ArticleVirology journal2006
Expression and processing of the Hepatitis E virus ORF1 nonstructural polyprotein.
Article in Virology journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 91 citations in OpenAlex.
- Molecular epidemiological investigation of swine hepatitis e virus (sHEV) in Guangdong Province, China: prevalence, genotypic characteristics, and zoonotic risk.BMC veterinary research · 2026Article
- EIF4H and YBX1 are essential host factors for hepatitis E virus replication and pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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- Hepatitis E Virus ORF1 Polyprotein Harbors a Pocket-Like Cavity That Is Vital for Virus Replication and Represents a Novel Antiviral Target.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Viral helicase and methyltransferase promote genotype one-hepatitis e virus internal ribosome entry site-like element activity.Npj viruses · 2025Article
- Hepatitis E and Potential Public Health Implications from a One-Health Perspective: Special Focus on the European Wild Boar (Pathogens (Basel, Switzerland) · 2024Review
- Hepatitis E Virus: What More Do We Need to Know?Medicina (Kaunas, Lithuania) · 2024Review
- The hepatitis E virus ORF1 hypervariable region confers partial cyclophilin dependency.The Journal of general virology · 2023Article
- Thrombin cleavage of the hepatitis E virus polyprotein at multiple conserved locations is required for genome replication.PLoS pathogens · 2023Article
- Hepatitis E Virus Protease Inhibits the Activity of Eukaryotic Initiation Factor 2-Alpha Kinase 4 and Promotes Virus Survival.Journal of virology · 2023Article
- Article
- Puzzles for Hepatitis E Virus.Advances in experimental medicine and biology · 2023Article
- Hepatitis E Virus Life Cycle.Advances in experimental medicine and biology · 2023Article
- Characteristics and Functions of HEV Proteins.Advances in experimental medicine and biology · 2023Article
- Structural aspects of hepatitis E virus.Archives of virology · 2022Review
- Article
- Cellular Organelles Involved in Hepatitis E Virus Infection.Pathogens (Basel, Switzerland) · 2021Review
- Virus-Host Cell Interplay during Hepatitis E Virus Infection.Trends in microbiology · 2021Review
- Identification of the interferon-inducible GTPase GBP1 as major restriction factor for the Hepatitis E virus.Journal of virology · 2021Article
- Advances in Hepatitis E Virus Biology and Pathogenesis.Viruses · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe ORF1 of hepatitis E virus (HEV) encodes a nonstructural polyprotein of approximately 186 kDa that has putative domains for four enzymes: a methyltransferase, a papain-like cysteine protease, a RNA helicase and a RNA dependent RNA polymerase. In the absence of a culture system for HEV, the ORF1 expressed using bacterial and mammalian expression systems has shown an approximately 186 kDa protein, but no processing of the polyprotein has been observed. Based on these observations, it was proposed that the ORF1 polyprotein does not undergo processing into functional units. We have studied ORF1 polyprotein expression and processing through a baculovirus expression vector system because of the high level expression and post-translational modification abilities of this system.
resultsThe baculovirus expressed ORF1 polyprotein was processed into smaller fragments that could be detected using antibodies directed against tags engineered at both ends. Processing of this approximately 192 kDa tagged ORF1 polyprotein and accumulation of lower molecular weight species took place in a time-dependent manner. This processing was inhibited by E-64d, a cell-permeable cysteine protease inhibitor. MALDI-TOF analysis of a 35 kDa processed fragment revealed 9 peptide sequences that matched the HEV methyltransferase (MeT), the first putative domain of the ORF1 polyprotein. Antibodies to the MeT region also revealed an ORF1 processing pattern identical to that observed for the N-terminal tag.
conclusionWhen expressed through baculovirus, the ORF1 polyprotein of HEV was processed into smaller proteins that correlated with their proposed functional domains. Though the involvement of non-cysteine protease(s) could not be be ruled out, this processing mainly depended upon a cysteine protease.
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