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resumen

Resumen
Foot and mouth disease is caused by a non-enveloped virus (FMDV), which disposes several antigenic sites at the surface of their capsid proteins. The most relevant and immunodominant antigenic site of FMDV (site A or AnSA) includes a key virus–cell interaction element (RGD motif) located in the Viral Protein 1 (VP1), more precisely at the GH loop. AnSA includes a set of overlapped and mainly linear epitopes, which are the main targets of the humoral [ver mas...]
dc.contributor.authorMarrero Diaz De Villegas, Rubén
dc.contributor.authorRodríguez Limardo, Ramiro
dc.contributor.authorCarrillo, Elisa Cristina
dc.contributor.authorKonig, Guido Alberto
dc.contributor.authorTurjanski, Adrián G.
dc.date.accessioned2019-06-12T12:58:07Z
dc.date.available2019-06-12T12:58:07Z
dc.date.issued2015-10
dc.identifier.issn0022-1759
dc.identifier.otherhttps://doi.org/10.1016/j.jim.2015.06.008
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0022175915300090
dc.identifier.urihttp://hdl.handle.net/20.500.12123/5301
dc.description.abstractFoot and mouth disease is caused by a non-enveloped virus (FMDV), which disposes several antigenic sites at the surface of their capsid proteins. The most relevant and immunodominant antigenic site of FMDV (site A or AnSA) includes a key virus–cell interaction element (RGD motif) located in the Viral Protein 1 (VP1), more precisely at the GH loop. AnSA includes a set of overlapped and mainly linear epitopes, which are the main targets of the humoral immune response. Taking advantage over specific structural features of the GH loop, we have evaluated the influence of every amino acid residue at AnSA in the interaction with 2 neutralizing antibodies by molecular modeling techniques. Additionally, we constructed diverse interaction complexes with multiple site A mutants and discussed about the structural influence of amino acidic insertions in such relevant antigenic site of FMDV. Our approach is in agreement with previous ELISA experiments and allows the understanding of how FMDV mutations may alter the interaction with different antibodies, as we can estimate the contribution of each amino acid to the interaction. Overall, our work contributes to the development of specific vaccination strategies for FMD control.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherElsevieres_AR
dc.rightsinfo:eu-repo/semantics/restrictedAccesses_AR
dc.sourceJournal of Immunological Methods 425 : 51-57 (October 2015)es_AR
dc.subjectFiebre Aftosaes_AR
dc.subjectFoot and Mouth Diseaseeng
dc.subjectEnfermedades de los Animaleses_AR
dc.subjectAnimal Diseaseseng
dc.subjectVirus Fiebre Aftosaes_AR
dc.subjectAphthoviruseng
dc.subjectAnticuerpos Monoclonaleses_AR
dc.subjectMonoclonal Antibodieseng
dc.subjectBioinformáticaes_AR
dc.subjectBioinformaticseng
dc.titleA computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodieses_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Biotecnologíaes_AR
dc.description.filFil: Marrero Diaz De Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentinaes_AR
dc.description.filFil: Rodríguez Limardo, Ramiro. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Bioinformática Estructural; Argentinaes_AR
dc.description.filFil: Carrillo, Elisa Cristina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Konig, Guido Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Turjanski, Adrian G. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentinaes_AR
dc.subtypecientifico


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