Basic phospholipase A2 homolog myotoxin II (MjTX-II) (MjTX-II)

Basic phospholipase A2 homolog myotoxin II (MjTX-II) is a non-catalytic protein isolated from the venom of the lance-headed viper Bothrops moojeni [1]. It belongs to the Lys49-PLA2 family, which lacks the enzymatic activity of typical phospholipases but retains potent myotoxic and neurotoxic properties [1, 2]. MjTX-II functions by binding to and physically disrupting host cell membranes through a two-site mechanism involving electrostatic docking and hydrophobic insertion, leading to pore formation and cell death [2, 3]. In the context of envenomation, it is a primary driver of local tissue necrosis and is often resistant to traditional antivenom treatments [3]. Beyond its toxicological role, MjTX-II is being explored as a therapeutic lead for cancer and parasitic infections like toxoplasmosis due to its ability to induce apoptosis and modulate VEGF and ROS pathways [5, 6]. Small-molecule inhibitors such as varespladib and suramin are currently being studied for their ability to neutralize MjTX-II and mitigate the severe clinical outcomes of snakebites [3, 4].

Other names

Myotoxin-IIMjTX-IIBasic phospholipase A2 homolog 2M-VILys49-PLA2 from Bothrops moojeni

Inhibition of the toxin's membrane-disrupting and membrane-docking sites, preventing pore formation and subsequent cell necrosis.