ArticleProceedings of the National Academy of Sciences of the United States of America2013
Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Generation and epitope mapping of two distinct neutralizing mAb subsets targeting BVDV E2: a pan-pestivirus cross-reactive linear epitope and a BVDV-specific conformational epitope.Veterinary research · 2026Article
- Molecular Characteristics and Pathogenicity Analysis of Bovine Viral Diarrhea Virus Strain Isolated from Persistently Infected Cattle.Animals : an open access journal from MDPI · 2026Article
- Isolation and identification of a potential new bovine viral diarrhea virus genotype associated with severe outbreaks in yaks (Frontiers in microbiology · 2026Article
- A Novel Trivalent BVDV mRNA Vaccine Displayed by Virus-like Particles Eliciting Potent and Broad-Spectrum Antibody Responses.Vaccines · 2025Article
- Isolation and Pathogenicity of an Emerging Highly Virulent CSFV 2.1c Strain in South China.Veterinary sciences · 2025Article
- Molecular detection and genotyping of bovine viral diarrhea virus in four provinces of China.Archives of virology · 2025Article
- Virus-neutralizing monoclonal antibodies against bovine viral diarrhea virus and classical swine fever virus target conformational and linear epitopes on E2 glycoprotein subdomains.Microbiology spectrum · 2025Article
- Article
- Exclusion of Superinfection or Enhancement of Superinfection in Pestiviruses-APPV Infection Is Not Dependent on ADAM17.Viruses · 2024Article
- Article
- Determinants of pegivirus persistence, cross-species infection, and adaptation in the laboratory mouse.PLoS pathogens · 2024Article
- Genetic analyses of the structural protein E2 bovine viral diarrhea virus isolated from dairy cattle in Yogyakarta, Indonesia.Veterinary world · 2024Article
- hsa-miR-548d-3p: a potential microRNA to target nucleocapsid and/or capsid genes in multiple members of the Flaviviridae family.Frontiers in bioinformatics · 2024Article
- Article
- Rice-produced classical swine fever virus glycoprotein E2 with herringbone-dimer design to enhance immune responses.Plant biotechnology journal · 2023Article
- Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism.PLoS biology · 2023Article
- Evaluation of the Mucosal Immunity Effect of Bovine Viral Diarrhea Virus Subunit Vaccine E2Fc and E2Ft.International journal of molecular sciences · 2023Article
- Immune evasion strategies of bovine viral diarrhea virus.Frontiers in cellular and infection microbiology · 2023Review
- Review
- Isolation of BVDV-1a, 1m, and 1v strains from diarrheal calf in china and identification of its genome sequence and cattle virulence.Frontiers in veterinary science · 2022Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
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Abstract
Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome into the host cell cytoplasm by fusion of their envelope with a cellular membrane. The crystal structure of bovine viral diarrhea virus E2 reveals a unique protein architecture consisting of two Ig-like domains followed by an elongated β-stranded domain with a new fold. E2 forms end-to-end homodimers with a conserved C-terminal motif rich in aromatic residues at the contact. A disulfide bond across the interface explains the acid resistance of pestiviruses and their requirement for a redox activation step to initiate fusion. From the structure of E2, we propose alternative possible membrane fusion mechanisms. We expect the pestivirus fusion apparatus to be conserved in hepatitis C virus.
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