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dc.creatorAngulo Ugalde, Yamileth
dc.creatorEscolano, José
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorSanz, Libia
dc.creatorCalvete Chornet, Juan José
dc.date.accessioned2016-11-18T20:26:13Z
dc.date.available2016-11-18T20:26:13Z
dc.date.issued2008
dc.identifier.citationhttp://pubs.acs.org/doi/abs/10.1021%2Fpr700610zes_ES
dc.identifier.issn1535-3907
dc.identifier.urihttp://hdl.handle.net/10669/29262
dc.description.abstractWe report the proteomic characterization of the Central American pitvipers Atropoides nummifer and Atropoides picadoi. The crude venoms were fractionated by reverse-phase high-performance liquid chromatography (HPLC), followed by analysis of each chromatographic fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), N-terminal sequencing, matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass fingerprinting, and collision-induced dissociation-tandem mass spectrometry (CID-MS/MS) of tryptic peptides. Each venom contained a number of bradykinin-potentiating peptides and around 25–27 proteins of molecular masses in the range of 7–112 kDa, belonging to only nine different toxin families (disintegrin, DC fragment, snake venom vascular endothelial growth factor, phospholipases A2, serine protease, cysteine-rich secretory proteins, C-type lectins, L-amino acid oxidase, and Zn2+-dependent metalloproteases), albeit distinctly distributed among the two Atropoides species. In addition, A. nummifer expresses low amounts of a three-finger toxin not detected in the venom of A. picadoi. The major toxins of A. nummifer belong to the PLA2 (relative abundance, 36.5%) and the serine proteinase (22%) families, whereas the most abundant A. picadoi toxins are Zn2+-dependent metalloproteinases (66.4%). We estimate that the similarity of venom proteins between the two Atropoides taxa may be around 14–16%. The high degree of differentiation in the venom proteome among congeneric taxa emphasizes unique aspects of venom composition of related species of Atropoides snakes and points to a strong role for adaptive diversification via natural selection as a cause of this distinctiveness. On the other hand, their distinct venom toxin compositions provide clues for rationalizing the low hemorrhagic, coagulant, and defibrinating activities and the high myotoxic and proteolytic effects evoked by A. nummifer snakebite in comparison to other crotaline snake venoms and the high hemorrhagic activity of A. picadoi.es_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteome Research; Volumen 7, Número 2. 2008es_ES
dc.subjectAtropoides Mexicanuses_ES
dc.subjectAtropoides Nummiferes_ES
dc.subjectAtropoides Picadoies_ES
dc.subjectBitis Caudalises_ES
dc.subjectJumping Pitviperes_ES
dc.subjectPicadoi’s Pitviperes_ES
dc.subjectSnake venom protein familieses_ES
dc.subjectProteomicses_ES
dc.subjectViperid toxinses_ES
dc.subjectN-terminal Sequencinges_ES
dc.subjectMass spectrometryes_ES
dc.subjectThree-finger Toxines_ES
dc.subjectSnake venomes_ES
dc.titleSnake Venomics of Central American Pitvipers: Clues for Rationalizing the Distinct Envenomation Profiles of Atropoides nummifer and Atropoides picadoies_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1021/pr700610z
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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