ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Expression, purification and crystallization of the ectodomain of the envelope glycoprotein E2 from Bovine viral diarrhoea virus.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular Characteristics and Pathogenicity Analysis of Bovine Viral Diarrhea Virus Strain Isolated from Persistently Infected Cattle.Animals : an open access journal from MDPI · 2026Article
- 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
- Alteration of a Second Putative Fusion Peptide of Structural Glycoprotein E2 of Classical Swine Fever Virus Alters Virus Replication and Virulence in Swine.Journal of virology · 2016Article
- Review
- Interaction of CSFV E2 protein with swine host factors as detected by yeast two-hybrid system.PloS one · 2014Article
- Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry.Cell reports · 2013Article
Corrections and comments
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
Abstract
Bovine viral diarrhoea virus (BVDV) is an economically important animal pathogen which is closely related to Hepatitis C virus. Of the structural proteins, the envelope glycoprotein E2 of BVDV is the major antigen which induces neutralizing antibodies; thus, BVDV E2 is considered as an ideal target for use in subunit vaccines. Here, the expression, purification of wild-type and mutant forms of the ectodomain of BVDV E2 and subsequent crystallization and data collection of two crystal forms grown at low and neutral pH are reported. Native and multiple-wavelength anomalous dispersion (MAD) data sets have been collected and structure determination is in progress.
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