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Isolation and characterization of an anti-leishmanial disintegrin from Cerastes cerastes venom.
Allane, Dihia; Oussedik-Oumehdi, Habiba; Harrat, Zoubir; Seve, Michel; Laraba-Djebari, Fatima.
Afiliación
  • Allane D; USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, Bab Ezzouar, Algiers, 16111, Algeria.
  • Oussedik-Oumehdi H; USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, Bab Ezzouar, Algiers, 16111, Algeria.
  • Harrat Z; Institut Pasteur d'Algérie, Service d'Eco-Epidémiologie Parasitaire, Dely Ibrahim, Algiers 16 047, Algeria.
  • Seve M; CHU Grenoble Alpes, Institut de Biologie et de Pathologie, Promethee Proteomic Platform, Grenoble, France.
  • Laraba-Djebari F; USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, Bab Ezzouar, Algiers, 16111, Algeria.
J Biochem Mol Toxicol ; 32(2)2018 Feb.
Article en En | MEDLINE | ID: mdl-29278277
Investigating new antimicrobial and antiparasitic components from Viperidae venoms represents an alternative therapeutic strategy. In this study, we report the characterization of a disintegrin isolated from Cerastes cerastes venom, exhibiting antiparasitic activity on Leishmania infantum promastigotes. Indeed, isolated disintegrin, referred to Disintegrin_Cc, induced 84.75% of parasiticidal activity and deep morphological alterations on the parasites. SDS-PAGE analysis indicated that this disintegrin was homogenous. This dimeric disintegrin of 14,193.97 Da contains an RGD domain and four intramolecular disulfide bridges. It presents a high percentage of identity with other related snake disintegrins. Predicted 3D structure indicated that this peptide shares partial homology with well-known active antimicrobial peptides. Disintegrin_Cc inhibited 80% of arachidonic acid-induced platelet aggregation. The obtained results suggest that the isolated molecule plays a dual role as a disintegrin and as an anti-leishmanial compound. This component could be useful as a drug in the treatment of leishmaniasis.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Venenos de Víboras / Viperidae / Leishmania infantum / Desintegrinas / Proteínas de Reptiles / Antiparasitarios Límite: Animals Idioma: En Revista: J Biochem Mol Toxicol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / TOXICOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Argelia

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Venenos de Víboras / Viperidae / Leishmania infantum / Desintegrinas / Proteínas de Reptiles / Antiparasitarios Límite: Animals Idioma: En Revista: J Biochem Mol Toxicol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA / TOXICOLOGIA Año: 2018 Tipo del documento: Article País de afiliación: Argelia