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dc.creatorLomonte, Bruno
dc.creatorDíaz Oreiro, Cecilia
dc.creatorChaves Mora, Fernando
dc.creatorFernández Ulate, Julián
dc.creatorRuiz, Marco
dc.creatorSalas, María
dc.creatorZavaleta Martínez Vargas, Alfonso
dc.creatorCalvete Chornet, Juan José
dc.creatorSasa Marín, Mahmood
dc.date.accessioned2021-03-15T19:24:09Z
dc.date.available2021-03-15T19:24:09Z
dc.date.issued2020
dc.identifier.citationhttps://www.sciencedirect.com/science/article/pii/S2590171020300229?via%3Dihub
dc.identifier.issn2590-1710
dc.identifier.urihttps://hdl.handle.net/10669/83057
dc.description.abstractSnake species within the Bothrops complex (sensu lato) are of medical relevance in Latin America, but knowledge on their venom characteristics is limited, or even unavailable, for some taxa. Perú harbors 17 species of pit vipers, within the genera Bothrops, Bothriechis, Bothrocophias, Porthidium, Crotalus, and Lachesis. This study compared the venoms of twelve species, through chromatographic and electrophoretic profiles, as well as proteolytic and phospholipase A2 (PLA2) activities. Also, proteomic profiles were analyzed for nine of the venoms using a shotgun approach. Results unveiled conspicuous differences in the expression of venom PLA2s among species, six of them presenting scarce levels as judged by RP-HPLC profiles. Since most species within the bothropoid lineage possess venoms with high to intermediate abundances of this protein family, our findings suggest the existence of a phenotypic duality in the expression of venom PLA2s within the Bothrops (sensu lato) complex. Bothrops barnetti and Bothrocophias andianus venoms, very scarce in PLA2s, were shown to lack significant myotoxic activity, highlighting that the observed variability in PLA2 expression bears toxicological correlations with effects attributed to these proteins. Finally, an attempt to identify phylogenetic relationships of bothropoid species from Perú presenting low- or high-PLA2 venom phenotypes showed an interspersed pattern, thus precluding a simple phylogenetic interpretation of this venom compositional dichotomy.es_ES
dc.language.isoenges_ES
dc.sourceToxicon-X 7 (2020), 100044es_ES
dc.subjectsnake venomes_ES
dc.subjectPerues_ES
dc.subjectViperidaees_ES
dc.subjectphospholipase A2es_ES
dc.titleComparative biochemical characterization of Viperidae snake venoms from Perú reveals two compositional patterns of phospholipase A2 expressiones_ES
dc.typeartículo científico
dc.identifier.doi10.1016/j.toxcx.2020.100044
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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