| Autor: |
Wanderley LF; Laboratório de Bioquímica Vegetal, Programa de Engenharia Química, Centro de Ciências Exatas e Tecnológica, Universidade Federal do Maranhão - UFMA, São Luís, MA, Brasil., Soares AMDS; Laboratório de Bioquímica Vegetal, Programa de Engenharia Química, Centro de Ciências Exatas e Tecnológica, Universidade Federal do Maranhão - UFMA, São Luís, MA, Brasil., Silva CRE; Laboratório de Controle de Parasitos, Departamento de Patologia, Centro de Ciências Biológicas e da Saúde, Universidade Federal do Maranhão - UFMA, São Luís, MA, Brasil., Figueiredo IM; Laboratório de Bioquímica Vegetal, Programa de Engenharia Química, Centro de Ciências Exatas e Tecnológica, Universidade Federal do Maranhão - UFMA, São Luís, MA, Brasil., Ferreira ATDS; Laboratório de Toxinologia, Fundação Oswaldo Cruz - FIOCRUZ, Rio de Janeiro, RJ, Brasil., Perales J; Laboratório de Toxinologia, Fundação Oswaldo Cruz - FIOCRUZ, Rio de Janeiro, RJ, Brasil., Mota HRO; Laboratório de Proteínas de Defesa Vegetal, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará - UFCE, Fortaleza, CE, Brasil., Oliveira JTA; Laboratório de Proteínas de Defesa Vegetal, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará - UFCE, Fortaleza, CE, Brasil., Costa Junior LM; Laboratório de Controle de Parasitos, Departamento de Patologia, Centro de Ciências Biológicas e da Saúde, Universidade Federal do Maranhão - UFMA, São Luís, MA, Brasil. |
| Abstrakt: |
Haemonchus contortus is a gastrointestinal nematode that is responsible for high mortality rates in ruminant herds. The resistance of nematodes to synthetic anthelmintics is widespread and requires a continuous search for new bioactive molecules, such as proteins. The objective of this study was to evaluate the anthelmintic potential of a protease purified from the latex of Ficus benjamina against H. contortus . Fresh latex was collected from plants via small incisions in the green stems, the rubber was removed by centrifugation, and the latex protein extract (LPE) was obtained. After LPE fractionation with ammonium sulfate and chromatography of the fraction containing the highest proteolytic activity on CM-cellulose, a cysteine protease (FbP) was purified. FbP has a molecular mass of approximately 23.97 kDa, and its proteolytic activity was stable between pH 6.0 and pH 10 and over a broad temperature range, with optimum activity at 60 °C. FbP inhibited both the development and exsheathment of H. contortus larvae, with 50% effective concentrations of 0.26 and 0.79 mg/mL, respectively. We conclude that this cysteine protease from F. benjamina latex with anthelmintic activity against H. contortus could be a promising alternative for the development of products for use in parasite control programmes. |
