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dc.creatorFernández Ulate, Julián
dc.creatorAlape Girón, Alberto
dc.creatorAngulo Ugalde, Yamileth
dc.creatorSanz, Libia
dc.creatorGutiérrez, José María
dc.creatorCalvete Chornet, Juan José
dc.creatorLomonte, Bruno
dc.date.accessioned2017-01-18T20:51:44Z
dc.date.available2017-01-18T20:51:44Z
dc.date.issued2011-01-31
dc.identifier.citationhttp://pubs.acs.org/doi/abs/10.1021/pr101091aes_ES
dc.identifier.issn1535-3907
dc.identifier.urihttp://hdl.handle.net/10669/29439
dc.descriptionEmbargo por política editorial 2081-01-21es_ES
dc.description.abstractThe proteome of the venom of Micrurus nigrocinctus (Central American coral snake) was analyzed by a “venomics” approach. Nearly 50 venom peaks were resolved by RP-HPLC, revealing a complex protein composition. Comparative analyses of venoms from individual specimens revealed that such complexity is an intrinsic feature of this species, rather than the sum of variable individual patterns of simpler composition. Proteins related to eight distinct families were identified by MS/MS de novo peptide sequencing or N-terminal sequencing: phospholipase A2 (PLA2), three-finger toxin (3FTx), l-amino acid oxidase, C-type lectin/lectin-like, metalloproteinase, serine proteinase, ohanin, and nucleotidase. PLA2s and 3FTxs are predominant, representing 48 and 38% of the venom proteins, respectively. Within 3FTxs, several isoforms of short-chain α-neurotoxins as well as muscarinic-like toxins and proteins with similarity to long-chain κ-2 bungarotoxin were identified. PLA2s are also highly diverse, and a toxicity screening showed that they mainly exert myotoxicity, although some are lethal and may contribute to the known presynaptic neurotoxicity of this venom. An antivenomic characterization of a therapeutic monospecific M. nigrocinctus equine antivenom revealed differences in immunorecognition of venom proteins that correlate with their molecular mass, with the weakest recognition observed toward 3FTxs.es_ES
dc.description.sponsorshipConsejo Nacional de Rectores/[2009CR0021]/CONARE/Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-A7-611]/UCR/Costa Ricaes_ES
dc.description.sponsorshipMinisterio de Innovaci on y Ciencia/[BFU2007-61563]//Españaes_ES
dc.description.sponsorshipMinisterio de Innovaci on y Ciencia/[BFU2010-17373]//Españaes_ES
dc.description.sponsorshipGeneralitat Valenciana/[PROMETEO/2010/005]//Españaes_ES
dc.description.sponsorshipPrograma Iberoamericano de Ciencia y Tecnología para el Desarrollo/[206AC0281]/CYTED/Españaes_ES
dc.description.sponsorshipConsejo Superior de Investigaciones Cienctíficas /[2009CR0021]/CRUSA-CSIC/Españaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteome Research; Volumen 10, Número 4. 2011es_ES
dc.subjectAntivenomicses_ES
dc.subjectCoral Snakees_ES
dc.subjectElapid toxinses_ES
dc.subjectMass spectrometryes_ES
dc.subjectMicrurus nigrocinctuses_ES
dc.subjectProteomicses_ES
dc.subjectvenomicses_ES
dc.subjectSnake venomes_ES
dc.titleVenomic and antivenomic analyses of the Central American coral snake, Micrurus nigrocinctus (Elapidae)es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1021/pr101091a
dc.identifier.doi741-A7-611
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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