ArticleScientific reports2023
Immunogenicity of a secreted, C-terminally truncated, form of bovine viral diarrhea virus E2 glycoprotein as a potential candidate in subunit vaccine development.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Construction and Immunogenicity of Modified Vaccinia Ankara (MVA) Viruses Expressing E1 and E2 Proteins of Bovine Viral Diarrhea Virus.Vaccines · 2026Article
- Bovine Viral Diarrhea Virus and Vaccine Protection Strategies.Veterinary sciences · 2026Review
- Novel BPI3Vc-vectored chimeric BVDV antigens elicit broadly neutralizing antibodies in cattle.Frontiers in immunology · 2026Article
- A Novel Trivalent BVDV mRNA Vaccine Displayed by Virus-like Particles Eliciting Potent and Broad-Spectrum Antibody Responses.Vaccines · 2025Article
- Molecular epidemiology and immunopathogenesis of bovine viral diarrhea virus: a growing threat to regional cattle industry of Xinjiang, China.Frontiers in microbiology · 2025Review
- Preclinical Efficacy of Cap-Dependent and Independent mRNA Vaccines against Bovine Viral Diarrhea Virus-1.Veterinary sciences · 2024Article
- Recombinant Subunit Vaccine Candidate against the Bovine Viral Diarrhea Virus.International journal of molecular sciences · 2024Article
- Immune protection induced by E2 recombinant glycoprotein of bovine viral diarrhea virus in a murine model.Frontiers in veterinary science · 2023Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Both current live, attenuated, and killed virus vaccines for bovine viral diarrhea virus (BVDV) have their limitations. Here, we report the development of a BVDV subunit vaccine by (i) the expression of a secreted form of a recombinant E2 glycoprotein using BHK21 cells and (ii) determination of the immune responses in mice. The E2 glycoprotein was modified by deletion of the C-terminal transmembrane anchor domain and fusion to a V5 epitope tag. This allowed detection using anti-V5 monoclonal antibodies together with simple purification of the expressed, secreted, form of E2 from the cell media. Furthermore, we genetically fused green fluorescent protein (GFP) linked to E2 via a Thosea asigna virus 2A (T2A) ribosome skipping sequence thereby creating a self-processing polyprotein [GFP-T2A-BVDV-E2
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.