Granulin peptide GRN-41 of Mozambique tilapia is a novel antimicrobial peptide against Vibrio species

Abstract

In our previous study, the novel GRN-41 peptide generated from alternative splicing of the Mozambique tilapia PGRN1 gene was identified to be a potent peptide that protected against V. vulnificus in the transgenic zebrafish model by modulating innate immune-related genes. In this study, the anti-bacterial activities of synthetic Mozambique tilapia GRN-41 peptide (OmGRN-41) against various bacterial pathogens were investigated. The results showed that OmGRN-41 had bactericidal activity against Vibrio species, including V. vulnificus, V. alginolyticus, and V. harveyi, but exhibited bacteriostatic activity against V. parahaemolyticus. OmGRN-41 maintained bactericidal activity (64 μM) against V. vulnificus at pH 2 to pH 10 or after heat treatment for 1 h at high temperatures between 40 °C and 100 °C. TEM observations revealed that the outer membrane of V. vulnificus was disrupted by OmGRN-41, leading to morphological rupture and loss of cytoplasmic contents. Additionally, little hemolytic activity against tilapia and sheep erythrocytes was detected after treatment with 128 μM OmGRN-41. OmGRN-41 can effectively enhance the survival of Nile tilapia infected by V. vulnificus. Our results suggest that the OmGRN-41 is a novel antimicrobial peptide possessing bactericidal activity, especially against Vibrio species. These results indicate that OmGRN-41 can be applied in human Vibriosis treatment and has the potential to defend against Vibrio spp. infection in critical aquaculture organisms.

Keywords: Antimicrobial peptide; Bactericidal; Bacteriostatic; Granulin; Tilapia; Vibrio.