ArticleProtein science : a publication of the Protein Society2013
Hepatitis E virus capsid protein assembles in 4M urea in the presence of salts.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 21 citations in OpenAlex.
- Analytical Ultracentrifugation for Biopharmaceutical Characterization and Quality Control.International journal of molecular sciences · 2026Review
- Nanobody-based combination vaccine using licensed protein nanoparticles protects animals against respiratory and viral infections.Nature biomedical engineering · 2026Article
- EngineeringVaccines · 2024Review
- Prophylactic Hepatitis E Vaccine.Advances in experimental medicine and biology · 2023Article
- Article
- Hepatitis E virus: Current epidemiology and vaccine.Human vaccines & immunotherapeutics · 2016Review
- Functional assessment and structural basis of antibody binding to human papillomavirus capsid.Reviews in medical virology · 2016Review
- The development of a recombinant hepatitis E vaccine HEV 239.Human vaccines & immunotherapeutics · 2015Review
- Lessons learned from successful human vaccines: Delineating key epitopes by dissecting the capsid proteins.Human vaccines & immunotherapeutics · 2015Review
- Subviral particle as vaccine and vaccine platform.Current opinion in virology · 2014Review
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Authors and funding
10 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The hepatitis E virus (HEV) capsid protein has been demonstrated to be able to assemble into particles in vitro. However, this process and the mechanism of protein-protein interactions during particle assembly remain unclear. In this study, we investigated the assembly mechanism of HEV structural protein subunits, the capsid protein p239 (aa368-606), using analytical ultracentrifugation. It was the first to observe that the p239 can form particles in 4M urea as a result of supplementation with salt, including ammonium sulfate [(NH₄)₂SO₄], sodium sulfate (Na₂SO₄), sodium chloride (NaCl), and ammonium chloride (NH₄Cl). Interestingly, it is the ionic strength that determines the efficiency of promoting particle assembly. The assembly rate was affected by temperature and salt concentration. When (NH₄)₂SO₄ was used, assembling intermediates of p239 with sedimentation coefficient values of approximately 5 S, which were mostly dodecamers, were identified for the first time. A highly conserved 28-aa region (aa368-395) of p239 was found to be critical for particle assembly, and the hydrophobic residues Leu³⁷², Leu³⁷⁵, and Leu³⁹⁵ of p239 was found to be critical for particle assembly, which was revealed by site-directed mutagenesis. This study provides new insights into the assembly mechanism of native HEV, and contributes a valuable basis for further investigations of protein assembly by hydrophobic interactions under denaturing conditions.
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