ArticlePLoS pathogens2014
Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Structural and electrostatic determinants of RNA recognition by the CSFV Erns glycoprotein.Archives of virology · 2026Article
- A Novel Bicistronic Adenovirus Vaccine Elicits Superior and Comprehensive Protection Against BVDV.Microorganisms · 2026Article
- Review
- Fifty Shades of EViruses · 2022Article
- Viral Traits and Cellular Knock-Out Genotype Affect Dependence of BVDV on Bovine CD46.Pathogens (Basel, Switzerland) · 2021Article
- 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
- Advanced Solid State Nano-Electrochemical Sensors and System for Agri 4.0 Applications.Sensors (Basel, Switzerland) · 2021Article
- Article
- Generation and immunogenicity analysis of recombinant classical swine fever virus glycoprotein E2 and EVirology journal · 2021Article
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- Review
- Autonomously Replicating RNAs of Bungowannah Pestivirus: EJournal of virology · 2020Article
- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- 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
- Complex Virus-Host Interactions Involved in the Regulation of Classical Swine Fever Virus Replication: A Minireview.Viruses · 2017Review
- Host-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of Flaviviridae.PLoS pathogens · 2017Article
- What can pestiviral endonucleases teach us about innate immunotolerance?Cytokine & growth factor reviews · 2016Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding properties of this sequence to gain a better understanding of the underlying mechanisms. CD spectroscopy in different setups, as well as Monte Carlo and molecular dynamics simulations confirmed the helical folding and showed that the helix is accommodated in the amphiphilic region of the lipid bilayer with a slight tilt rather than lying parallel to the surface. This model was confirmed by NMR analyses that also identified a central stretch of 15 residues within the helix that is fully shielded from the aqueous layer, which is C-terminally followed by a putative hairpin structure. These findings explain the strong membrane binding of the protein and provide clues to establishing the E(rns) membrane contact, processing and secretion.
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