ArticleScientific reports2019
New insights into the ORF2 capsid protein, a key player of the hepatitis E virus lifecycle.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 63 citations in OpenAlex.
- Extra-Hepatic Manifestations of Hepatitis E Virus (HEV): A Narrative Review on Meningoencephalitis.Life (Basel, Switzerland) · 2026Review
- Unraveling a mechanism underlying hepatitis E-associated kidney disease : Discovery of HEV ORF2 capsid protein-associated immune complex glomerulonephritis.Pathologie (Heidelberg, Germany) · 2026Article
- The hepatitis E virus capsid protein ORF2 counteracts cell-intrinsic antiviral responses to enable persistent replication in cell culture.PLoS pathogens · 2025Article
- Plasmacytoid dendritic cell sensing of hepatitis E virus is shaped by both viral and host factors.Life science alliance · 2025Article
- Monitoring of hepatitis E virus infection and replication by functional tagging of the ORF2 protein.JHEP reports : innovation in hepatology · 2025Article
- Broadly neutralizing antibodies isolated from HEV convalescents confer protective effects in human liver-chimeric mice.Nature communications · 2025Article
- Effect of Hepatitis E Virus on the Male Reproductive System: A Review of Current Evidence.Viruses · 2025Review
- Cell line-dependent release of quasi-enveloped hepatitis E virus reveals alternative Golgi-associated egress in the absence of pORF3.Frontiers in cellular and infection microbiology · 2025Article
- Cell binding tropism of rat hepatitis E virus is a pivotal determinant of its zoonotic transmission to humans.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- HEV ORF2 protein-antibody complex deposits are associated with glomerulonephritis in hepatitis E with reduced immune status.Nature communications · 2024Article
- Hepatitis E and Potential Public Health Implications from a One-Health Perspective: Special Focus on the European Wild Boar (Pathogens (Basel, Switzerland) · 2024Review
- The AP-1 adaptor complex is essential for intracellular trafficking of the ORF2 capsid protein and assembly of Hepatitis E virus.Cellular and molecular life sciences : CMLS · 2024Article
- Hepatitis E Virus: What More Do We Need to Know?Medicina (Kaunas, Lithuania) · 2024Review
- Characterization of virus‒host recombinant variants of the hepatitis E virus.Journal of virology · 2024Article
- Article
- Molecular identification and genotyping of hepatitis E virus from Southern Punjab, Pakistan.Scientific reports · 2024Article
- Hepatitis E virus neutralization by porcine serum antibodies.Journal of clinical microbiology · 2023Article
- Review
- Intrinsic disorder in the open reading frame 2 of hepatitis E virus: a protein with multiple functions beyond viral capsid.Journal, genetic engineering & biotechnology · 2023Article
- Genetic Evolution of Hepatitis E Virus.Advances in experimental medicine and biology · 2023Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatitis E Virus (HEV) genome encodes three proteins including the ORF2 capsid protein. Recently, we demonstrated that HEV produces three different forms of ORF2: (i) the ORF2i form (infectious ORF2) which is the component of infectious particles, (ii) the secreted ORF2g (glycosylated ORF2) and ORF2c (cleaved ORF2) forms that are not associated with infectious particles, but are the major antigens in HEV-infected patient sera. The ORF2 protein sequence contains three highly conserved potential N-glycosylation sites (N1, N2 and N3). The status and biological relevance of ORF2 N-glycosylation in HEV lifecycle remain to be elucidated. Here, we generated and extensively characterized a series of ORF2 mutants in which the three N-glycosylation sites were mutated individually or in combination. We demonstrated that the ORF2g/c protein is N-glycosylated on N1 and N3 sites but not on the N2 site. We showed that N-glycosylation of ORF2 protein does not play any role in replication and assembly of infectious HEV particles. We found that glycosylated ORF2g/c forms are very stable proteins which are targeted by patient antibodies. We also demonstrated that the ORF2i protein is translocated into the nucleus of infected cells. Hence, our study led to new insights into the molecular mechanisms of ORF2 expression.
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