Abstract
The increase in microbial resistance to conventional antimicrobial agents is driving research for the discovery of new antibiotics and antifungal agents. The greatest challenge in this endeavor is to find antimicrobial agents with broad antimicrobial activity and low toxicity. Antimicrobial peptides, for example, RNases, are one of the promising areas. The production of RNases increases during infection, but their role is still being explored. Whereas the enzymatic activity of RNases is well documented, their physiological function is still being investigated. This study aimed to evaluate the antimicrobial activity of RNase 1, 2, 5, and 8 against E. coli strains, S. aureus, Streptococcus thermophilus, P. aeruginosa, Candida albicans, and Candida glabrata. The results demonstrated that RNases have a strain-specific antimicrobial activity. RNase 1 had the highest antimicrobial activity compared to other RNases. All the microorganisms screened had varying levels of susceptibility to RNases, except P. aeruginosa and E. coli DR115. RNase 1 showed dose-dependent activity against C. albicans. The RNase killed Candida albicans by lowering the mitochondrial membrane potential but did not damage the cell membrane. We concluded that strain-specific antimicrobial activity is one of the physiological roles of RNases.
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