ArticleJournal of virology2005
The carboxy-terminal sequence of the pestivirus glycoprotein E(rns) represents an unusual type of membrane anchor.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- First Identification, Recombinant Production, and Structural Characterization of a Putative Structural Protein from the Haseki Tick Virus Polyprotein.Biomolecules · 2025Article
- Host cell factors involved in classical swine fever virus entry.Veterinary research · 2023Review
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- Fifty Shades of EViruses · 2022Article
- A double deletion prevents replication of the pestivirus bovine viral diarrhea virus in the placenta of pregnant heifers.PLoS pathogens · 2021Article
- The Molecular Basis for EViruses · 2021Article
- The EViruses · 2021Article
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- Generation and immunogenicity analysis of recombinant classical swine fever virus glycoprotein E2 and EVirology journal · 2021Article
- BoHV-1-Vectored BVDV-2 Subunit Vaccine Induces BVDV Cross-Reactive Cellular Immune Responses and Protects against BVDV-2 Challenge.Vaccines · 2021Article
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- Autonomously Replicating RNAs of Bungowannah Pestivirus: EJournal of virology · 2020Article
- Article
- Glycoprotein 3 of Porcine Reproductive and Respiratory Syndrome Virus Exhibits an Unusual Hairpin-Like Membrane Topology.Journal of virology · 2018Article
- Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Scientific reports · 2018Article
- In vitro adaptation and genome analysis of a sub-subgenotype 2.1c isolate of classical swine fever virus.Virus genes · 2016Article
- What can pestiviral endonucleases teach us about innate immunotolerance?Cytokine & growth factor reviews · 2016Review
- Review
- Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns.PloS one · 2015Article
- Immune Responses Against Classical Swine Fever Virus: Between Ignorance and Lunacy.Frontiers in veterinary science · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The E(rns) protein is a structural glycoprotein of pestiviruses that lacks a typical membrane anchor sequence and is known to be secreted from the infected cell. However, major amounts of the protein are retained within the cell and attached to the virion by a so far unknown mechanism. Transient-expression studies with cDNA constructs showed that in a steady-state situation, 16% of the protein is found in the supernatant of the transfected cells while 84% appears as intracellular protein. We show here that E(rns) represents a membrane-bound protein. Membrane binding occurs via the carboxy-terminal region of E(rns). By fusion of this sequence to the carboxy terminus of green fluorescent protein (GFP), the subcellular localization of the reporter protein switched from cytosolic to membrane bound. A core sequence of 11 amino acids necessary for membrane binding was elicited in truncation experiments with GFP constructs. However, this peptide is not sufficient to confer membrane anchoring but needs either upstream or downstream accessory sequences. Analyses with different extraction procedures showed that E(rns) is neither easily stripped from the membrane, like a peripheral membrane protein, nor as tightly membrane bound as a transmembrane protein.
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Registered trials
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