CONICET | Buscador de Institutos y Recursos Humanos

Phospholipase A2 enzyme (PLA2) present in ophidian venoms is able to hydrolyze membrane phospholipids and fatty acid esters, while exhibiting also other activities as indirect hemolysis, edematogenic, myotoxicity, cardiotoxicity, neurotoxicity, anticoagulant and platelet aggregation Paraguay and Brazilian Amazonia are regions where are found ethnomedicine references to the use of Eclipta prostrata (L.) L., as antivenom. Both extracts and isolated wedelolactone, have been reported to inhibit phospholipase A2 activity of Lachesis muta and Calloselasma rhodostoma venoms from Brazil and Thailand respectively. In the present work, the action of different extracts against PLA2 from the main snakes responsable of accidents in the Argentinean northeast, Bothrops diporus, B. alternatus and Crotalus durissus terrificus, was studied to validate this action with autochthonous species. Aerial parts (AP) and roots (R) of native plants collected in Corrientes were dried and ground to prepare by maceration aqueous (1), ethanolic (2) and hexanic (3) extracts. The extracts were dried under vacuum. Inhibition of PLA2 from the different venoms was demonstrated by the in vitro inhibition of indirect hemolytic activity on blood agar plates phosphatidylcholine, incubating the minimal hemolytic doses (doses producing a hemolysis halo of 10 mm after the plates were incubated by 20 hours at 37 °C), the plant extracts and the preincubated venom with the plant extracts 30 minutes at 37ºC in 1:40 ratio (venom: extract). The results showed that both extracts, A2 and R2, were active: A2 inhibited 33% of B. diporus PLA2 activity, 28% of B. alternatus and 31% of Crotalus, while R2 inhibited 31%, 25% and 100% of the activity respectively. The rest of extracts did no show significant activity. The results here found showed the E. prostrata ethanolic root extract as an efficient inhibitor of PLA2 activity present in Crotalus durissus terrificus venom. Thus validating its ethnopharmacological use.