ArticleJournal of clinical microbiology1999
Antigenic domains of the open reading frame 2-encoded protein of hepatitis E virus.
Article in Journal of clinical microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 56 citations in OpenAlex.
- [Prophylactic vaccines for hepatitis type E].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2023Article
- An In Silico Deep Learning Approach to Multi-Epitope Vaccine Design: A Hepatitis E Virus Case Study.Vaccines · 2023Article
- Prophylactic Hepatitis E Vaccine.Advances in experimental medicine and biology · 2023Article
- Viral hepatitis in pregnancy.Journal of viral hepatitis · 2022Review
- Prediction of promiscuous epitopes in ORF2 of Hepatitis E virus: anAfrican health sciences · 2022Article
- Expression, Purification and Characterization of the Hepatitis E Virus Like-Particles in theFrontiers in microbiology · 2020Article
- Characterization of the Specificity, Functionality, and Durability of Host T-Cell Responses Against the Full-Length Hepatitis E Virus.Hepatology (Baltimore, Md.) · 2016Article
- Lessons learned from successful human vaccines: Delineating key epitopes by dissecting the capsid proteins.Human vaccines & immunotherapeutics · 2015Review
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- Seroprevalence study in forestry workers from eastern Germany using novel genotype 3- and rat hepatitis E virus-specific immunoglobulin G ELISAs.Medical microbiology and immunology · 2012Article
- A single amino acid substitution changes antigenicity of ORF2-encoded proteins of hepatitis E virus.International journal of molecular sciences · 2010Article
- Application of truncated immunodominant polypeptide from hepatitis E virus (HEV) ORF2 in an assay to exclude nonspecific binding in detecting anti-HEV immunoglobulin M.Journal of clinical microbiology · 2010Article
- Screening of specific diagnostic peptides of swine hepatitis E virus.Virology journal · 2009Article
- Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- T-cell epitope mapping of ORF2 and ORF3 proteins of human hepatitis E virus.Journal of viral hepatitis · 2007Article
- Hepatitis E vaccines: progress and prospects.Drugs · 2004Review
- Hepatitis E virus epidemiology in industrialized countries.Emerging infectious diseases · 2003Article
- Hepatitis E virus (HEV) capsid antigens derived from viruses of human and swine origin are equally efficient for detecting anti-HEV by enzyme immunoassay.Journal of clinical microbiology · 2002Article
- Detection by reverse transcription-PCR and genetic characterization of field isolates of swine hepatitis E virus from pigs in different geographic regions of the United States.Journal of clinical microbiology · 2002Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antigenic composition of the hepatitis E virus (HEV) protein encoded by open reading frame 2 (ORF2) was determined by using synthetic peptides. Three sets of overlapping 18-, 25-, and 30-mer peptides, with each set spanning the entire ORF2 protein of the HEV Burma strain, were synthesized. All synthetic peptides were tested by enzyme immunoassay against a panel of 32 anti-HEV-positive serum specimens obtained from acutely HEV-infected persons. Six antigenic domains within the ORF2 protein were identified. Domains 1 and 6 located at the N and C termini of the ORF2 protein, respectively, contain strong immunoglobulin G (IgG) and IgM antigenic epitopes that can be efficiently modeled with peptides of different sizes. In contrast, antigenic epitopes identified within the two central domains (3 and 4) were modeled more efficiently with 30-mer peptides than with either 18- or 25-mers. Domain 2 located at amino acids (aa) 143 to 222 was modeled best with 25-mer peptides. A few 30-mer synthetic peptides derived from domain 5 identified at aa 490 to 579 demonstrated strong IgM antigenic reactivity. Several 30-mer synthetic peptides derived from domains 1, 4, and 6 immunoreacted with IgG or IgM with more than 70% of anti-HEV-positive serum specimens. Thus, the results of this study demonstrate the existence of six diagnostically relevant antigenic domains within the HEV ORF2 protein.
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