ArticleThe Journal of biological chemistry2010
A new type of signal peptidase cleavage site identified in an RNA virus polyprotein.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Classical Swine Fever Virus Envelope Glycoproteins EBiomolecules · 2025Article
- Circular mRNA-LNP vaccine encoding self-assembled E2-TMD-mi3 nanoparticles licit enhanced CSFV-specific immunity over commercial subunit vaccine.Frontiers in immunology · 2025Article
- Computational investigation in inhibitory effects of amantadine on classical swine fever virus p7 ion channel activity.Scientific reports · 2024Article
- Fifty Shades of EViruses · 2022Article
- The Molecular Basis for EViruses · 2021Article
- Characterization of Membrane Topology and Retention Signal of Pestiviral Glycoprotein E1.Journal of virology · 2021Article
- The EViruses · 2021Article
- Article
- Recent Advances on the Bovine Viral Diarrhea Virus Molecular Pathogenesis, Immune Response, and Vaccines Development.Frontiers in veterinary science · 2021Review
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- Classical swine fever in India: current status and future perspective.Tropical animal health and production · 2018Review
- Uncoupling of ProteaseJournal of virology · 2017Article
- A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.PLoS pathogens · 2017Article
- Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Characterization of a Non-Canonical Signal Peptidase Cleavage Site in a Replication Protein from Tomato Ringspot Virus.PloS one · 2016Article
- Characterization of the Determinants of NS2-3-Independent Virion Morphogenesis of Pestiviruses.Journal of virology · 2015Article
- Review
- Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.PLoS pathogens · 2014Article
- Selection of classical swine fever virus with enhanced pathogenicity reveals synergistic virulence determinants in E2 and NS4B.Journal of virology · 2012Article
- Pestivirus virion morphogenesis in the absence of uncleaved nonstructural protein 2-3.Journal of virology · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pestiviruses, a group of enveloped positive strand RNA viruses belonging to the family Flaviviridae, express their genes via a polyprotein that is subsequently processed by proteases. The structural protein region contains typical signal peptidase cleavage sites. Only the site at the C terminus of the glycoprotein E(rns) is different because it does not contain a hydrophobic transmembrane region but an amphipathic helix functioning as the E(rns) membrane anchor. Despite the absence of a hydrophobic region, the site between the C terminus of E(rns) and E1, the protein located downstream in the polyprotein, is cleaved by signal peptidase, as demonstrated by mutagenesis and inhibitor studies. Thus, E(rns)E1 is processed at a novel type of signal peptidase cleavage site showing a different membrane topology. Prevention of glycosylation or introduction of mutations into the C-terminal region of E(rns) severely impairs processing, presumably by preventing proper membrane interaction or disturbing a conformation critical for the protein to be accepted as a substrate by signal peptidase.
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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.