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Immunochemical and biological characterization of monoclonalantibodies against BaP1, a metalloproteinase from Bothrops aspersnake venom
Fernandes, I; Assumpção, G. G; Silveira, C. R. F; Faquim Mauro, E. L; Tanjoni, I; Carmona, A. K; Alves, M. F. M; Takehara, H. A; Rucavado, A; Ramos, O. H. P; Moura-da-Silva, A. M; Gutiérrez, J. M.
Afiliação
  • Fernandes, I; Instituto Butantan. São Paulo. BR
  • Assumpção, G. G; Instituto Butantan. São Paulo. BR
  • Silveira, C. R. F; Instituto Butantan. São Paulo. BR
  • Faquim Mauro, E. L; Instituto Butantan. São Paulo. BR
  • Tanjoni, I; Instituto Butantan. São Paulo. BR
  • Carmona, A. K; s.af
  • Alves, M. F. M; s.af
  • Takehara, H. A; Instituto Butantan. São Paulo. BR
  • Rucavado, A; s.af
  • Ramos, O. H. P; Instituto Butantan. São Paulo. BR
  • Moura-da-Silva, A. M; Instituto Butantan. São Paulo. BR
  • Gutiérrez, J. M; s.af
Toxicon ; Toxicon;56(6): 1059-1065, Jul 17, 2010.
Article em En | SES-SP, SESSP-IBPROD, SES-SP, SESSP-IBACERVO | ID: biblio-1068259
Biblioteca responsável: BR78.1
Localização: BR78.1
ABSTRACT
BaP1 is a P-I class of Snake Venom Metalloproteinase (SVMP) relevant in the local tissue damage associated with envenomations by Bothrops asper, a medically-important species in Central America and parts of South America. Six monoclonal antibodies (MoAb) against BaP1 (MABaP1) were produced and characterized regarding their isotype, dissociation constant (Kd), specificity and ability to neutralize BaP1-induced hemorrhagic and proteolytic activity. Two MABaP1 are IgM, three are IgG1 and one is IgG2b. The Kds of IgG MoAbs were in the nM range. All IgG MoAbs recognized conformational epitopes of BaP1 and B. asper venom components but failed to recognize venoms from 27 species of Viperidae, Colubridae and Elapidae families. Clone 7 cross-reacted with three P-I SVMPs tested (moojeni protease, insularinase and neuwiedase). BaP1-induced hemorrhage was totally neutralized by clones 3, 6 and 8 but not by clone 7. Inhibition of BaP1 enzymatic activity on a synthetic substrate by MABaP1 was totally achieved by clones 3 and 6, and partially by clone 8, but not by clone 7. In conclusion, these neutralizing MoAbs against BaP1 may become important tools to understand structure–function relationships of BaP1 and the role of P-I class SVMP in snakebite envenomation.
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Coleções: 06-national / BR Base de dados: SES-SP / SESSP-IBACERVO / SESSP-IBPROD Assunto principal: Venenos de Serpentes / Antivenenos / Bothrops / Metaloproteases / Anticorpos Monoclonais Limite: Animals Idioma: En Revista: Toxicon Ano de publicação: 2010 Tipo de documento: Article
Buscar no Google
Adicionar na Minha BVS
Imprimir
XML

Coleções: 06-national / BR Base de dados: SES-SP / SESSP-IBACERVO / SESSP-IBPROD Assunto principal: Venenos de Serpentes / Antivenenos / Bothrops / Metaloproteases / Anticorpos Monoclonais Limite: Animals Idioma: En Revista: Toxicon Ano de publicação: 2010 Tipo de documento: Article