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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
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dc.contributor.author | Merwaiss, Fernando | |
dc.contributor.author | Pascual, María José | |
dc.contributor.author | Pomilio, María Trinidad | |
dc.contributor.author | Lopez, Maria Gabriela | |
dc.contributor.author | Taboga, Oscar Alberto | |
dc.contributor.author | Alvarez, Diego Ezequiel | |
dc.date.accessioned | 2021-12-10T13:22:22Z | |
dc.date.available | 2021-12-10T13:22:22Z | |
dc.date.issued | 2021-06 | |
dc.identifier.issn | 1999-4915 | |
dc.identifier.other | https://doi.org/10.3390/v13061157 | |
dc.identifier.uri | http://hdl.handle.net/20.500.12123/10881 | |
dc.identifier.uri | https://www.mdpi.com/1999-4915/13/6/1157 | |
dc.description.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 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.format | application/pdf | es_AR |
dc.language.iso | eng | es_AR |
dc.publisher | MDPI | es_AR |
dc.rights | info:eu-repo/semantics/openAccess | es_AR |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | |
dc.source | Viruses 13 (6) : 1157 (2021) | es_AR |
dc.subject | Enfermedades de los Animales | es_AR |
dc.subject | Animal Diseases | eng |
dc.subject | Pestivirus de la Diarrea Bovina | es_AR |
dc.subject | Bovine Diarrhoea Pestivirus | eng |
dc.subject | Pestivirus | eng |
dc.subject | Proteínas Recombinantes | es_AR |
dc.subject | Recombinant Proteins | eng |
dc.subject.other | Proteína E2 | es_AR |
dc.subject.other | Protein E2 | eng |
dc.subject.other | BVDV | eng |
dc.title | A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus | es_AR |
dc.type | info:ar-repo/semantics/artículo | es_AR |
dc.type | info:eu-repo/semantics/article | es_AR |
dc.type | info:eu-repo/semantics/publishedVersion | es_AR |
dc.rights.license | Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) | |
dc.description.origen | Instituto de Biotecnología | es_AR |
dc.description.fil | Fil: Merwaiss, Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Merwaiss, Fernando. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Pascual, María José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Pascual, María José. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Pomilio, María Trinidad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Pomilio, María Trinidad. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Lopez, Maria Gabriela. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina | es_AR |
dc.description.fil | Fil: Lopez, Maria Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es_AR |
dc.description.fil | Fil: Taboga, Oscar Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Agrobiotecnología y Biología Molecular (IABIMO); Argentina | es_AR |
dc.description.fil | Fil: Taboga, Oscar Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina | es_AR |
dc.description.fil | Fil: Alvarez, Diego Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.description.fil | Fil: Alvarez, Diego Ezequiel. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina | es_AR |
dc.subtype | cientifico |
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