Abstract：
: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 antifungal 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 β-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 blocker, 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.
journal_name
Microbiol Resjournal_title
Microbiological researchauthors
Sowa-Jasiłek A,Zdybicka-Barabas A,Stączek S,Wydrych J,Skrzypiec K,Mak P,Deryło K,Tchórzewski M,Cytryńska Mdoi
10.1016/j.micres.2016.10.003subject
Has Abstractpub_date
2016-12-01 00:00:00pages
121-131eissn
0944-5013issn
1618-0623pii
S0944-5013(16)30079-9journal_volume
193pub_type
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