| Literature DB >> 33356857 |
Mieke Van Ende1,2, Bea Timmermans1,2, Giel Vanreppelen1,2, Sofía Siscar-Lewin3, Daniel Fischer3, Stefanie Wijnants1,2, Celia Lobo Romero1,2, Saleh Yazdani1,2, Ona Rogiers1,2,4,5, Liesbeth Demuyser1,2, Griet Van Zeebroeck1,2, Yuke Cen1,2, Karl Kuchler6, Sascha Brunke3, Patrick Van Dijck1,2.
Abstract
Candida glabrata is an opportunistic human fungal pathogen and is frequently present in the human microbiome. It has a high relative resistance to environmental stresses and several antifungal drugs. An important component involved in microbial stress tolerance is trehalose. In this work, we characterized the three C. glabrata trehalase enzymes Ath1, Nth1 and Nth2. Single, double and triple deletion strains were constructed and characterized both in vitro and in vivo to determine the role of these enzymes in virulence. Ath1 was found to be located in the periplasm and was essential for growth on trehalose as sole carbon source, while Nth1 on the other hand was important for oxidative stress resistance, an observation which was consistent by the lower survival rate of the NTH1 deletion strain in human macrophages. No significant phenotype was observed for Nth2. The triple deletion strain was unable to establish a stable colonization of the gastrointestinal (GI) tract in mice indicating the importance of having trehalase activity for colonization in the gut.Entities:
Keywords: Candida glabrata ; colonization; stress; trehalase; trehalose; virulence
Year: 2021 PMID: 33356857 PMCID: PMC7808424 DOI: 10.1080/21505594.2020.1868825
Source DB: PubMed Journal: Virulence ISSN: 2150-5594 Impact factor: 5.882