ABSTRACT
Antibodies raised against denatured and native forms of bothrojaracin were used to analyze the immunological similarities compared to the structural and biological features of five C-type lectin proteins from snake venom (bothrojaracin, botrocetin, Factor IX/X binding protein (FIX/Xbp), convulxin and Bothrops jararaca lectin). Anti-denatured-bothrojaracin antibodies, which recognize mainly linear epitopes, cross-reacted with botrocetin, FIX/Xbp and convulxin, as expected for homologous proteins. On the other hand, anti-native-bothrojaracin antibodies, which mostly interact with conformational epitopes, exhibited a higher degree of selectivity. These results show that differences exist at the surface of these proteins and that they should be related to their different biological activities, while they share a common and similar scaffold.
