In either case, identification of the epitopes bound by antivenom serum antibodies will improve the quality of antivenoms. In the case of B. jararacussu snake venom, the most effective treatment involves the administration

of a combination of anti-bothropic and anti-crotalic antivenom to neutralize the myotoxic, coagulant and lethal activities of the venom than when one of these antivenom sera is used alone ( dos Santos et al., 1992, de Roodt et al., 1998 and de Roodt et al., 1999). It is evident that each of the individual antivenoms delivers antibodies that are necessary for neutralizing the effect of the Alectinib nmr venom. Considering the proteins present in venom, the PLA2s are the main enzymes responsible for

the harmful effects. Since the performances of the individual antivenom sera are not well check details understood, we focused on determining the antigenic determinants present in the PLA2s proteins from B. jararacussu venom that are bound by antibodies present in the individual anti-bothropic and anti-crotalic horse antivenom. The mapping experiments presented in Fig. 1 showed the immunogenicity of the array of peptides that was synthesized to represent the three PLA2s from B. jararacussu snake venom. Two antigenic determinants were recognized by the anti-bothropic horse antivenom, four antigenic determinants by the anti-crotalic horse antivenom and six peptides were recognized by both antivenom sera ( Table 1). While cross reactivity Selleckchem Verteporfin has been described for distinct proteins from snake venoms ( de Roodt et al., 1998, Oshima-Franco et al., 2001 and Beghini et al., 2007), which may reflect genetic relationship within proteins of the same family in various species and/or repetitive

segments in distinct toxins, the use of spot synthesis peptide array employed here provided more detail of the common and unique epitopes bound by the two commercial horse antivenom sera. The advantages of this micro-immunoassay employing cellulose immobilized peptides over other different assays as classical ELISA for screening of antigenic peptide-arrays has been extensively discussed ( Copeland et al., 2004 and Henderson and Bradley, 2007). In our assays it was employed a cellulose membrane derivatized with amino-PEG500 to attach the amino acids. The advantage of this link over that using beta-alanine is the neglected background generated. The Lys49-PLA2s are proteins that exhibit various toxic effects including oedema, membrane depolarization (Kihara et al., 1992) and myonecrotic activity (Montecucco et al., 2008).