Fig  2 confirms that both venoms were able to hydrolyze sphingomy

Fig. 2 confirms that both venoms were able to hydrolyze sphingomyelin, but PLlv exhibited higher sphingomyelinase activity than BLlv, and this difference was statistically significant. These data confirm previous observations suggesting that lethal and skin

effects of Loxosceles venoms are correlated to their sphingomyelinase activity ( de Oliveira et al., 2005). The higher lethal and sphingomyelinase activity observed in PLlv, may explain the higher frequency of systemic loxoscelism reported in Peru: 25–32% of cases in this country are reported as viscerocutaneous loxoscelism ( Sanabria and Zavaleta, 1997; Instituto ICG-001 datasheet Nacional de Salud, 2006), compared to 13–16% of cases reported with Loxosceles spp in Brazil ( Isbister and

Fan, 2011). The components of PLlv ( Fig. 3A) and BLlv ( Fig. 3B) were separated by two-dimensional gel electrophoresis and the gels were stained with silver nitrate. Differences in the number and intensity of spots were found between the venoms. A large portion of proteins from PLlv and BLlv venoms (52 of 105 and 52 of 134 for, respectively) had molecular mass between 29 and 36 kDa. Fig. 3C shows the alignment between PLlv and BLlv profiles, using the software Progenesis SameSpot. The green spots belong to PLlv, the pink spots to BLlv and the dark signals are overlapping spots. The alignment revealed 40.4% of difference in the protein pattern between both venoms, GSK-3 signaling pathway within the 29–36 kDa region, particularly in the zone with basic isoelectric point (pI), where several PLlv proteins are located (green spots). This region corresponds to proteins with dermonecrotic and/or sphingomyelinase activity previously

isolated from the venom gland of Loxosceles spiders ( Kalapothakis et al., 2007). In addition, PLlv presents several other proteins, between 20 and 29 kDa, with basic pI. This region probably corresponds to proteins with metalloprotease (astacin-like) activity, described as a protein family in venoms of L. intermedia, L. gaucho and BLlv ( Trevisan-Silva et al., 2010). Machado et al. (2005), reported Cytidine deaminase several isoforms of dermonecrotic toxins in the venoms of L. laeta, L. gaucho and L. intermedia Brazilian spiders, thus, corroborating our results showing intraspecific differences in the protein profile. Dermonecrotic toxins, sphingomyelinases D (SMases D), phospholipase D family or Loxtox protein family ( Tambourgi et al., 1995; Chaim et al., 2006; Kalapothakis et al., 2007), are the main toxic venom components, responsible for local and systemic effects induced by whole venom from Loxosceles spiders. These proteins constitute a family of homologs with 190 non-redundant sequences described in 21 species of the Sicariidae family ( Binford et al., 2009). SMase D (EC number 3.1.4.

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