dc.creatorCorrea Netto, Carlos
dc.creatorAraujo, Ricardo Teixeira
dc.creatorAguiar, Aniesse Silva
dc.creatorMelgarejo, Aníbal Rafael
dc.creatorDe Simone, Salvatore Giovanni
dc.creatorSoares, Márcia Regina
dc.creatorFoguel, Debora
dc.creatorZingali, Russolina Benedeta
dc.date2017-09-19T15:37:34Z
dc.date2017-09-19T15:37:34Z
dc.date2010
dc.date.accessioned2023-09-26T20:10:23Z
dc.date.available2023-09-26T20:10:23Z
dc.identifierCORREA NETO, Carlos; et al. Immunome and venome of Bothrops jararacussu: A proteomic approach to study the molecular immunology of snake toxins. Toxicon, v.55, p.1222-1235, 2010.
dc.identifier0041-0101
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/21060
dc.identifier10.1016/j.toxicon.2009.12.018
dc.identifier1879-3150
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8850396
dc.descriptionA combination of anti-bothropic and anti-crotalic sera has been reported to be more effective in neutralizing the effects of Bothrops jararacussu venom than anti-bothropic serum alone. The role of proteins from B. jararacussu venom in the horse immune response was evaluated via the analysis of cross-reactivity with homologous and heterologous sera. Many of the proteins in B. jararacussu venom were identified via 2D gel electrophoresis. Western blots revealed that anti-jararacussu showed higher reactivity to l-aminoxidase (LAOs) and snake venom metalloproteinase, (SVMPs) and weaker reactivity towards Snake venom serine proteases (SVSPs), PLA(2), C-type lectin and cysteine-rich proteins. Anti-jararaca preferentially recognized LAOs, SVMPs and SVSPs. Both of these sera failed to recognize low-molecular weight proteins. Anti-crotalic serum clearly recognized LAOs, C-type lectin, SVSP, cysteine-rich proteins, SVMP and Asp49-PLA(2). The cross-reactivity with anti-PLA(2) revealed the immunoreactivity of these antibodies to proteins with molecular masses in a range that is poorly recognized by other studied anti-sera. Our results suggest that the contribution of anti-crotalic serum to the neutralization of B. jararacussu by may be due to its cross-reactivity with proteins such as C-type lectins, SVSPs, Asp49-PLA(2). These results also reinforce the importance of neutralizing the highly toxic proteins inclusive those with low immunogenicity in commercial antivenom production to obtain a highly protective serum against snake venoms.
dc.description2030-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectBothrops
dc.subjectVenenos de Serpentes
dc.subjectBothrops jararacussu
dc.subjectBothrops jararaca
dc.subjectCrotalus durissus
dc.subjectSnake venom proteome
dc.subjectImmunome
dc.titleImmunome and venome of Bothrops jararacussu: a proteomic approach to study the molecular immunology of snake toxins
dc.typeArticle


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