Better characterization of individual snake venom toxins is useful for analyzing the association of their toxic domains and relevant antigenic epitopes. Here we analyzed the Bitis arietans
hemorrhagic-inducing toxin present in a representative venom sample. Among the 1´ to 5´ protein peaks isolated using a Sephacryl S 100 HR chromatography column, hemorrhagic activity was expressed by all according to the following intensity, P´5 > P´3 > P´2 >, P´4. The proteins were recognized and measured with antibodies present in polyvalent horse F(ab)´2
spp., Lachesis muta
, B. atrox, Bothrops spp., Crotalus spp
., and Naja spp
. or in IgY anti-B. arietans
and anti-Bitis spp.
using enzyme-linked immunosorbent assays and western blotting. In addition, in an in vitro-in vivo assay these anti-venoms were able to block hemorrhagic-inducing activity. The evident cross-reactivity expressed by different specific anti-venoms indicates that metalloproteinases induce an immunological signature indicating the presence of similar antigenic epitopes for several snake venoms.
Key words: Snake venoms, anti-venoms, Bitis arietans, hemorrhage, metalloproteinases