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dc.creatorLomonte, Bruno
dc.creatorEscolano, José
dc.creatorFernández Ulate, Julián
dc.creatorSanz, Libia
dc.creatorAngulo Ugalde, Yamileth
dc.creatorGutiérrez, José María
dc.creatorCalvete Chornet, Juan José
dc.date.accessioned2016-11-22T15:17:09Z
dc.date.available2016-11-22T15:17:09Z
dc.date.issued2008-04-30
dc.identifier.citationhttp://pubs.acs.org/doi/abs/10.1021/pr8000139es_ES
dc.identifier.issn1535-3907
dc.identifier.urihttp://hdl.handle.net/10669/29312
dc.description.abstractWe report the comparative proteomic characterization of the venoms of two related neotropical arboreal pitvipers from Costa Rica of the genus Bothriechis, B. lateralis (side-striped palm pit viper) and B. schlegelii (eyelash pit viper). The crude venoms were fractionated by reverse-phase HPLC, followed by analysis of each chromatographic fraction by SDS-PAGE, N-terminal sequencing, MALDI-TOF mass fingerprinting, and collision-induced dissociation tandem mass spectrometry of tryptic peptides. The venom proteomes of B. lateralis and B. schlegelii comprise similar number of distinct proteins belonging, respectively, to 8 and 7 protein families. The two Bothriechis venoms contain bradykinin-potentiating peptides (BPPs), and proteins from the phospholipase A2 (PLA2), serine proteinase, l-amino acid oxidase (LAO), cysteine-rich secretory protein (CRISP), and Zn2+-dependent metalloproteinase (SVMP) families, albeit each species exhibit different relative abundances. Each venom also contains unique components, for example, snake venom vascular endothelial growth factor (svVEGF) and C-type lectin-like molecules in B. lateralis, and Kazal-type serine proteinase inhibitor-like proteins in B. schlegelii. Using a similarity coefficient, we estimate that the similarity of the venom proteins between the two Bothriechis taxa may be <10%, indicating a high divergence in their venom compositions, in spite of the fact that both species have evolved to adapt to arboreal habits. The major toxin families of B. lateralis and B. schlegelii are SVMP (55% of the total venom proteins) and PLA2 (44%), respectively. Their different venom toxin compositions provide clues for rationalizing the distinct signs of envenomation caused by B. schlegelii and B. lateralis. An antivenomic study of the immunoreactivity of the Instituto Clodomiro Picado (ICP) polyvalent antivenom toward Bothriechis venoms revealed that l-amino acid oxidase and SVMPs represent the major antigenic protein species in both venoms. Our results provide a ground for rationalizing the reported protection of the ICP polyvalent antivenom against the hemorrhagic, coagulant, defibrinating, caseinolytic and fibrin(ogen)olytic activities of Bothriechis (schlegelii, lateralis) venoms. However, these analyses also evidenced the limited recognition capability of the polyvalent antivenom toward a number of Bothriechis venom components, predominantly BPPs, svVEGF, Kazal-type inhibitors, some PLA2 proteins, some serine proteinases, and CRISP molecules.es_ES
dc.description.sponsorshipinfo:eu-repo//Ministerio de Educación y Ciencia// BFU2004-01432/BMC/ [Madrid, España]//es_ES
dc.description.sponsorshipinfo:eu-repo//Universidad de Costa Rica-CSIC//2006CR0010/[Costa Rica]//es_ES
dc.description.sponsorshipinfo:eu-repo//Ciencia y tecnología para el Desarrollo (CYTED)//206AC0281/[España]//es_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteome Research; Volumen 7, Número 6. 2008es_ES
dc.subjectAntivenomicses_ES
dc.subjectBothriechis Lateralises_ES
dc.subjectBothriechis Schlegeliies_ES
dc.subjectEyelash Pit Viperes_ES
dc.subjectKazal-type Inhibitores_ES
dc.subjectMass spectrometryes_ES
dc.subjectN-terminal Sequencinges_ES
dc.subjectPolyvalent (Crotalinae) Antivenomes_ES
dc.subjectProteomicses_ES
dc.subjectSide-striped Palm Pit viperes_ES
dc.subjectSnake venom protein familieses_ES
dc.subjectSnake venomicses_ES
dc.subjectViperid toxinses_ES
dc.titleSnake Venomics and Antivenomics of the Arboreal Neotropical Pitvipers Bothriechis lateralis and Bothriechis schlegeliies_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1021/pr8000139
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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