ArticleThe Journal of biological chemistry2015
A Cell-based Fluorescence Resonance Energy Transfer (FRET) Sensor Reveals Inter- and Intragenogroup Variations in Norovirus Protease Activity and Polyprotein Cleavage.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Viral protease-mediated polyprotein processing in human astroviruses.Npj viruses · 2026Article
- Article
- Molecular mechanisms of protease precursor autoprocessing of RNA viruses: a comprehensive review.Virology journal · 2026Review
- Chronic persistent Norovirus in the immune-compromised host.Current opinion in infectious diseases · 2025Review
- Development of a replication competent murine norovirus reporter system.PLoS pathogens · 2025Article
- Assessment of optimized FRET substrates as universal corona- and picornavirus main protease substrates for screening assays.RSC advances · 2024Article
- Selective Polyprotein Processing Determines Norovirus Sensitivity to Trim7.Journal of virology · 2022Article
- The proximal proteome of 17 SARS-CoV-2 proteins links to disrupted antiviral signaling and host translation.PLoS pathogens · 2021Article
- Characterising proteolysis during SARS-CoV-2 infection identifies viral cleavage sites and cellular targets with therapeutic potential.Nature communications · 2021Article
- A Novel Class of Norovirus Inhibitors Targeting the Viral Protease with Potent Antiviral Activity In Vitro and In Vivo.Viruses · 2021Article
- Murine norovirus virulence factor 1 (VF1) protein contributes to viral fitness during persistent infection.The Journal of general virology · 2021Article
- The proximal proteome of 17 SARS-CoV-2 proteins links to disrupted antiviral signaling and host translation.bioRxiv : the preprint server for biology · 2021Article
- Resonance Energy Transfer-Based Biosensors for Point-of-Need Diagnosis-Progress and Perspectives.Sensors (Basel, Switzerland) · 2021Review
- Single-particle virology.Biophysical reviews · 2020Review
- Novel biosensor platforms for the detection of coronavirus infection and severe acute respiratory syndrome coronavirus 2.Journal of the Chinese Medical Association : JCMA · 2020Article
- Norovirus infection results in eIF2α independent host translation shut-off and remodels the G3BP1 interactome evading stress granule formation.PLoS pathogens · 2020Article
- Polyprotein processing and intermolecular interactions within the viral replication complex spatially and temporally control norovirus protease activity.The Journal of biological chemistry · 2019Article
- Structural and Antiviral Studies of the Human Norovirus GII.4 Protease.Biochemistry · 2019Article
- Selection and Characterization of Rupintrivir-Resistant Norwalk Virus Replicon CellsAntimicrobial agents and chemotherapy · 2018Article
- Concepts in Light Microscopy of Viruses.Viruses · 2018Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The viral protease represents a key drug target for the development of antiviral therapeutics. Because many protease inhibitors mimic protease substrates, differences in substrate recognition between proteases may affect their sensitivity to a given inhibitor. Here we use a cell-based FRET sensor to investigate the activity of different norovirus proteases upon cleavage of various norovirus cleavage sites inserted into a linker region separating cyan fluorescent protein and yellow fluorescent protein. Using this system, we demonstrate that differences in substrate processing exist between proteases from human noroviruses (genogroups I (GI) and II) and the commonly used murine norovirus (MNV, genogroup V) model. These altered the cleavage efficiency of specific cleavage sites both within and between genogroups. The differences observed between these proteases may affect sensitivity to protease inhibitors and the suitability of MNV as a model system for testing such molecules against the human norovirus protease. Finally, we demonstrate that replacement of MNV polyprotein cleavage sites with the GI or GII equivalents, with the exception of the NS6-7 junction, leads to the production of infectious virus when the MNV NS6 protease, but not the GI or GII proteases, are present.
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Registered trials
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.