonella (wax moth larvae) and a mouse infection model. This is the first report that trehalase is important for bacterial virulence.
journal_name
Virulencejournal_title
Virulenceauthors
Vanaporn M,Sarkar-Tyson M,Kovacs-Simon A,Ireland PM,Pumirat P,Korbsrisate S,Titball RW,Butt Adoi
10.1080/21505594.2016.1199316subject
Has Abstractpub_date
2017-01-02 00:00:00pages
30-40issue
1eissn
2150-5594issn
2150-5608journal_volume
8pub_type
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