| Revista: | The journal of venomous animals and toxins including tropical diseases |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000298904 |
| ISSN: | 1678-9199 |
| Autores: | Radis-Baptista, G1 Moreno, F.B.M.B Nogueira, L.L Martins, A.M.C2 Toyama, D.O3 Toyama, M.H4 Azevedo-Junior, W.F5 Cavada, B.S Yamane, T6 |
| Instituciones: | 1Universidade Federal do Ceara, Departamento de Bioquimica e Biologia Molecular, Fortaleza, Ceara. Brasil 2Universidade Federal do Ceara, Departamento de Analises Clinicas e Toxicologicas, Fortaleza, Ceara. Brasil 3Universidade Estadual de Campinas, Departamento de Bioquimica, Campinas, Sao Paulo. Brasil 4Universidade Estadual Paulista "Julio de Mesquita Filho", Departamento de Quimica, Sao Paulo. Brasil 5Universidade Estadual Paulista "Julio de Mesquita Filho", Instituto de Biociencias, Letras e Ciencias Exatas, Sao Paulo. Brasil 6Comissao Nacional de Energia Nuclear, Instituto de Pesquisas Energeticas e Nucleares, Sao Paulo. Brasil |
| Año: | 2005 |
| Periodo: | Dic |
| Volumen: | 11 |
| Número: | 4 |
| Paginación: | 557-578 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental |
| Resumen en inglés | Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins, which are able to interfere with hemostasis. They share significant similarity in their primary structures with C-type lectins of other animals, and also present a conserved carbohydrate recognition domain (CRD). A very well studied sv C-type lectin is the heterodimeric toxin, convulxin (CVX), from the venoms of South American rattlesnakes, Crotalus durissus terrificus and C. d. cascavella. It consists of two subunits, alfa (CVXalpha , 13.9 kDa) and beta (CVXbeta , 12.6 kDa), joined by inter and intra-chain disulfide bounds, and is arranged in a tetrameric alpha4beta4 conformation. Convulxin is able to activate platelet and induce their aggregation by acting via p62/GPVI collagen receptor. Several cDNA precursors, homolog of CVX subunits, were cloned by PCR homology screening. As determined by computational analysis, one of them, named crotacetin beta subunit, was predicted as a polypeptide with a tridimensional conformation very similar to other subunits of convulxin-like snake toxins. Crotacetin was purified from C. durissus venoms by gel permeation and reverse phase high performance liquid chromatography. The heterodimeric crotacetin is expressed in the venoms of several C. durissus subspecies, but it is prevalent in the venom of C. durissus cascavella. As inferred from homology modeling, crotacetin induces platelet aggregation but noticeably exhibits antimicrobial activity against Gram-positive and Gram-negative bacteria |
| Disciplinas: | Biología |
| Palabras clave: | Toxicología, Bioquímica, Veneno de víbora, Lectinas, Agregación plaquetaria, Actividad antimicrobiana, Crotalus durissus, Viperidae |
| Keyword: | Biology, Toxicology, Biochemistry, Snake venom, Lectins, Platelet aggregation, Antimicrobial activity, Crotalus durissus, Viperidae |
| Texto completo: | Texto completo (Ver HTML) |
