ArticleJournal of virology2003
In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 150 citations in OpenAlex.
- The MNV-1 protease-polymerase precursor cleaves a novel site in the NS1-2 protein.The Journal of general virology · 2026Article
- Molecular mechanisms of protease precursor autoprocessing of RNA viruses: a comprehensive review.Virology journal · 2026Review
- Activity and cryo-EM structure of the polymerase domain of the human norovirus ProPol precursor.Journal of virology · 2024Article
- Article
- Structural Investigations on Novel Non-Nucleoside Inhibitors of Human Norovirus Polymerase.Viruses · 2022Article
- Norovirus GII.2[P16] strain in Shenzhen, China: a retrospective study.BMC infectious diseases · 2021Article
- Human Norovirus NTPase Antagonizes Interferon-β Production by Interacting With IkB Kinase ε.Frontiers in microbiology · 2021Article
- Human Norovirus Proteins: Implications in the Replicative Cycle, Pathogenesis, and the Host Immune Response.Frontiers in immunology · 2020Review
- GII.4 Norovirus Protease Shows pH-Sensitive Proteolysis with a Unique Arg-His Pairing in the Catalytic Site.Journal of virology · 2019Article
- Therapeutics and Immunoprophylaxis Against Noroviruses and Rotaviruses: The Past, Present, and Future.Current drug metabolism · 2018Review
- Membrane alterations induced by nonstructural proteins of human norovirus.PLoS pathogens · 2017Article
- Structure(s), function(s), and inhibition of the RNA-dependent RNA polymerase of noroviruses.Virus research · 2017Review
- Norovirus-Mediated Modification of the Translational Landscape via Virus and Host-Induced Cleavage of Translation Initiation Factors.Molecular & cellular proteomics : MCP · 2017Article
- A Proposal for a Structural Model of the Feline Calicivirus Protease Bound to the Substrate Peptide under Physiological Conditions.Frontiers in microbiology · 2017Article
- Current tools for norovirus drug discovery.Expert opinion on drug discovery · 2016Review
- Article
- A Conserved Interaction between a C-Terminal Motif in Norovirus VPg and the HEAT-1 Domain of eIF4G Is Essential for Translation Initiation.PLoS pathogens · 2016Article
- A Cell-based Fluorescence Resonance Energy Transfer (FRET) Sensor Reveals Inter- and Intragenogroup Variations in Norovirus Protease Activity and Polyprotein Cleavage.The Journal of biological chemistry · 2015Article
- Development of enhanced primer sets for detection of norovirus.BioMed research international · 2015Article
- Comprehensive review of human sapoviruses.Clinical microbiology reviews · 2015Review
14 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The MD145-12 strain (GII/4) is a member of the genus Norovirus in the Caliciviridae and was detected in a patient with acute gastroenteritis in a Maryland nursing home. The open reading frame 1 (ORF1) (encoding the nonstructural polyprotein) was cloned as a consensus sequence into various expression vectors, and a proteolytic cleavage map was determined. The virus-encoded cysteine proteinase mediated at least five cleavages (Q(330)/G(331), Q(696)/G(697), E(875)/G(876), E(1008)/A(1009), and E(1189)/G(1190)) in the ORF1 polyprotein in the following order: N-terminal protein; nucleoside triphosphatase; 20-kDa protein (p20); virus protein, genome linked (VPg); proteinase (Pro); polymerase (Pol). A time course analysis of proteolytic processing of the MD145-12 ORF1 polyprotein in an in vitro coupled transcription and translation assay allowed the identification of stable precursors and final mapped cleavage products. Stable precursors included p20VPg (analogous to the 3AB of the picornaviruses) and ProPol (analogous to the 3CD of the picornaviruses). Less stable processing intermediates were identified as p20VPgProPol, p20VPgPro, and VPgPro. The MD145-12 Pro and ProPol proteins were expressed in bacteria as active forms of the proteinase and used to further characterize their substrate specificities in trans cleavage assays. The MD145-12 Pro was able to cleave its five mapped cleavage sites in trans and, in addition, could mediate trans cleavage of the Norwalk virus (GI/I) ORF1 polyprotein into a similar proteolytic processing profile. Taken together, our data establish a model for proteolytic processing in the noroviruses that is consistent with nonstructural precursors and products identified in studies of caliciviruses that replicate in cell culture systems.
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Registered trials
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