Abstract
Binary or Bin toxin produced by Lysinibacillus sphaericus is composed of BinA (42 kDa) and BinB (51 kDa) subunits. These work together to exert maximal toxicity against mosquito larvae via pore formation and induction of apoptosis. The C-terminal domains in both subunits are homologous to those of aerolysin-type β pore-forming toxins, including parasporin-2 (PS2). The latter is one of the Bacillus thuringiensis toxins that exhibits specific cytotoxicity against human cancer cells. The present study investigates the possible anticancer activity of Bin toxin using PS2 as a control. We demonstrate that treatment with a high concentration of trypsin-activated Bin inhibits cell proliferation in human cancer cells A549, Caco-2, HepG2, HK-1 and KKU-M055. In the most susceptible cells, HK-1, Bin toxin exposure led to morphological alterations, decreased migration, decreased adhesion activity and apoptosis induction. Although these effects necessitated high concentrations, they suggest that Bin toxin may be optimized as a novel potential cancer-therapeutic agent.