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dc.creatorFernandes, Irene
dc.creatorAssumpção, G. G.
dc.creatorSilveira, C. R. F.
dc.creatorFaquim Mauro, E. L.
dc.creatorTanjoni, Isabelle
dc.creatorCarmona, A. K.
dc.creatorAlves, M. F. M.
dc.creatorTakehara, Harumi Ando
dc.creatorRucavado Romero, Alexandra
dc.creatorRamos, O. H. P.
dc.creatorMoura Da Silva, Ana M.
dc.creatorGutiérrez, José María
dc.date.accessioned2016-11-28T15:35:11Z
dc.date.available2016-11-28T15:35:11Z
dc.date.issued2010-11
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0041010110002953es_ES
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/10669/29320
dc.description.abstractBaP1 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.es_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico//CNPq/Brasiles_ES
dc.description.sponsorshipFundação de Amparo a Pesquisa do Estado de São Paulo//FAPESP/Brasiles_ES
dc.description.sponsorshipNeTropica///es_ES
dc.language.isoen_USes_ES
dc.sourceToxicon; Volumen 56, Número 6. 2010es_ES
dc.subjectMonoclonal antibodieses_ES
dc.subjectMetalloproteinasees_ES
dc.subjectBaP1es_ES
dc.subjectHemorrhagees_ES
dc.subjectSnake venomes_ES
dc.subjectNeutralizing antibodyes_ES
dc.titleImmunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venomes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.toxicon.2010.07.014
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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