ArticleCell research2015
Structural basis for the neutralization of hepatitis E virus by a cross-genotype antibody.
Article in Cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 86 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
- Clinical Guidelines for Hepatitis E Vaccination in India: An Expert Panel Consensus Report on the Recombinant Hepatitis E Vaccine, HEV 239.Pathogens (Basel, Switzerland) · 2026Review
- Nanobody-based combination vaccine using licensed protein nanoparticles protects animals against respiratory and viral infections.Nature biomedical engineering · 2026Article
- A modular nanoparticle display strategy for varicella-zoster virus gE based on a licensed protein scaffold.PLoS pathogens · 2026Article
- The crucial but insufficient role of E2s domain's residues 490 and 492 in determining the host tropism of hepatitis E virus.Nature communications · 2026Article
- GRP75 blocks hepatitis E virus infection by targeting HEV-ORF2 for degradation through chaperone-mediated autophagy and promoting IRF3 activation.Journal of virology · 2026Article
- Article
- Vaccination Strategies and Research Gaps in Hepatitis E Virus for Special Populations.Vaccines · 2025Review
- Structural basis for hepatitis E virus neutralization by potent human antibodies.Science advances · 2025Article
- Therapeutic treatment of hepatitis E virus infection in pigs with a neutralizing monoclonal antibody.Scientific reports · 2025Article
- Broadly neutralizing antibodies isolated from HEV convalescents confer protective effects in human liver-chimeric mice.Nature communications · 2025Article
- Immunogenicity, Efficacy, and Effectiveness of Two-Dose and Shorter Schedules of Hepatitis E Vaccine: A Systematic Review.Vaccines · 2024Review
- Structural basis for the synergetic neutralization of hepatitis E virus by antibody-antibody interaction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hepatitis E virus: from innate sensing to adaptive immune responses.Nature reviews. Gastroenterology & hepatology · 2024Review
- A Broad-specificity Neutralizing Nanobody against Hepatitis E Virus Capsid Protein.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Viral hepatitis E: Clinical manifestations, treatment, and prevention.Liver research (Beijing, China) · 2024Review
- Hepatitis E Virus Outbreak among Tigray War Refugees from Ethopia, Sudan.Emerging infectious diseases · 2023Article
- Prophylactic Hepatitis E Vaccine.Advances in experimental medicine and biology · 2023Article
- Genetic Evolution of Hepatitis E Virus.Advances in experimental medicine and biology · 2023Review
- Hepatitis E vaccine-Illuminating the barriers to use.PLoS neglected tropical diseases · 2023Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
Abstract
Hepatitis E virus (HEV), a non-enveloped, positive-sense, single-stranded RNA virus, is a major cause of enteric hepatitis. Classified into the family Hepeviridae, HEV comprises four genotypes (genotypes 1-4), which belong to a single serotype. We describe a monoclonal antibody (mAb), 8G12, which equally recognizes all four genotypes of HEV, with ∼ 2.53-3.45 nM binding affinity. The mAb 8G12 has a protective, neutralizing capacity, which can significantly block virus infection in host cells. Animal studies with genotypes 1, 3 and 4 confirmed the cross-genotype neutralizing capacity of 8G12 and its effective prevention of hepatitis E disease. The complex crystal structures of 8G12 with the HEV E2s domain (the most protruded region of the virus capsid) of the abundant genotypes 1 and 4 were determined at 4.0 and 2.3 Å resolution, respectively. These structures revealed that 8G12 recognizes both genotypes through the epitopes in the E2s dimerization region. Structure-based mutagenesis and cell-model assays with virus-like particles identified several conserved residues (Glu549, Lys554 and Gly591) that are essential for 8G12 neutralization. Moreover, the epitope of 8G12 is identified as a key epitope involved in virus-host interactions. These findings will help develop a common strategy for the prevention of the most abundant form of HEV infection.
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