Role of membrane sterol and redox system in the anti-candida activity reported for Mo-CBP2, a protein from Moringa oleifera seeds

Abstract

Plant proteins are emerging as an alternative to conventional treatments against candidiasis. The aim of this study was to better understand the mechanism of action of Mo-CBP₂ against Candida spp, evaluating redox system activity, lipid peroxidation, DNA degradation, cytochrome c release, medium acidification, and membrane interaction. Anti-candida activity of Mo-CBP₂ decreased in the presence of ergosterol, which was not observed with antioxidant agents. C. albicans treated with Mo-CBP₂ also had catalase and peroxidase activities inhibited, while superoxide dismutase was increased. Mo-CBP₂ increased the lipid peroxidation, but it did not alter the ergosterol profile in live cells. External medium acidification was strongly inhibited, and cytochrome c release and DNA degradation were detected. Mo-CBP₂ interacts with cell membrane constituents, changes redox system enzymes in C. albicans and causes lipid peroxidation by ROS overproduction. DNA degradation and cytochrome c release suggest apoptotic or DNAse activity. Lipid peroxidation and H⁺-ATPases inhibition may induce the process of apoptosis. Finally, Mo-CBP₂ did not have a cytotoxic effect in mammalian Vero cells. This study highlights the biotechnological potential of Mo-CBP₂ as a promising molecule with low toxicity and potent activity. Further studies should be performed to better understand its mode of action and toxicity.