A novel bactericidal homodimeric PLA2 group-I from Walterinnesia aegyptia venom
2018
Ben Bacha, Abir | Alonazi, Mona Awad | Elshikh, Mohamed Solman | Karray, Aida
A novel non-toxic phospholipase A₂ was purified to homogeneity in a single chromatography step from the venom of Walterinnesia aegyptia, a monotypic elapid snake caught in Saudi Arabia, and its antimicrobial and hemolytic properties were evaluated as well. This enzyme, namely WaPLA₂, is a homodimer with an estimated molecular mass of 30 kDa, and its NH₂-terminal sequence exhibits a significant degree of similarity with PLA₂ group-I. At optimal pH (8.5) and temperature (45 °C), the purified PLA₂ exhibited a specific activity of 2100 U/mg, and it requires bile salts and Ca²⁺ for its activity. However, other cations such as Cd²⁺ and Hg²⁺ diminished the enzyme activity remarkably, thereby suggesting that the catalytic site arrangement has an exclusive structure for Ca²⁺ binding. Furthermore, WaPLA₂ maintained almost 100% and 60% of its full activity in a pH range of 6.0–10 after 24 h incubation or after 60 min treatment at 70 °C, respectively. In the biological activity assays, WaPLA₂ displayed potent indirectly hemolytic and antimicrobial activities that were strongly correlated. These promising findings encourage further in-depth research to understand the molecular mechanism of WaPLA₂'s antimicrobial properties for its possible use as a potential therapeutic lead molecule for treating infections.
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