Trehalase plays a role in macrophage colonization and virulence of Burkholderia pseudomallei in insect and mammalian hosts
Taylor & Francis
Reason for embargo
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.
This work was supported by Defense Science and Technology Laboratory, grant DSTLX-1000060221 (WP2), Transformational Medical Technologies program contract W911NF-08-C-0023 from the Department of Defense Chemical and Biological Defense program through the Defense Threat Reduction Agency (DTRA), Thailand research fund (TRF), Commission of Higher Education (CRE) and Mahidol University. MV is a grantee of TRF MRG5480076 and ICTM grant from The Faculty of Tropical Medicine, Mahidol University, Thailand.
This is the author accepted manuscript. The final version is available from Taylor & Francis via the DOI in this record.
Vol. 8 (1), pp. 30 - 40