View Item
- xmlui.general.dspace_homeCentros e Institutos de InvestigaciónCICVyA. Centro de Investigación en Ciencias Veterinarias y AgronómicasInstituto de BiotecnologíaArtículos científicosxmlui.ArtifactBrowser.ItemViewer.trail
- DSpace Home
- Centros e Institutos de Investigación
- CICVyA. Centro de Investigación en Ciencias Veterinarias y Agronómicas
- Instituto de Biotecnología
- Artículos científicos
- View Item
A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus
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...]
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.
[Cerrar]
Author
Merwaiss, Fernando;
Pascual, María José;
Pomilio, María Trinidad;
Lopez, Maria Gabriela;
Taboga, Oscar Alberto;
Alvarez, Diego Ezequiel;
Fuente
Viruses 13 (6) : 1157 (2021)
Date
2021-06
Editorial
MDPI
ISSN
1999-4915
Formato
pdf
Tipo de documento
artículo
Palabras Claves
Derechos de acceso
Abierto
Excepto donde se diga explicitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)