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Hepatitis

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Hepatitis is an inflammatory condition of the liver most commonly caused by hepatotropic viruses (A–E), though non-infectious causes such as alcohol and drugs also exist.Hepatitis AHepatitis A virus (HAV) is a non-enveloped RNA virus of the Picornaviridae family. It is primarily transmitted via the fecal-oral route, typically through ingestion of contaminated food or water. After ingestion, HAV enters the bloodstream through the oropharynx or intestinal epithelium and reaches the liver. The...

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Related Experiment Video

Updated: Jun 6, 2026

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods

Published on: May 11, 2018

Spatial configuration of hepatitis E virus antigenic domain.

Li Xing¹, Joseph C Wang, Tian-Cheng Li

¹Molecular and Cellular Biology, University of California, 1 Shields Ave., Davis, CA 95616, USA.

Journal of Virology

|November 12, 2010

Summary

Hepatitis E virus (HEV) virus-like particles (VLPs) can display foreign epitopes. These T=1 HEV VLPs are a novel system for inducing immunity against both HEV and inserted foreign antigens.

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A Cell Culture Model for Producing High Titer Hepatitis E Virus Stocks

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Published on: June 26, 2020

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Last Updated: Jun 6, 2026

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods

Surface Functionalization of Hepatitis E Virus Nanoparticles Using Chemical Conjugation Methods

Published on: May 11, 2018

A Cell Culture Model for Producing High Titer Hepatitis E Virus Stocks

A Cell Culture Model for Producing High Titer Hepatitis E Virus Stocks

Published on: June 26, 2020

Area of Science:

Virology
Structural Biology
Immunology

Background:

Hepatitis E virus (HEV) causes acute hepatitis in humans.
Recombinant HEV capsid proteins can self-assemble into T=1 virus-like particles (VLPs) that mimic the native virion's antigenicity.

Purpose of the Study:

To characterize the binding sites of anti-HEV antibodies on HEV VLPs.
To investigate the potential of HEV VLPs as a delivery system for foreign epitopes.

Main Methods:

Cryoelectron microscopy and image reconstruction were used to determine antibody binding sites.
Molecular docking was employed to analyze the interaction between antibodies and HEV VLPs.
A chimeric HEV VLP with an inserted B-cell tag was constructed and analyzed.

Main Results:

Anti-HEV monoclonal antibodies bind to the protruding domain of the HEV capsid protein, specifically covering surface loops.
The binding site of a specific antibody (Fab224) was distinct from the location of an inserted foreign epitope on a chimeric VLP.
The chimeric HEV VLP demonstrated the capacity to display foreign epitopes.

Conclusions:

The T=1 HEV VLP serves as a versatile platform for displaying foreign epitopes.
This novel delivery system can potentially induce immunity against both HEV and the displayed foreign antigen.