Article
Linear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A2’s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom
Registro en:
SIMONE, Salvatore G. De; et al. Linear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A2’s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom. Toxicon, v.72, p.90–101, 2013.
0041-0101
10.1016/j.toxicon.2013.06.004
Autor
De Simone, Salvatore Giovanni
Pêgo, Paloma Napoleão
Pinto, Luiz André Lucas Teixeira
Santos, Jonathas D. L.
Simone, Thatiane S. De
Melgarejo Gimenez, Anibal Rafael
Aguiar, Aniesse S.
Salvador, Daniela P. Marchi
Resumen
The benefits from treatment with antivenom sera are indubitable. However, the mechanism
for toxin neutralization has not been completely elucidated. A mixture of antibothropic
and anti-crotalic horse antivenom has been reported to be more effective in
neutralizing the effects of Bothrops jararacussu snake venom than anti-bothropic antivenom
alone. This study determined which regions in the three PLA2s from B. jararacussu
snake venom are bound by antibodies in tetravalent anti-bothropic and monovalent anticrotalic
commercial horse antivenom. Mapping experiments of BthTX-I, BthTX-II and BthAI
using two small libraries of 69 peptides each revealed six major IgG-binding epitopes that
were recognized by both anti-bothropic and anti-crotalic horse antivenom. Two epitopes
in BthTX-I were only recognized by the anti-bothropic horse antivenom, while anti-crotalic
horse antivenom recognized four unique epitopes across the three PLA2s. Our studies
suggest that the harmful activities of the PLA2s present in the venom of B. jararacussu are
neutralized by the combinatorial treatment with both antivenom sera through their
complementary binding sites, which provides a wide coverage on the PLA2s. This is the
first peptide microarray of PLA2s from B. jararacussu snake venom to survey the performance
of commercial horse antiophidic antivenom. Regions recognized by the protective
antivenom sera are prime candidates for improved venom cocktails or a chimeric protein
encoding the multiple epitopes to immunize animals as well as for designing future
synthetic vaccines.