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Investigating antivenom function and cross-reactivity – a atudy of antibodies and their targets

dc.creatorEngmark, Mikael Mikael Gerling
dc.creatorde Masi, Federico
dc.creatorAndersen, Mikael Rørdam
dc.creatorLaustsen, Andreas Hougaard
dc.creatorGutiérrez, José María
dc.creatorLomonte, Bruno
dc.creatorLund, Ole
dc.date.accessioned2026-06-01T19:47:09Z
dc.date.issued2015-04
dc.description.abstractSnakebite envenoming remains one of the world’s most neglected tropical diseases, affecting millions each year. Antivenoms, produced by immunizing animals with snake venoms, are the main treatment, but their molecular mechanisms and cross-reactivity among related snake species are still poorly understood. This study applied high-density peptide microarray technology to identify linear epitopes from snake venom toxins recognized by antibodies in antivenoms. More than 93,000 peptides from 966 toxins of pit viper species were analyzed to map antibody-toxin interactions. The results revealed specific binding cores responsible for toxin neutralization and suggested cross-reactivity between Bothrops asper and Crotalus atrox venom metalloproteinases. These findings provide insights into improving the design, prediction, and potential recombination of antivenoms, contributing to the development of safer and broader-spectrum treatments for snakebite victims.
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)
dc.description.procedenceUCR::Vicerrectoría de Docencia::Salud::Facultad de Microbiología
dc.identifier.doihttps://doi.org/10.13140/rg.2.2.18714.64960
dc.identifier.urihttps://hdl.handle.net/10669/104656
dc.language.isoeng
dc.rightsacceso restringido
dc.sourceProtein.DTU 12th Workshop
dc.subjectsnakebite
dc.subjectantivenom
dc.subjectantibodies
dc.subjectepitopes
dc.subjectcross-reactivity
dc.subjectproteomics
dc.titleInvestigating antivenom function and cross-reactivity – a atudy of antibodies and their targets
dc.typepóster de congreso

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