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dc.creatorLomonte, Bruno
dc.date.accessioned2018-04-19T21:14:50Z
dc.date.available2018-04-19T21:14:50Z
dc.date.issued2012
dc.identifier.citationhttps://www.sciencedirect.com/science/article/pii/S0041010112005041es_ES
dc.identifier.urihttp://hdl.handle.net/10669/74495
dc.description.abstractKnowledge on toxin immunogenicity at the molecular level can provide valuable information for the improvement of antivenoms, as well as for understanding toxin structure– function relationships. The aims of this study are two-fold: first, to identify the linear B-cell epitopes of myotoxin II from Bothrops asper snake venom, a Lys49 phospholipase A2 homologue; and second, to use antibodies specifically directed against an epitope having functional relevance in its toxicity, to probe the dimeric assembly mode of this protein in solution. Linear B-cell epitopes were identified using a library of overlapping synthetic peptides spanning its complete sequence. Epitopes recognized by a rabbit antiserum to purified myotoxin II, and by three batches of a polyvalent (Crotalidae) therapeutic antivenom (prepared in horses immunized with a mixture of B. asper, Crotalus simus, and Lachesis stenophrys venoms) were mapped using an enzyme-immunoassay based on the capture of biotinylated peptides by immobilized streptavidin. Some of the epitopes identified were shared between the two species, whereas others were unique. Differences in epitope recognition were observed not only between the two species, but also within the three batches of equine antivenom. Epitope V, located at the C-terminal region of this protein, is known to be relevant for toxicity and neutralization. Affinity-purified rabbit antibodies specific for this site were able to immunoprecipitate myotoxin II, suggesting that the two copies of epitope V are simultaneously available to antibody binding, which would be compatible with the mode of dimerization known as “conventional” dimer.es_ES
dc.description.sponsorshipInternational Center of Genetic Engineering and Biotechnology/[CRP Program COS-08-03]/ICGEB/Indiaes_ES
dc.language.isoen_USes_ES
dc.sourceToxicon, 60(5), 782-790 (2012)es_ES
dc.subjectmyotoxines_ES
dc.subjectphospholipase A2es_ES
dc.subjectSnake venomes_ES
dc.titleIdentification of linear B-cell epitopes on myotoxin-II, a Lys49 phospholipase A2 homologue from Bothrops asper snake venomes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.toxicon.2012.05.028
dc.identifier.doi0041-0101
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.codproyecto741-A9-513


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