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dc.creatorSánchez Brenes, Andrés
dc.creatorHerrera Vega, María
dc.creatorVillalta Arrieta, Mauren
dc.creatorSolano, Daniela
dc.creatorSegura Ruiz, Álvaro
dc.creatorLomonte, Bruno
dc.creatorGutiérrez, José María
dc.creatorLeón Montero, Guillermo
dc.creatorVargas Arroyo, Mariángela
dc.date.accessioned2019-02-04T15:35:21Z
dc.date.available2019-02-04T15:35:21Z
dc.date.issued2018-06
dc.identifier.citationhttps://www.sciencedirect.com/science/article/pii/S1874391918301660?via%3Dihubes_ES
dc.identifier.issn1874-3919
dc.identifier.urihttp://hdl.handle.net/10669/76542
dc.description.abstractThe protein composition and toxinological profile of the venom of the African spitting elapid Hemachatus haemachatus (Ringhals) were characterized by bottom-up proteomics and functional in vitro and in vivo assays. Venom is composed of abundant three-finger toxins (3FTxs; 63.3%), followed by phospholipases A2 (PLA2s; 22.8%), snake venom metalloproteinases (SVMPs; 7.1%), cysteine-rich secretory proteins (CRISPs; 4.1%) and Kunitz type protease inhibitors (KTPIs; 1.5%). 3FTxs are the main responsible for lethality and myotoxicity in mice and in vitro anticoagulant activity. In contrast to closely related spitting species, whose venom 3FTxs induces dermonecrosis, the 3FTxs of H. haemachatus did not induce dermonecrotic activity. The venom showed in vitro PLA2 activity, and most likely PLA2s contribute to some extent in venom lethality, as judged by partial reduction in toxicity after inhibition of their catalytic activity. Despite its relatively high content of SVMPs, compared to most elapids, the venom of H. haemachatus did not exert hemorrhagic effect, proteolytic activity on azocasein or defibrinogenating activity. Toxicovenomic characterization of H. haemachatus venom revealed that RP-HPLC fractions with higher abundance of 3FTxs presented lethal activity, while fractions with high content of PLA2s did not, underscoring the role of 3FTxs in the pathophysiology caused by this venom. Biological significance: The proteomic composition and toxinological profile of the venom of Ringhals snake, Hemachatus haemachatus, a cobra-like spitting snake endemic to southern Africa, were investigated. In vitro, Ringhals venom showed anticoagulant and phospholipase A2 activities, but was devoid of proteolytic activity on azocasein. In mice, venom induced lethality and myotoxicity, but no local hemorrhage or dermonecrosis. The lack of dermonecrotic activity is in sharp contrast to venoms of closely related spitting cobras which present a similar relative abundance of 3FTxs but are potently dermonecrotic. 3FTxs, the most abundant protein family in the venom, are predominantly responsible for toxic effects. PLA2 enzyme inactivation experiments suggest that H. haemachatus venom lethality is not dependent on PLA2s, but instead is more related to neurotoxic or cardiotoxic 3FTxs. The characterization of this venom, based on proteomic and toxicovenomic approaches, is useful for more in depth studies associated with biogeography, phylogeny, toxinology and antivenom efficacy towards the venom of this species, and its association with related elapidses_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B7-108]/UCR7Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Proteomics, vol.181, pp. 104-117es_ES
dc.subjectHemachatus haemachatuses_ES
dc.subjectVenomicses_ES
dc.subjectRinghalses_ES
dc.subjectThree-finger toxinses_ES
dc.subjectPhospholipase A2es_ES
dc.subjectSnake venomes_ES
dc.subject615.946 Venenos animaleses_ES
dc.titleProteomic and toxinological characterization of the venom of the South African Ringhals cobra Hemachatus haemachatuses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.identifier.doi10.1016/j.jprot.2018.04.007
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-B7-108


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