Biochemical and Functional Characterization ofParawixia bistriataSpider Venom with Potential Proteolytic and Larvicidal Activities | Zendy

Gizeli S. Gimenez | Zendy; Antônio Coutinho-Neto | Zendy; Anderson M. Kayano | Zendy; Rodrigo SimõesSilva | Zendy; Frances Tatiane Tavares Trindade | Zendy; Alexandre de Almeida e Silva | Zendy; Silvana Marcussi | Zendy; Saulo L. da Silva | Zendy; Carla Freire Celedônio Fernandes | Zendy; Juliana P. Zuliani | Zendy; Leonardo A. Calderón | Zendy; Andreimar M. Soares | Zendy; Rodrigo G. Stábeli | Zendy

Open Access

Biochemical and Functional Characterization ofParawixia bistriataSpider Venom with Potential Proteolytic and Larvicidal Activities

Author(s) -

Gizeli S. Gimenez,

Antônio Coutinho-Neto,

Anderson M. Kayano,

Rodrigo SimõesSilva,

Frances Tatiane Tavares Trindade,

Alexandre de Almeida e Silva,

Silvana Marcussi,

Saulo L. da Silva,

Carla Freire Celedônio Fernandes,

Juliana P. Zuliani,

Leonardo A. Calderón,

Andreimar M. Soares,

Rodrigo G. Stábeli

Publication year - 2014

Publication title -

biomed research international

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.772

H-Index - 126

eISSN - 2314-6141

pISSN - 2314-6133

DOI - 10.1155/2014/950538

Subject(s) - venom , biochemistry , myotoxin , proteolysis , chemistry , proteolytic enzymes , isoelectric focusing , snake venom , biology , enzyme

Toxins purified from the venom of spiders have high potential to be studied pharmacologically and biochemically. These biomolecules may have biotechnological and therapeutic applications. This study aimed to evaluate the protein content of Parawixia bistriata venom and functionally characterize its proteins that have potential for biotechnological applications. The crude venom showed no phospholipase, hemorrhagic, or anti-Leishmania activities attesting to low genotoxicity and discrete antifungal activity for C. albicans . However the following activities were observed: anticoagulation, edema, myotoxicity and proteolysis on casein, azo-collagen, and fibrinogen. The chromatographic and electrophoretic profiles of the proteins revealed a predominance of acidic, neutral, and polar proteins, highlighting the presence of proteins with high molecular masses. Five fractions were collected using cation exchange chromatography, with the P4 fraction standing out as that of the highest purity. All fractions showed proteolytic activity. The crude venom and fractions P1, P2, and P3 showed larvicidal effects on A. aegypti . Fraction P4 showed the presence of a possible metalloprotease (60 kDa) that has high proteolytic activity on azo-collagen and was inhibited by EDTA. The results presented in this study demonstrate the presence of proteins in the venom of P. bistriata with potential for biotechnological applications.

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