Show simple item record

dc.creatorAntúnez Oliva, Josées_ES
dc.creatorFernández Ulate, Juliánes_ES
dc.creatorLomonte, Brunoes_ES
dc.creatorAngulo Ugalde, Yamilethes_ES
dc.creatorSanz, Libiaes_ES
dc.creatorPérez, Aliciaes_ES
dc.creatorCalvete Chornet, Juan Josées_ES
dc.creatorGutiérrez, José Maríaes_ES
dc.date.accessioned2016-11-28T14:44:03Zes_ES
dc.date.available2016-11-28T14:44:03Zes_ES
dc.date.issued2010-09-30es_ES
dc.identifier.citationhttp://libpubmedia.co.uk/antivenomics-of-atropoides-mexicanus-and-atropoides-picadoi-snake-venoms-relationship-to-the-neutralization-of-toxic-and-enzymatic-activities/es_ES
dc.identifier.issn2044-0324es_ES
dc.identifier.urihttp://hdl.handle.net/10669/29318es_ES
dc.description.abstractViperid snakes of the genus Atropoides are distributed in Mexico and Central America and, owing to their size and venom yield, are capable of provoking severe envenomings in humans. This study evaluated, using an ‘antivenomics’ approach, the ability of a polyspecific (polyvalent) antivenom manufactured in Costa Rica to recognize the proteins of Atropoides mexicanus and A. picadoi venoms, which are not included in the immunization mixture. In addition, the neutralization of lethal, hemorrhagic, myotoxic, coagulant, proteinase and phospholipase A2 (PLA2) activities of these venoms by the antivenom was assessed. The antivenom was highly-effective in immunodepleting many venom components, particularly high molecular mass P-III metalloproteinases (SVMPs), L-amino acid oxidases, and some serine proteinases and P-I SVMPs. In contrast, PLA2s, certain serine proteinases and P-I SVMPs, and a C type lectin-like protein were only partially immunodepleted, and two PLA2 molecules were not depleted at all. The antivenom was able to neutralize all toxic and enzymatic activities tested, although neutralization of lethality by A. nummifer venom was achieved when a challenge dose of 3 LD50s of venom was used, but was iffective when 4 LD50s were used. These results, and previously obtained evidence on the immunoreactivity of this antivenom towards homologous and heterologous venoms, revealed the low immunogenicity of a number of venom components (PLA2s, CRISPs, P-I SVMPs, and some serine proteinases), underscoring the need to search for innovative immunization protocols to improve the immune response to these antigens.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-A7-611]/UCR/Costa Ricaes_ES
dc.description.sponsorshipCRUSA-CSIC/2007CR0004//Españaes_ES
dc.description.sponsorshipConsejo Nacional de Rectores//CONARE/Costa Ricaes_ES
dc.description.sponsorshipMinisterio de Ciencia e Innovación/[BFU2007-61563]//Españaes_ES
dc.description.sponsorshipMinisterio de Ciencia e Innovación/[BFU2010-17373]//Españaes_ES
dc.language.isoen_USes_ES
dc.sourceJournal of Venom Research; Volumen 1. 2010es_ES
dc.subjectAtropoides picadoies_ES
dc.subjectAtropoides mexicanuses_ES
dc.subjectAntivenomicses_ES
dc.subjectAntivenomes_ES
dc.subjectNeutralizationes_ES
dc.subjectToxicityes_ES
dc.subjectImmunodepletiones_ES
dc.subjectSnake venomes_ES
dc.titleAntivenomics of Atropoides mexicanus and Atropoides picadoi snake venoms: Relationship to the neutralization of toxic and enzymatic activitieses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record