ArticleJournal of virology2000
Identification of immunodominant and conformational epitopes in the capsid protein of hepatitis E virus by using monoclonal antibodies.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 96 citations in OpenAlex.
- ORF2 of hepatitis E virus: genetic and antigenic variation across genotypes and implications for immunity, diagnostics and vaccine development.The Journal of general virology · 2026Review
- Hepatitis E Virus Infection in Pregnant Women.Microorganisms · 2026Review
- Hepatitis E virus: from innate sensing to adaptive immune responses.Nature reviews. Gastroenterology & hepatology · 2024Review
- Multi-epitope vaccine design for hepatitis E virus based on protein ORF2 and ORF3.Frontiers in microbiology · 2024Article
- An In Silico Deep Learning Approach to Multi-Epitope Vaccine Design: A Hepatitis E Virus Case Study.Vaccines · 2023Article
- Laboratory Diagnosis of HEV Infection.Advances in experimental medicine and biology · 2023Review
- High-Yield Production of Chimeric Hepatitis E Virus-Like Particles Bearing the M2e Influenza Epitope and Receptor Binding Domain of SARS-CoV-2 in Plants Using Viral Vectors.International journal of molecular sciences · 2022Article
- Viral hepatitis in pregnancy.Journal of viral hepatitis · 2022Review
- Prediction of promiscuous epitopes in ORF2 of Hepatitis E virus: anAfrican health sciences · 2022Article
- A ribavirin-induced ORF2 single-nucleotide variant produces defective hepatitis E virus particles with immune decoy function.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- A broadly cross-reactive monoclonal antibody against hepatitis E virus capsid antigen.Applied microbiology and biotechnology · 2021Article
- Functional epitopes on hepatitis E virions and recombinant capsids are highly conformation-dependent.Human vaccines & immunotherapeutics · 2020Article
- CD8Journal of medical virology · 2019Article
- Article
- New insights into the ORF2 capsid protein, a key player of the hepatitis E virus lifecycle.Scientific reports · 2019Article
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- Identification and characterization of two linear epitope motifs in hepatitis E virus ORF2 protein.PloS one · 2017Article
- Characterization of the Specificity, Functionality, and Durability of Host T-Cell Responses Against the Full-Length Hepatitis E Virus.Hepatology (Baltimore, Md.) · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody to the capsid (PORF2) protein of hepatitis E virus (HEV) is sufficient to confer immunity, but knowledge of B-cell epitopes in the intact capsid is limited. A panel of murine monoclonal antibodies (MAbs) was generated following immunization with recombinant ORF2.1 protein, representing the C-terminal 267 amino acids (aa) of the 660-aa capsid protein. Two MAbs reacted exclusively with the conformational ORF2.1 epitope (F. Li, J. Torresi, S. A. Locarnini, H. Zhuang, W. Zhu, X. Guo, and D. A. Anderson, J. Med. Virol. 52:289-300, 1997), while the remaining five demonstrated reactivity with epitopes in the regions aa 394 to 414, 414 to 434, and 434 to 457. The antigenic structures of both the ORF2.1 protein expressed in Escherichia coli and the virus-like particles (VLPs) expressed using the baculovirus system were examined by competitive enzyme-linked immunosorbent assays (ELISAs) using five of these MAbs and HEV patient sera. Despite the wide separation of epitopes within the primary sequence, all the MAbs demonstrated some degree of cross-inhibition with each other in ORF2. 1 and/or VLP ELISAs, suggesting a complex antigenic structure. MAbs specific for the conformational ORF2.1 epitope and a linear epitope within aa 434 to 457 blocked convalescent patient antibody reactivity against VLPs by approximately 60 and 35%, respectively, while MAbs against epitopes within aa 394 to 414 and 414 to 434 were unable to block patient serum reactivity. These results suggest that sequences spanning aa 394 to 457 of the capsid protein participate in the formation of strongly immunodominant epitopes on the surface of HEV particles which may be important in immunity to HEV infection.
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