Immunochemical Recognition of Bothrops rhombeatus Venom by Two Polyvalent Antivenoms

The protein profile of venom was compared to and and the effectiveness of antivenoms from the National Institute of Health of Colombia (INS) and Antivipmyn-Tri (AVP-T) of Mexico were analyzed. Protein profiles were studied with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and reverse-phase high-performance liquid chromatography (RP-HPLC). The neutralizing potency and the level of immunochemical recognition of the antivenoms to the venoms were determined using Western blot, affinity chromatography, and enzyme-linked immunosorbent assay (ELISA). Bands of phospholipase A2 (PLA2), metalloproteinases (svMPs) I, II, and III as well as serine proteinases (SPs) in the venom of were recognized by SDS-PAGE. With Western blot, both antivenoms showed immunochemical recognition towards PLA2 and svMP. INS showed 94% binding to venom and 92% to while AVP-T showed 90.4% binding to venom and 96.6% to . Both antivenoms showed binding to PLA2 and svMP, with greater specificity of AVP-T towards Antivenom neutralizing capacity was calculated by species and mL of antivenom, finding the following for INS: 6.6 mgV/mL, 5.5 mgV/mL, and 1.3 mgV/mL. Meanwhile, for AVP-T, the following neutralizing capacities were found: 2.7 mgV/mL, 2.1 mgV/mL, and 1.4 mgV/mL. These results show that both antivenoms presented similarity between calculated neutralizing capacities in our trial, reported in a product summary for the public for the species; however, this does not apply to the other species tested in this trial.