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dc.creatorSanz, Libia
dc.creatorQuesada Bernat, Sarai
dc.creatorPérez, Alicia
dc.creatorde Morais Zani, Karen
dc.creatorSantˈAnna, Sávio S.
dc.creatorHatakeyama, Daniela M.
dc.creatorTasima, Lidia J.
dc.creatorde Souza, Moisés B.
dc.creatorKayano, Anderson M.
dc.creatorZavaleta Martínez Vargas, Alfonso
dc.creatorSalas, María
dc.creatorSoares, Andreimar Martins
dc.creatorCalderón, Leonardo de A.
dc.creatorTanaka Azevedo, Anita Mitico
dc.creatorLomonte, Bruno
dc.creatorCalvete Chornet, Juan José
dc.creatorCaldeira, Cleópatra A. S.
dc.date.accessioned2021-04-05T21:47:15Z
dc.date.available2021-04-05T21:47:15Z
dc.date.issued2020
dc.identifier.citationhttps://pubs.acs.org/doi/10.1021/acs.jproteome.0c00337es_ES
dc.identifier.issn1535-3893
dc.identifier.issn1535-3907
dc.identifier.urihttps://hdl.handle.net/10669/83164
dc.description.abstractWe report a structural and functional proteomics characterization of venoms of the two subspecies (Bothrops bilineatusbilineatus and B. b. smaragdinus) of the South American palm pit viper from the Brazilian state of Rondônia and B. b. smaragdinus from Perú. These poorly known arboreal and mostly nocturnal generalist predators are widely distributed in lowland rainforests throughout the entire Amazon region, where they represent an important cause of snakebites. The three B. bilineatus spp. venom samples exhibit overall conserved proteomic profiles comprising components belonging to 11 venom protein classes, with PIII (34–40% of the total venom proteins) and PI (8–18%) SVMPs and their endogenous tripeptide inhibitors (SVMPi, 8–10%); bradykinin-potentiating-like peptides (BBPs, 10.7–15%); snake venom serine proteinases (SVSP, 5.5–14%); C-type lectin-like proteins (CTL, 3–10%); phospholipases A2 (PLA2, 2.8–7.6%); cysteine-rich secretory proteins (CRISP, 0.9–2.8%); l-amino acid oxidases (LAO, 0.9–5%) representing the major components of their common venom proteomes. Comparative analysis of the venom proteomes of the two geographic variants of B. b. smaragdinus with that of B. b. bilineatus revealed that the two Brazilian taxa share identical molecules between themselves but not with Peruvian B. b. smaragdinus, suggesting hybridization between the geographically close, possibly sympatric, Porto Velho (RO, BR) B. b. smaragdinus and B. b. bilineatus parental populations. However, limited sampling does not allow determining the frequency of this event. The toxin arsenal of the South American palm pit vipers may account for the in vitro recorded collagenolytic, caseinolytic, PLA2, l-amino acid oxidase, thrombin-like and factor X-activating activities, and the clinical features of South American palm pit viper envenomings, i.e., local and progressively ascending pain, shock and loss of consciousness, spontaneous bleeding, and profound coagulopathy. The remarkable cross-reactivity of the Brazilian pentabothropic SAB antivenom toward the heterologous B. b. bilineatus venom suggests that the paraspecific antigenic determinants should have been already present in the venom of the last common ancestor of the Bothrops ″jararaca″ and ″taeniatus″ clades, about 8.5 Mya in the mid-late Miocene epoch of the Cenozoic era. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the data set identifiers PXD020043, PXD020026, and PXD020013.es_ES
dc.description.sponsorshipMinisterio de Ciencia, Innovación y Universidades/[BFU2017-89103-P]//Españaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[]/UCR/Costa Ricaes_ES
dc.language.isoenges_ES
dc.sourceJournal of Proteome Research, vol.19(8), pp.3518-3532es_ES
dc.subjectComparative snake venomicses_ES
dc.subjectSouth American palm viperes_ES
dc.subjectBothrops bilineatuses_ES
dc.subjectAntivenomicses_ES
dc.subjectBrazilian pentabothropic antivenomes_ES
dc.titleDanger in the canopy: comparative proteomics and bioactivities of the venoms of the South American palm viper Bothrops bilineatus subspecies bilineatus and smaragdinus, and antivenomics of B. b. bilineatus (Rondônia) venom against the Brazilian pentabothropic antivenomes_ES
dc.typeartículo científicoes_ES
dc.identifier.doi10.1021/acs.jproteome.0c00337
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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