Journal of biochemical and molecular toxicology · 2017
Isolation and characterization of an anti-leishmanial disintegrin from Cerastes cerastes venom.
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Allane Dihia, Oussedik-Oumehdi Habiba, Harrat Zoubir, Seve Michel, Laraba-Djebari Fatima
Аннотация
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.
Предметные рубрики MeSH
Amino Acid SequenceAnimalsAntiparasitic AgentsCell SurvivalComputational BiologyConserved SequenceDimerizationDisintegrinsExpert SystemsGene OntologyLeishmania infantumMolecular WeightPhylogenyPlatelet AggregationPlatelet Aggregation InhibitorsProtein ConformationProtein Interaction Domains and MotifsReptilian ProteinsSequence AlignmentSequence Homology, Amino AcidViper VenomsViperidae