期刊
MICROBIOLOGICAL RESEARCH
卷 193, 期 -, 页码 121-131出版社
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.micres.2016.10.003
关键词
Galleria mellonella; Candida albicans; Lysozyme; Apoptosis; Phosphatidylserine externalization; Potassium channels
类别
资金
- European Regional Development Fund under the Operational Programme Innovative Economy, project: 'National Multidisciplinary Laboratory of Functional Nanornaterials'-'NanoFun' [POIG.02.02.00-00-025/09]
The greater wax moth Galleria mellonella has been increasingly used as a model host to determine Candida albicans virulence and efficacy of antifungal treatment. The G. mellonella lysozyme, similarly to its human counterpart, is a member of the c-type family of lysozymes that exhibits antibacterial and anti fungal activity. However, in contrast to the relatively well explained bactericidal action, the mechanism of fungistatic and/or fungicidal activity of lysozymes is still not clear. In the present study we provide the direct evidences that the G. mellonella lysozyme binds to the protoplasts as well as to the intact C. albicans cells and decreases the survival rate of both these forms in a time-dependent manner. No enzymatic activity of the lysozyme towards typical chitinase and P-glucanase substrates was detected, indicating that hydrolysis of main fungal cell wall components is not responsible for anti-Candida activity of the lysozyme. On the other hand, pre-treatment of cells with tetraethylammonium, a potassium channel blacker, prevented them from the lysozyme action, suggesting that lysozyme acts by induction of programmed cell death. In fact, the C. albicans cells treated with the lysozyme exhibited typical apoptotic features, i.e. loss of mitochondrial membrane potential, phosphatidylserine exposure in the outer leaflet of the cell membrane, as well as chromatin condensation and DNA fragmentation. (C) 2016 Elsevier GmbH. All rights reserved.
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