Snake venoms are composed of a complex mixture of active proteins and peptides which induce a wide range of toxic effects. Envenomation by Bothrops jararaca venom results in hemorrhage, edema, pain, tissue necrosis and hemolysis. In this work, the effect of a mixture of two secodolastane diterpenes (linearol/isolinearol), previously isolated from the Brazilian marine brown alga, Canistrocarpus cervicornis, was evaluated against some of the toxic effects induced by B. jararaca venom. The mixture of diterpenes was dissolved in dimethylsulfoxide and incubated with venom for 30 min at room temperature, and then several in vivo (hemorrhage, edema and lethality) and in vitro (hemolysis, plasma clotting and proteolysis) assays were performed. The diterpenes inhibited hemolysis, proteolysis and hemorrhage, but failed to inhibit clotting and edema induced by B. jararaca venom. Moreover, diterpenes partially protected mice from lethality caused by B. jararaca venom. The search for natural inhibitors of B. jararaca venom in C. cervicornis algae is a relevant subject, since seaweeds are a rich and powerful source of active molecules which are as yet but poorly explored. Our results suggest that these diterpenes have the potential to be used against Bothropic envenomation accidents or to improve traditional treatments for snake bites.
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http://dx.doi.org/10.3390/molecules20033515 | DOI Listing |
J Proteome Res
January 2025
Departamento de Bioquímica, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo 04023-901, Brazil.
Antivenoms are the only effective treatment for snakebite envenomation and have saved countless lives over more than a century. Despite their value, antivenoms present risks of adverse reactions. Current formulations contain a fraction of nonspecific antibodies and serum proteins.
View Article and Find Full Text PDFToxicon
January 2025
Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brazil; Programa de Pós-Graduação Interunidades em Biotecnologia, São Paulo, Brazil; Laboratório de Fisiopatologia, Instituto Butantan, São Paulo, Brazil. Electronic address:
Coagulation disorders are a primary symptom of envenomation caused by snakes belonging to the genus Bothrops. In the Northeast region of Brazil, the species Bothrops erythromelas and Bothrops leucurus are the main responsible for snakebite accidents. Due to the specific action of Bothrops venoms on several components of the coagulation cascade, the objective of this work was to characterize the coagulotoxic profile of B.
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December 2024
Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina.
Inoculation of Bothrops jararaca snake venom (BjV) induces thrombocytopenia in humans and various animal species. Although several BjV toxins acting on hemostasis have been well characterized in vitro, it is not known which one is responsible for inducing thrombocytopenia in vivo. In previous studies, we showed that BjV incubated with metalloproteinase or serine proteinase inhibitors and/or anti-botrocetin antibodies still induced thrombocytopenia in rats and mice.
View Article and Find Full Text PDFToxins (Basel)
December 2024
Immunopathology Laboratory, Butantan Institute, São Paulo 05585-090, Brazil.
Jararhagin-C (JarC) is a protein from the venom of consisting of disintegrin-like and cysteine-rich domains. JarC shows a modulating effect on angiogenesis and remodeling of extracellular matrix constituents, improving wound healing in a mouse experimental model. JarC is purified from crude venom, and the yield is less than 1%.
View Article and Find Full Text PDFToxins (Basel)
November 2024
Facultad de Ciencias Exactas y Naturales, Pontificia Universidad Católica del Ecuador, Quito 170525, Ecuador.
Previous proteomic studies of viperid venom revealed that it is mainly composed of metalloproteinases (SVMPs), serine proteinases (SVSPs), phospholipase A2 (PLA2), and C-type lectins (CTLs). However, other proteins appear in minor amounts that affect prey and need to be identified. This study aimed to identify novel toxic proteins in the venom gland transcriptome of and , using data from NCBI.
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