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Originally published In Press as doi:10.1074/jbc.M201387200 on February 26, 2002

J. Biol. Chem., Vol. 277, Issue 19, 17072-17078, May 10, 2002
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Proteins from Mucuna pruriens and Enzymes from Echis carinatus Venom
CHARACTERIZATION AND CROSS-REACTIONS*

Roberto GuerrantiDagger , John C. Aguiyi§, Stefano NeriDagger , Roberto LeonciniDagger , Roberto PaganiDagger , and Enrico MarinelloDagger

From the Dagger  Institute of Biochemistry and Enzymology, University of Siena, Via A. Moro 2, 53100 Siena, Italy and the § Department of Pharmacology, University of Jos, P. M. B. 2084 Jos, Nigeria

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 A2, 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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 39-577-234286; Fax: 39-577-234285; E-mail: marinello@unisi.it.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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