Separation and biological activities of phospholipase A2 (Mb-PLA2) from the venom of montivipera bornmuelleri, a lebanese viper

Phospholipase A2 (PLA2), a common toxic component of snake venom, is responsible for a wide spectrum of biological and toxicological effects including bactericidal, anticoagulant, hemolytic, as well as neurotoxic and cardiotoxicity activities. In the present work, phospholipase A2 named (Mb-PLA2) was isolated from the venom of Montivipera bornmuelleri a Lebanese snake, by a two-step procedure consisting of gel filtration chromatography on Biogel P60 and reverse phase high pressure liquid chromatography (RP-HPLC) on a Restek Ultra II C18 column. The experimentally determined molecular weight of the Mb-PLA2 was 13650 Da, which was determined by electrospray ionization mass spectrometry and close to 14400 Da as judged by SDS-PAGE electrophoresis. The isolated Mb-PLA2 was evaluated for bactericidal activity against Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Mb-PLA2 showed strong antibacterial activity against the Gram positive bacteria S. aureus, followed by the Gram negative bacteria, E. coli, and then P. aeruginosa. Moreover, the Mb-PLA2 exhibited hemolytic activity toward human erythrocyte, as well as an anticoagulant activity when evaluated on human plasma.