Heterologous Expression and Immunogenic Potential of the Most Abundant Phospholipase A from Coral Snake to Develop Antivenoms.

is a coral snake of clinic interest in Colombia. Its venom is mainly composed of phospholipases A being MdumPLA the most abundant protein. Nevertheless, species produce a low quantity of venom, which makes it difficult to produce anticoral antivenoms. Therefore, in this work, we present the recombinant expression of MdumPLA to evaluate its biological activities and its immunogenic potential to produce antivenoms. For this, a genetic construct rMdumPLA was cloned into the pET28a vector and expressed heterologously in bacteria. His-rMdumPLA was extracted from inclusion bodies, refolded in vitro, and isolated using affinity and RP-HPLC chromatography. His-rMdumPLA was shown to have phospholipase A activity, a weak anticoagulant effect, and induced myonecrosis and edema. The anti-His-rMdumPLA antibodies produced in rabbits recognized native PLA, the complete venom of , and a phospholipase from another species of the genus. Antibodies neutralized 100% of the in vitro phospholipase activity of the recombinant toxin and a moderate percentage of the myotoxic activity of venom in mice. These results indicate that His-rMdumPLA could be used as an immunogen to improve anticoral antivenoms development. This work is the first report of an functional recombinant PLA.