Cell Mol Life Sci. 2008 Oct;65(19):3081-92.

Recombinant scorpine: a multifunctional antimicrobial peptide with activity against different pathogens.

Carballar-Lejarazú R, Rodríguez MH, de la Cruz Hernández-Hernández F, Ramos-Castañeda J, Possani LD, Zurita-Ortega M, Reynaud-Garza E, Hernández-Rivas R, Loukeris T, Lycett G, Lanz-Mendoza H.

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Centro de Investigaciones sobre Enfermedades Infecciosas, Instituto Nacional de Salud Pública, Av. Universidad 655. Sta. María Ahuacatitlán, Cuernavaca, Morelos, México, CP 62100.

Abstract

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 microM, respectively. It also produced 98% mortality in sexual stages of (Plasmodium berghei) at 15 microM and 100% reduction in (Plasmodium falciparum) parasitemia at 5 microM. 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.

PMID:: 18726072; [PubMed - indexed for MEDLINE]

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