dc.creator | Correa Netto, Carlos | |
dc.creator | Araujo, Ricardo Teixeira | |
dc.creator | Aguiar, Aniesse Silva | |
dc.creator | Melgarejo, Aníbal Rafael | |
dc.creator | De Simone, Salvatore Giovanni | |
dc.creator | Soares, Márcia Regina | |
dc.creator | Foguel, Debora | |
dc.creator | Zingali, Russolina Benedeta | |
dc.date | 2017-09-19T15:37:34Z | |
dc.date | 2017-09-19T15:37:34Z | |
dc.date | 2010 | |
dc.date.accessioned | 2023-09-26T20:10:23Z | |
dc.date.available | 2023-09-26T20:10:23Z | |
dc.identifier | CORREA 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.identifier | 0041-0101 | |
dc.identifier | https://www.arca.fiocruz.br/handle/icict/21060 | |
dc.identifier | 10.1016/j.toxicon.2009.12.018 | |
dc.identifier | 1879-3150 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/8850396 | |
dc.description | A 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.description | 2030-01-01 | |
dc.format | application/pdf | |
dc.language | eng | |
dc.publisher | Elsevier | |
dc.rights | restricted access | |
dc.subject | Bothrops | |
dc.subject | Venenos de Serpentes | |
dc.subject | Bothrops jararacussu | |
dc.subject | Bothrops jararaca | |
dc.subject | Crotalus durissus | |
dc.subject | Snake venom proteome | |
dc.subject | Immunome | |
dc.title | Immunome and venome of Bothrops jararacussu: a proteomic approach to study the molecular immunology of snake toxins | |
dc.type | Article | |