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dc.creatorCalvete Chornet, Juan José
dc.creatorBorges, Adolfo
dc.creatorSegura Ruiz, Álvaro
dc.creatorFlores Díaz, Marietta
dc.creatorAlape Girón, Alberto
dc.creatorGutiérrez, José María
dc.creatorDiez, Nardy
dc.creatorDe Sousa, Leonardo
dc.creatorKiriakos, Demetrio
dc.creatorSánchez, Eladio
dc.creatorFaks, José G.
dc.creatorEscolano, José
dc.creatorSanz, Libia
dc.date.accessioned2016-11-16T20:59:09Z
dc.date.available2016-11-16T20:59:09Z
dc.date.issued2009-03-06
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S187439190900013X
dc.identifier.issn1874-3919
dc.identifier.urihttps://hdl.handle.net/10669/29260
dc.description.abstractThe taxonomic status of the medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela, which has been classified as Bothrops colombiensis, remains incertae cedis. To help resolving this question, the venom proteome of B. colombiensis was characterized by reverse-phase HPLC fractionation 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 contained proteins belonging to 8 types of families. PI Zn2+-metalloproteinases and K49 PLA2 molecules comprise over 65% of the venom proteins. Other venom protein families comprised PIII Zn2+-metalloproteinases (11.3%), D49 PLA2s (10.2%), l-amino acid oxidase (5.7%), the medium-sized disintegrin colombistatin (5.6%), serine proteinases (1%), bradykinin-potentiating peptides (0.8%), a DC-fragment (0.5%), and a CRISP protein (0.1%). A comparison of the venom proteomes of B. colombiensis and B. atrox did not support the suggested synonymy between these two species. The closest homologues to B. colombiensis venom proteins appeared to be toxins from B. asper. A rough estimation of the similarity between the venoms of B. colombiensis and B. asper indicated that these species share approximately 65–70% of their venom proteomes. The close kinship of B. colombiensis and B. asper points at the ancestor of B. colombiensis as the founding Central American B. asper ancestor. This finding may be relevant for reconstructing the natural history and cladogenesis of Bothrops. Further, the virtually indistinguishable immunological crossreactivity of a Venezuelan ABC antiserum (raised against a mixture of B. colombiensis and Crotalus durissus cumanensis venoms) and the Costa Rican ICP polyvalent antivenom (generated against a mixture of B. asper, Crotalus simus, and Lachesis stenophrys venoms) towards the venoms of B. colombiensis and B. asper, supports this view and suggests the possibility of indistinctly using these antivenoms for the management of snakebites by any of these Bothrops species. However, our analyses also evidenced the limited recognition capability or avidity of these antivenoms towards a number of B. colombiensis and B. asper venom components, most notably medium-size disintegrins, bradykinin-potentiating peptides, PLA2 proteins, and PI Zn2+-metalloproteinases.es_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteomics; Volumen 72, Número 2. 2009es_ES
dc.subjectSnake venomicses_ES
dc.subjectBothrops colombiensises_ES
dc.subjectSnake venom protein familieses_ES
dc.subjectProteomicses_ES
dc.subjectViperid toxinses_ES
dc.subjectN-terminal Sequencinges_ES
dc.subjectMass spectrometryes_ES
dc.subjectAntivenomicses_ES
dc.subjectAntibothropic and anticrotalic ABC antivenomes_ES
dc.subjectPolyvalent (Crotalinae) ICP antivenomes_ES
dc.subjectSnake venomes_ES
dc.titleSnake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite managementes_ES
dc.typeartículo original
dc.identifier.doi10.1016/j.jprot.2009.01.005
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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