ArticleJournal of virology1998
Processing of proteinase precursors and their effect on hepatitis A virus particle formation.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Identification and P1 genetic evolutionary analysis of duck hepatitis a virus type 3 in selected areas of Jiangsu, China in 2024.Poultry science · 2026Article
- Isolation, characterization and whole-genome analysis of a potentially novel strain of duck hepatitis A virus type 3 from a vaccinated duck flock in China.Frontiers in microbiology · 2026Article
- Hepatovirus infections in juvenile seals from the North Sea.Npj viruses · 2025Article
- Hepatitis A virus infection.Nature reviews. Disease primers · 2023Review
- Insights into Polyprotein Processing and RNA-Protein Interactions in Foot-and-Mouth Disease Virus Genome Replication.Journal of virology · 2023Article
- Pathogenicity and virulence of hepatitis A virus.Virulence · 2021Review
- Article
- Hepatitis A Virus Genome Organization and Replication Strategy.Cold Spring Harbor perspectives in medicine · 2018Review
- The Strategy of Picornavirus Evading Host Antiviral Responses: Non-structural Proteins Suppress the Production of IFNs.Frontiers in microbiology · 2018Review
- Induction and Suppression of Innate Antiviral Responses by Hepatitis A Virus.Frontiers in microbiology · 2018Review
- Structures and Corresponding Functions of Five Types of Picornaviral 2A Proteins.Frontiers in microbiology · 2017Review
- Coxsackievirus B3 protease 3C: expression, purification, crystallization and preliminary structural insights.Acta crystallographica. Section F, Structural biology communications · 2016Article
- Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis A virus protease-polymerase processing intermediate, 3CD.PLoS pathogens · 2011Article
- Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Poly(A) binding protein, C-terminally truncated by the hepatitis A virus proteinase 3C, inhibits viral translation.Nucleic acids research · 2007Article
- Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization.The Biochemical journal · 2005Article
- Full-length genome of wild-type hepatitis A virus (DL3) isolated in China.World journal of gastroenterology · 2003Article
- Hepatitis A virus inhibits cellular antiviral defense mechanisms induced by double-stranded RNA.Journal of virology · 2002Article
- Foodborne viruses.FEMS microbiology reviews · 2002Review
- Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC.Journal of virology · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proteolytic processing of the picornaviral polyprotein mediated by the differential action of virus-encoded proteinase(s) is pivotal to both RNA genome replication and capsid formation. Possibly to enlarge the array of viral proteins, picornaviral polyprotein processing results in intermediate and mature products which apparently have distinct functions within the viral life cycle. For hepatitis A virus (HAV), we report here on the autoproteolysis of precursor polypeptides comprising the only viral proteinase, 3Cpro, and on their role in viral particle formation. Following transient expression of a nested set of 3Cpro-containing proteins (P3, 3ABC, 3BCD, 3CD, 3BC, and 3C) in eukaryotic cells, the extent of processing was determined by analyzing the cleavage products. The 3C/3D site was more efficiently cleaved than those at the 3A/3B and 3B/3C sites, leading to the accumulation of the intermediate product 3ABC. In the absence of 3A from the precursor, cleavage at the 3B/3C site was further reduced and a switch to an alternative 3C/3D site was observed. Coexpression of various parts of P3 with the precursor of the viral structural proteins P1-2A showed that all 3C-containing intermediates cleaved P1-2A with almost equal efficiency; however, viral particles carrying the neutralizing epitope form much more readily in the presence of the complete P3 domain than with parts of it. These data support the notion that efficient liberation of structural proteins from P1-2A is necessary but not sufficient for productive HAV capsid formation and suggest that the polypeptides flanking 3Cpro promote the assembly of viral particles.
Indexed as
Identifiers
What OpenQuestion holds
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.