Recombinant scorpine: a multifunctional antimicrobial peptide with activity against different pathogens
2008
Carballar-Lejarazú, R | Rodríguez, M. H | de la Cruz Hernández-Hernández, F | Ramos-Castañeda, J | Possani, L. D | Zurita-Ortega, M | Reynaud-Garza, E | Hernández-Rivas, R | Loukeris, T | Lycett, G | Lanz-Mendoza, H
Scorpine is an antimicrobial peptide whose structure resembles a hybrid between a defensin and a cecropin. It exhibits antibacterial activity and inhibits the sporogonic development of parasites responsible for murine malaria. In this communication we report the production of scorpine in a heterelogous system, using a specific vector containing its cloned gene. The recombinantly expressed scorpine (RScp) in Anopheles gambie cells showed antibacterial activity against Bacillus subtilis and Klebsiella pneumoniae, at 5 and 10 μM, respectively. It also produced 98% mortality in sexual stages of Plasmodium berghei at 15 μM and 100% reduction in Plasmodium falciparum parasitemia at 5 μM. RScp also inhibited virus dengue-2 replication in C6/36 mosquito cells. In addition, we generated viable and fertile transgenic Drosophila that overexpresses and correctly secretes RScp into the insect hemolymph, suggesting that the generation of transgenic mosquitoes resistant to different pathogens may be viable.
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