Comparative evaluation of immunological and structural similarities of snake venom C-type lectin proteins.
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.
Castro
H C
HC
Laboratório de Hemostase e Venenos, Departamento de Bioquímica Médica, ICB/CCS, Univ. Federal do Rio de Janeiro, Bloco H, 20. andar-Ilha do Fundão Cidade Universitaria, Rio de Janeiro, RJ CEP 21941-590, Brazil.
Lemos
M G J
MG
Bon
C
C
Zingali
R B
RB
D000818:Animals; D000906:Antibodies / Q000276:immunology; D015153:Blotting, Western; D003435:Crotalid Venoms / Q000737:chemistry / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D037181:Lectins, C-Type / Q000737:chemistry* / Q000276:immunology*; D012910:Snake Venoms / Q000737:chemistry* / Q000276:immunology*; D012911:Snakes
D000906:Antibodies; D003435:Crotalid Venoms; D000939:Epitopes; D037181:Lectins, C-Type; D012910:Snake Venoms; C083739:bothrojaracin