ArticlePathogens (Basel, Switzerland)2021
The Capsid (ORF2) Protein of Hepatitis E Virus in Feces Is C-Terminally Truncated.
Article in Pathogens (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Monitoring of hepatitis E virus infection and replication by functional tagging of the ORF2 protein.JHEP reports : innovation in hepatology · 2025Article
- HEV ORF2 protein-antibody complex deposits are associated with glomerulonephritis in hepatitis E with reduced immune status.Nature communications · 2024Article
- Article
- Development of a HiBiT-tagged reporter hepatitis E virus and its utility as an antiviral drug screening platform.Journal of virology · 2023Article
- Three Distinct Reporter Systems of Hepatitis E Virus and Their Utility as Drug Screening Platforms.Viruses · 2023Review
- Expanding the Hepatitis E Virus Toolbox: Selectable Replicons and Recombinant Reporter Genomes.Viruses · 2023Review
- HEV Cell Culture.Advances in experimental medicine and biology · 2023Article
- Characteristics and Functions of HEV Proteins.Advances in experimental medicine and biology · 2023Article
- Hepatitis E Virus.Advances in experimental medicine and biology · 2023Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The hepatitis E virus (HEV) is a causative agent of hepatitis E. HEV virions in circulating blood and culture media are quasi-enveloped, while those in feces are nonenveloped. The capsid (ORF2) protein associated with an enveloped HEV virion is reported to comprise the translation product of leucine 14/methionine 16 to 660 (C-terminal end). However, the nature of the ORF2 protein associated with fecal HEV remains unclear. In the present study, we compared the molecular size of the ORF2 protein among fecal HEV, cell-culture-generated HEV (HEVcc), and detergent-treated protease-digested HEVcc. The ORF2 proteins associated with fecal HEV were C-terminally truncated and showed the same size as those of the detergent-treated protease-digested HEVcc virions (60 kDa), in contrast to those of the HEVcc (68 kDa). The structure prediction of the ORF2 protein (in line with previous studies) demonstrated that the C-terminal region (54 amino acids) of an ORF2 protein is in flux, suggesting that proteases target this region. The nonenveloped nondigested HEV structure prediction indicates that the C-terminal region of the ORF2 protein moves to the surface of the virion and is unnecessary for HEV infection. Our findings clarify the maturation of nonenveloped HEV and will be useful for studies on the HEV lifecycle.
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