Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal ActivitiesReport as inadecuate

Biochemical and Functional Characterization of Parawixia bistriata Spider Venom with Potential Proteolytic and Larvicidal Activities - Download this document for free, or read online. Document in PDF available to download.

BioMed Research International - Volume 2014 2014, Article ID 950538, 13 pages -

Research Article

Centro de Estudos de Biomoléculas Aplicadas a Saúde, CEBio, Fundação Oswaldo Cruz, Fiocruz Rondônia e Departamento de Medicina, Universidade Federal de Rondônia, UNIR, 76812-245 Porto Velho, RO, Brazil

Laboratório de Entomologia Médica, Fundação Oswaldo Cruz, Fiocruz Rondônia e Laboratório de Bioecologia de Insetos, Departamento de Biologia, UNIR, 76812-245 Porto Velho, RO, Brazil

Departamento de Química, Universidades Federal de Lavras, UFLA, 37200-000 Lavras, MG, Brazil

Departamento de Química, Biotecnologia e Engenharia de Bioprocessos, Universidade Federal de São João del Rei, UFSJ, Campus Altoparaopeba, 36420-000 Ouro Branco, MG, Brazil

Received 20 October 2013; Revised 19 February 2014; Accepted 20 February 2014; Published 7 May 2014

Academic Editor: Edward G. Rowan

Copyright © 2014 Gizeli S. Gimenez et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.

Author: Gizeli S. Gimenez, Antonio Coutinho-Neto, Anderson M. Kayano, Rodrigo Simões-Silva, Frances Trindade, Alexandre de Almeida e



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