ArticleJournal of virology2013
Autocatalytic cleavage within classical swine fever virus NS3 leads to a functional separation of protease and helicase.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Review
- Exclusion of Superinfection or Enhancement of Superinfection in Pestiviruses-APPV Infection Is Not Dependent on ADAM17.Viruses · 2024Article
- Article
- LDHB inhibition induces mitophagy and facilitates the progression of CSFV infection.Autophagy · 2021Article
- Characterization of a Cytopathogenic Reporter CSFV.Viruses · 2021Article
- A positively charged surface patch on the pestivirus NS3 protease module plays an important role in modulating NS3 helicase activity and virus production.Archives of virology · 2021Article
- Review
- Clinical and Serological Evaluation of LINDA Virus Infections in Post-Weaning Piglets.Viruses · 2019Article
- Classical swine fever virus non-structural protein 4B binds tank-binding kinase 1.Journal of biosciences · 2018Article
- Targeting intramolecular proteinase NS2B/3 cleavages forProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Uncoupling of ProteaseJournal of virology · 2017Article
- TRAF6 is a novel NS3-interacting protein that inhibits classical swine fever virus replication.Scientific reports · 2017Article
- Novel Pestivirus Species in Pigs, Austria, 2015.Emerging infectious diseases · 2017Article
- Molecular chaperone Jiv promotes the RNA replication of classical swine fever virus.Virus genes · 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
- Congenital infection with atypical porcine pestivirus (APPV) is associated with disease and viral persistence.Veterinary research · 2017Article
- X-ray structure of the pestivirus NS3 helicase and its conformation in solution.Journal of virology · 2015Article
- Npro of classical swine fever virus contributes to pathogenicity in pigs by preventing type I interferon induction at local replication sites.Veterinary research · 2014Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Classical swine fever virus (CSFV) is a positive-stranded RNA virus belonging to the genus Pestivirus within the Flaviviridae family. Pivotal for processing of a large portion of the viral polyprotein is a serine protease activity within nonstructural protein 3 (NS3) that also harbors helicase and NTPase activities essential for RNA replication. In CSFV-infected cells, NS3 appears as two forms, a fully processed NS3 of 80 kDa and the precursor molecule NS2-3 of 120 kDa. Here we report the identification and mapping of additional autocatalytic intramolecular cleavages. One cleavable peptide bond occurs between Leu1781 and Met1782, giving rise to a helicase subunit of 55 kDa and, depending on the substrate, a NS2-3 fragment of 78 kDa (NS2-3p) or a NS3 protease subunit of 26 kDa (NS3p). In trans-cleavage assays using NS4-5 as a substrate, NS3p acts as a fully functional protease that is able to process the polyprotein. NS3p comprises the minimal essential protease, as deletion of Leu1781 results in inactivation. A second intramolecular cleavage was mapped to the Leu1748/Lys1749 peptide bond that yields a proteolytically inactive NS3 fragment. Deletion of either of the cleavage site residues resulted in a loss of RNA infectivity, indicating the functional importance of amino acid identity at the respective positions. Our data suggest that internal cleavage within the NS3 moiety is a common process that further extends the functional repertoires of the multifunctional NS2-3 or NS3 and represents another level of the complex polyprotein processing of Flaviviridae.
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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.