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Article

A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus

1
Instituto de Investigaciones Biotecnológicas (IIB), Universidad Nacional de San Martín (UNSAM), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires B1650HMR, Argentina
2
Instituto de Agrobiotecnología y Biología Molecular (IABIMO), Instituto Nacional de Tecnología Agropecuaria (INTA), CONICET, Buenos Aires B1686IGC, Argentina
*
Author to whom correspondence should be addressed.
These authors equally contributed to the work.
Academic Editors: Paul Becher, Nicolas Ruggli and Norbert Tautz
Viruses 2021, 13(6), 1157; https://doi.org/10.3390/v13061157
Received: 7 May 2021 / Revised: 9 June 2021 / Accepted: 10 June 2021 / Published: 17 June 2021
(This article belongs to the Special Issue Advances in Pestivirus Research)
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. View Full-Text
Keywords: pestivirus; entry; virus-receptor interaction pestivirus; entry; virus-receptor interaction
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MDPI and ACS Style

Merwaiss, F.; Pascual, M.J.; Pomilio, M.T.; Lopez, M.G.; Taboga, O.A.; Alvarez, D.E. A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus. Viruses 2021, 13, 1157. https://doi.org/10.3390/v13061157

AMA Style

Merwaiss F, Pascual MJ, Pomilio MT, Lopez MG, Taboga OA, Alvarez DE. A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus. Viruses. 2021; 13(6):1157. https://doi.org/10.3390/v13061157

Chicago/Turabian Style

Merwaiss, Fernando, María J. Pascual, María T. Pomilio, María G. Lopez, Oscar A. Taboga, and Diego E. Alvarez. 2021. "A β-Hairpin Motif in the Envelope Protein E2 Mediates Receptor Binding of Bovine Viral Diarrhea Virus" Viruses 13, no. 6: 1157. https://doi.org/10.3390/v13061157

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