Proteins from Mucuna pruriens and enzymes from Echis carinatus venom: characterization and cross-reactions.
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.
Guerranti
Roberto
R
Institute of Biochemistry and Enzymology, University of Siena, Via A. Moro 2, 53100 Siena, Italy.
Aguiyi
John C
JC
Neri
Stefano
S
Leoncini
Roberto
R
Pagani
Roberto
R
Marinello
Enrico
E
D000818:Animals; D000997:Antivenins / Q000494:pharmacology*; D015153:Blotting, Western; D002850:Chromatography, Gel; D004058:Diffusion; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes; D005779:Immunodiffusion; D007074:Immunoglobulin G / Q000378:metabolism; D007700:Kinetics; D013058:Mass Spectrometry; D051379:Mice; D010741:Phospholipases A / Q000737:chemistry*; D010936:Plant Extracts / Q000494:pharmacology*; D019685:Rosales / Q000737:chemistry*; D012910:Snake Venoms / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization; D013696:Temperature
D000997:Antivenins; D000939:Epitopes; D007074:Immunoglobulin G; D010936:Plant Extracts; D012910:Snake Venoms; D010741:Phospholipases A