Biochemical and biological characterization of a dermonecrotic metalloproteinase isolated from Cerastes cerastes snake venom |
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| Authors: | Amina Ami Habiba Oussedik‐Oumehdi Fatima Laraba‐Djebari |
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| Affiliation: | USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, Bab Ezzouar, Algiers, Algeria |
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| Abstract: | A dermonecrotic metalloproteinase (CcD‐II) was isolated from C. cerastes venom. Venom fractionation was performed using three chromatographic steps (molecular exclusion on Sephadex G‐75, ion‐exchange on DEAE‐Sephadex A‐50, and reversed‐phase high‐performance liquid chromatography on C8 column). CcD‐II presented an apparent molecular mass of 39.9 kDa and displayed a dermonecrotic activity with a minimal necrotic dose of 0.2 mg/kg body weight. CcD‐II showed proteolytic ability on casein chains and on α and β fibrinogen chains that was inhibited by ethylenediamine tetraacetic acid and 1,10‐phenanthroline while remained unaffected by phenylmethylsulphonyl fluoride and heparin. CcD‐II displayed gelatinase activity and degraded extracellular matrix compounds (type‐IV collagen and laminin). These results correlated with histopathological analysis showing a complete disorganization of collagenous skin fibers. These data suggested that CcD‐II belongs to P‐II class of snake venom metalloproteinase. The characterization of venom compounds involved in tissue damage may contribute in the development of new therapeutic strategies in envenomation. |
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| Keywords: | Dermonecrosis extracellular matrix metalloproteinase viper venom |
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