Anti-Plasmodium properties of group IA, IB, IIA and III secreted phospholipases A2 are serum-dependent.

Abstract Antibacterial, antiparasitidal and antiviral properties have recently been attributed to members of the secreted phospholipases A 2 (sPLA 2 s) superfamily. Seven sPLA 2 s from groups IA, IB, IIA and III, were tested here in different culture conditions for inhibition of the in vitro intraerythrocytic development of Plasmodium falciparum , the causative agent of the most severe form of human malaria. In the presence of human serum, all sPLA 2 s were inhibitory, with three out of seven exhibiting IC 50 2 with the infected erythrocyte, is a general feature of the anti- Plasmodium properties of sPLA 2 s. Furthermore, in serum, six out of the seven sPLA 2 s were toxic against both trophozoite and schizont stages of the parasite development, contrasting with the trophozoite-selective bee venom enzyme's toxicity. Deciphering the molecular mechanisms at play in the phenotypic singularity of the bee venom enzyme toxicity might offer new prospects in antimalarial fight.