A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies

Autores
Marrero Diaz De Villegas, Rubén; Rodríguez Limardo, Ramiro; Carrillo, Elisa Cristina; Konig, Guido Alberto; Turjanski, Adrián G.
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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 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.
Instituto de Biotecnología
Fil: Marrero Diaz De Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Rodríguez Limardo, Ramiro. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Bioinformática Estructural; Argentina
Fil: Carrillo, Elisa Cristina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Konig, Guido Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: 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; Argentina
Fuente
Journal of Immunological Methods 425 : 51-57 (October 2015)
Materia
Fiebre Aftosa
Enfermedades de los Animales
Virus Fiebre Aftosa
Anticuerpos Monoclonales
Bioinformática
Foot and Mouth Disease
Animal Diseases
Aphthovirus
Monoclonal Antibodies
Bioinformatics
Nivel de accesibilidad
acceso restringido
Condiciones de uso
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/5301
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network_name_str INTA Digital (INTA)
spelling A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodiesMarrero Diaz De Villegas, RubénRodríguez Limardo, RamiroCarrillo, Elisa CristinaKonig, Guido AlbertoTurjanski, Adrián G.Fiebre AftosaEnfermedades de los AnimalesVirus Fiebre AftosaAnticuerpos MonoclonalesBioinformáticaFoot and Mouth DiseaseAnimal DiseasesAphthovirusMonoclonal AntibodiesBioinformaticsFoot 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.Instituto de BiotecnologíaFil: Marrero Diaz De Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; ArgentinaFil: Rodríguez Limardo, Ramiro. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Bioinformática Estructural; ArgentinaFil: Carrillo, Elisa Cristina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Konig, Guido Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: 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; ArgentinaElsevier2019-06-12T12:58:07Z2019-06-12T12:58:07Z2015-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://www.sciencedirect.com/science/article/pii/S0022175915300090http://hdl.handle.net/20.500.12123/53010022-1759https://doi.org/10.1016/j.jim.2015.06.008Journal of Immunological Methods 425 : 51-57 (October 2015)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccess2025-10-16T09:29:33Zoai:localhost:20.500.12123/5301instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-16 09:29:33.736INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
title A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
spellingShingle A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
Marrero Diaz De Villegas, Rubén
Fiebre Aftosa
Enfermedades de los Animales
Virus Fiebre Aftosa
Anticuerpos Monoclonales
Bioinformática
Foot and Mouth Disease
Animal Diseases
Aphthovirus
Monoclonal Antibodies
Bioinformatics
title_short A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
title_full A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
title_fullStr A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
title_full_unstemmed A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
title_sort A computational study of the interaction of the foot and mouth disease virus VP1 with monoclonal antibodies
dc.creator.none.fl_str_mv Marrero Diaz De Villegas, Rubén
Rodríguez Limardo, Ramiro
Carrillo, Elisa Cristina
Konig, Guido Alberto
Turjanski, Adrián G.
author Marrero Diaz De Villegas, Rubén
author_facet Marrero Diaz De Villegas, Rubén
Rodríguez Limardo, Ramiro
Carrillo, Elisa Cristina
Konig, Guido Alberto
Turjanski, Adrián G.
author_role author
author2 Rodríguez Limardo, Ramiro
Carrillo, Elisa Cristina
Konig, Guido Alberto
Turjanski, Adrián G.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Fiebre Aftosa
Enfermedades de los Animales
Virus Fiebre Aftosa
Anticuerpos Monoclonales
Bioinformática
Foot and Mouth Disease
Animal Diseases
Aphthovirus
Monoclonal Antibodies
Bioinformatics
topic Fiebre Aftosa
Enfermedades de los Animales
Virus Fiebre Aftosa
Anticuerpos Monoclonales
Bioinformática
Foot and Mouth Disease
Animal Diseases
Aphthovirus
Monoclonal Antibodies
Bioinformatics
dc.description.none.fl_txt_mv 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 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.
Instituto de Biotecnología
Fil: Marrero Diaz De Villegas, Rubén. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina
Fil: Rodríguez Limardo, Ramiro. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica. Laboratorio de Bioinformática Estructural; Argentina
Fil: Carrillo, Elisa Cristina. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Konig, Guido Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: 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; Argentina
description 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 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-10
2019-06-12T12:58:07Z
2019-06-12T12:58:07Z
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://www.sciencedirect.com/science/article/pii/S0022175915300090
http://hdl.handle.net/20.500.12123/5301
0022-1759
https://doi.org/10.1016/j.jim.2015.06.008
url https://www.sciencedirect.com/science/article/pii/S0022175915300090
http://hdl.handle.net/20.500.12123/5301
https://doi.org/10.1016/j.jim.2015.06.008
identifier_str_mv 0022-1759
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
eu_rights_str_mv restrictedAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv Journal of Immunological Methods 425 : 51-57 (October 2015)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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score 12.712165

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