dc.creator | Lomonte, Bruno | |
dc.creator | Mora Obando, Diana | |
dc.creator | Fernández Ulate, Julián | |
dc.creator | Sanz, Libia | |
dc.creator | Pla Ferrer, Davinia | |
dc.creator | Gutiérrez, José María | |
dc.creator | Calvete Chornet, Juan José | |
dc.date.accessioned | 2014-12-15T16:48:08Z | |
dc.date.available | 2014-12-15T16:48:08Z | |
dc.date.issued | 2015-01 | |
dc.identifier.citation | http://www.sciencedirect.com/science/article/pii/S0041010114006060 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.other | essn:1879-3150 | |
dc.identifier.uri | https://hdl.handle.net/10669/11223 | |
dc.description | artículo -- Universidad de Costa Rica, Instituto de Investigaciones Clodomiro Picado, 2015. Investigación apoyada por ICGEB-Italia, CYTED, Ministerio de Economía y Competitividad de España. Este documento es privado debido a limitaciones de derechos de autor. | es_ES |
dc.description.abstract | Bothriechis nigroviridis is an arboreal Neotropical pitviper found in Costa Rica and Panam a. A previous
proteomic profiling of its venom revealed the presence of proteins with homology to the A and B subunits
of crotoxin/Mojave toxin, a heterodimeric phospholipase A2 (PLA2) complex only described in
rattlesnake venoms (genera Crotalus and Sistrurus). The native crotoxin-like heterodimer, named
nigroviriditoxin, and its A and B subunits were isolated in the present work, and the complete amino acid
sequence of the B subunit was determined. The purified A and B components were demonstrated to form
a complex when reconstituted under native conditions. Nigroviriditoxin presents features similar to
crotoxin, albeit displaying lower toxicity: the A component decreases the PLA2 activity of the B
component, and increases its lethal potency in mice. Also in similarity to crotoxin B, nigroviriditoxin B
induces myonecrosis. Its 122 amino acid sequence presents 81% identity with crotoxin B. Accordingly,
nigroviriditoxin B was cross-recognized by equine antibodies from a Crotalus durissus terrificus antivenom.
Phylogenetic analysis shows that the novel PLA2 from B. nigroviridis venom is basal to the branch
including all the homologous PLA2 enzymes described in rattlesnakes, and more distant from PLA2s from
Bothriechis species. Nigroviriditoxin is the first heterodimeric PLA2 complex found in a non-rattlesnake,
Neotropical viperid venom, which displays structural, functional, and immunochemical similarities to
crotoxin. The present findings are compatible with the existence of the particular structural trait of
crotoxin-like molecules in New World pitvipers before the split of the Meso-South American and the
Nearctic clades. | es_ES |
dc.description.sponsorship | Universidad de Costa Rica.
ICGEB-Italia.
CYTED.
Ministerio de Economía y Competitividad de España. | es_ES |
dc.language.iso | en_US | es_ES |
dc.publisher | Toxicon vol 93:144–154 | es_ES |
dc.subject | Snake venom | es_ES |
dc.subject | Veneno de serpiente | es_ES |
dc.subject | Sustancia peligrosa | es_ES |
dc.title | First crotoxin-like phospholipase A2 complex from a New World non-rattlesnake species: Nigroviriditoxin, from the arboreal Neotropical snake Bothriechis nigroviridis | es_ES |
dc.type | artículo original | |
dc.identifier.doi | doi: 10.1016/j.toxicon.2014.11.235 | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.identifier.codproyecto | 741-B4-100 | |