Abstract
Mucuna pruriens seeds have been widely used against snakebite in traditional medicine. The antivenin property of a water extract of seeds was assessed in vivo in mice. The serum of mice treated with extract was tested for its immunological properties. Two proteins of Echis carinatus venom with apparent molecular masses of 25 and 16 kDa were detected by Western blot analysis carried out using IgG of mice immunized with extract or its partially purified protein fractions. By enzymatic in-gel digestion and electrospray ionization-mass spectrometry/mass spectrometry analysis of immunoreactive venom proteins, phospholipase A(2,) the most toxic enzyme of snake venom, was identified. These results demonstrate that the observed antivenin activity has an immune mechanism. Antibodies of mice treated with non-lethal doses of venom reacted against some proteins of M. pruriens extract. Proteins of E. carinatus venom and M. pruriens extract have at least one epitope in common as confirmed by immunodiffusion assay.
Highlights
Mucuna pruriens seeds have been widely used against snakebite in traditional medicine
Two proteins of Echis carinatus venom with apparent molecular masses of 25 and 16 kDa were detected by Western blot analysis carried out using IgG of mice immunized with extract or its partially purified protein fractions
In preliminary experiments [3, 4] we demonstrated that extract of M. pruriens (MPE),1 a medicinal plant widely used in Nigeria for its chemical and pharmacological properties, protects mice against the lethal effect of Echis carinatus venom
Summary
Mucuna pruriens seeds have been widely used against snakebite in traditional medicine. By enzymatic in-gel digestion and electrospray ionization-mass spectrometry/mass spectrometry analysis of immunoreactive venom proteins, phospholipase A2, the most toxic enzyme of snake venom, was identified These results demonstrate that the observed antivenin activity has an immune mechanism. In preliminary experiments [3, 4] we demonstrated that extract of M. pruriens (MPE), a medicinal plant widely used in Nigeria for its chemical and pharmacological properties, protects mice against the lethal effect of Echis carinatus venom (EV). Both MPE and EV are heterogeneous mixtures, their interaction represents a complex phenomenon, and there is no information about its biochemical mechanism. The aim of the present study was to study the mechanism, the factors of MPE, and the proteins of EV involved in the observed phenomenon
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