Production and partial characterization of monoclonal antibodies to Bothrops asper (terciopelo) myotoxin.

Seven murine monoclonal antibodies against Bothrops asper myotoxin were produced and partially characterized. They revealed the presence of at least four cross-reacting basic components in crude venom, with a common subunit mol. wt of 16,000 by sodium dodecylsulfate-polyacrylamide gel electrophoresis, but slight differences in charge. These myotoxin-related components might be isoforms of the toxin. By Western blotting and enzyme-immunoassay binding techniques, differences in the reactivities with basic venom fractions were observed among monoclonal antibodies, suggesting differences in epitope specificities. Three antibodies cross-reacted with B. nummifer crude venom. Two monoclonal antibodies were utilized to develop a two-site enzyme-immunoassay for myotoxin detection at the nanogram level. Three of the antibodies (one IgM and two IgG1) showed ability to neutralize myotoxicity of purified myotoxin in preincubation type experiments.