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Abstract
Pestivirus envelope protein E2 is crucial to virus infection and accomplishes virus-receptor interaction during entry. However, mapping of E2 residues mediating these interactions has remained unexplored. In this study, to investigate the structure-function relationship for a β-hairpin motif exposed to the solvent in the crystal structure of bovine viral diarrhea virus (BVDV) E2, we designed two amino acidic substitutions that result in a change of [ver mas...]
dc.contributor.authorMerwaiss, Fernando
dc.contributor.authorPascual, María José
dc.contributor.authorPomilio, María Trinidad
dc.contributor.authorLopez, Maria Gabriela
dc.contributor.authorTaboga, Oscar Alberto
dc.contributor.authorAlvarez, Diego Ezequiel
dc.date.accessioned2021-12-10T13:22:22Z
dc.date.available2021-12-10T13:22:22Z
dc.date.issued2021-06
dc.identifier.issn1999-4915
dc.identifier.otherhttps://doi.org/10.3390/v13061157
dc.identifier.urihttp://hdl.handle.net/20.500.12123/10881
dc.identifier.urihttps://www.mdpi.com/1999-4915/13/6/1157
dc.description.abstractPestivirus envelope protein E2 is crucial to virus infection and accomplishes virus-receptor interaction during entry. However, mapping of E2 residues mediating these interactions has remained unexplored. In this study, to investigate the structure-function relationship for a β-hairpin motif exposed to the solvent in the crystal structure of bovine viral diarrhea virus (BVDV) E2, we designed two amino acidic substitutions that result in a change of electrostatic potential. First, using wild type and mutant E2 expressed as soluble recombinant proteins, we found that the mutant protein had reduced binding to susceptible cells compared to wild type and diminished ability to inhibit BVDV infection, suggesting a lower affinity for BVDV receptors. We then analyzed the effect of β-hairpin mutations in the context of recombinant viral particles. Mutant viruses recovered from cell culture supernatant after transfection of recombinant RNA had almost completely inhibited ability to re-infect susceptible cells, indicating an impact of mutations on BVDV infectivity. Finally, sequential passaging of the mutant virus resulted in the selection of a viral population in which β-hairpin mutations reverted to the wild type sequence to restore infectivity. Taken together, our results show that this conserved region of the E2 protein is critical for the interaction with host cell receptors.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherMDPIes_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourceViruses 13 (6) : 1157 (2021)es_AR
dc.subjectEnfermedades de los Animaleses_AR
dc.subjectAnimal Diseaseseng
dc.subjectPestivirus de la Diarrea Bovinaes_AR
dc.subjectBovine Diarrhoea Pestiviruseng
dc.subjectPestiviruseng
dc.subjectProteínas Recombinanteses_AR
dc.subjectRecombinant Proteinseng
dc.subject.otherProteína E2es_AR
dc.subject.otherProtein E2eng
dc.subject.otherBVDVeng
dc.titleA β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Viruses_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: Merwaiss, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Merwaiss, Fernando. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Pascual, María José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Pascual, María José. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Pomilio, María Trinidad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Pomilio, María Trinidad. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Lopez, Maria Gabriela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentinaes_AR
dc.description.filFil: Lopez, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Taboga, Oscar Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentinaes_AR
dc.description.filFil: Taboga, Oscar Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Alvarez, Diego Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.description.filFil: Alvarez, Diego Ezequiel. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentinaes_AR
dc.subtypecientifico


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