ArticleJournal of virology2011
Biosynthesis of classical swine fever virus nonstructural proteins.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 95 citations in OpenAlex.
- SUMOylation-dependent degradation of nucleocapsid is responsible forJournal of virology · 2025Article
- Classical swine fever virus hijacks ESCRT-III and VPS4A to promote phagophore closure for accelerating mitophagy.Autophagy · 2025Article
- AlphaFold Prediction of Protein-Protein Interactions in theInternational journal of molecular sciences · 2025Article
- Deciphering the membrane topology of the pestiviral non-structural protein 4B (NS4B).Journal of virology · 2025Article
- Comparison of Viral RNA Extraction Protocols for Senecavirus A and Classical Swine Fever Virus.Folia microbiologica · 2025Article
- 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
- Essential role ofJournal of virology · 2025Article
- Maternal and protective antibody responses to E2 subunit and C-strain classical swine fever vaccines in piglets: a comparative analysis.Frontiers in veterinary science · 2025Article
- Transcriptome analysis of 3D4/21 cells expressing CSFV NS4B.Frontiers in microbiology · 2025Article
- Exclusion of Superinfection or Enhancement of Superinfection in Pestiviruses-APPV Infection Is Not Dependent on ADAM17.Viruses · 2024Article
- Computational investigation in inhibitory effects of amantadine on classical swine fever virus p7 ion channel activity.Scientific reports · 2024Article
- Host cell factors involved in classical swine fever virus entry.Veterinary research · 2023Review
- Packaging defects in pestiviral NS4A can be compensated by mutations in NS2 and NS3.Journal of virology · 2023Article
- A Genetically Engineered Bivalent Vaccine Coexpressing a Molecular Adjuvant against Classical Swine Fever and Porcine Epidemic Diarrhea.International journal of molecular sciences · 2023Article
- Kinesin-1 Regulates Endocytic Trafficking of Classical Swine Fever Virus along Acetylated Microtubules.Journal of virology · 2023Article
- Transcriptome analysis of PK-15 cells expressing CSFV NS4A.BMC veterinary research · 2022Article
- The NS4A Protein of Classical Swine Fever Virus Suppresses RNA Silencing in Mammalian Cells.Journal of virology · 2022Article
- DNAJC14-Independent Replication of the Atypical Porcine Pestivirus.Journal of virology · 2022Article
- Article
- Fatty Acid Synthase Is Involved in Classical Swine Fever Virus Replication by Interaction with NS4B.Journal of virology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolytic processing of polyproteins is considered a crucial step in the life cycle of most positive-strand RNA viruses. An enhancement of NS2-3 processing has been described as a major difference between the noncytopathogenic (non-CP) and the cytopathogenic (CP) biotypes of pestiviruses. The effects of accelerated versus delayed NS2-3 processing on the maturation of the other nonstructural proteins (NSP) have never been compared. In this study, we analyzed the proteolytic processing of NSP in Classical swine fever virus (CSFV). Key to the investigation was a panel of newly developed monoclonal antibodies (MAbs) that facilitated monitoring of all nonstructural proteins involved in virus replication (NS2, NS3, NS4A, NS5A, and NS5B). Applying these MAbs in Western blotting and radioimmunoprecipitation allowed an unambiguous identification of the mature proteins and precursors in non-CP CSFV-infected cells. Furthermore, the kinetics of processing were determined by pulse-chase analyses for non-CP CSFV, CP CSFV, and a CP CSFV replicon. A slow but constant processing of NS4A/B-5A/B occurred in non-CP CSFV-infected cells, leading to balanced low-level concentrations of mature NSP. In contrast, the turnover of the polyprotein precursors was three times faster in CP CSFV-infected cells and in cells transfected with a CP CSFV replicon, causing a substantial increase of mature NSP concentrations. We conclude that a delayed processing not only of NS3 but further of all NSP represents a hallmark of regulation in non-CP pestiviruses.
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