Glycoprotein E of the Japanese encephalitis virus forms virus-like particles and induces syncytia when expressed by a

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Ruikun Du1, Feifei Yin1, Manli Wang1

  • 1State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, PR China.

The Journal of General Virology
|January 17, 2015
PubMed

Insights

The Japanese encephalitis virus (JEV) envelope protein (E) can self-assemble into virus-like particles (VLPs) and retains fusion ability without the prM chaperone. This finding aids in developing new antiviral screening methods for JEV.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The prM glycoprotein acts as a chaperone for Japanese encephalitis virus (JEV) envelope protein (E) folding, membrane association, and assembly.
  • Understanding the role of prM in E protein maturation and function is crucial for JEV pathogenesis and antiviral development.

Purpose of the Study:

  • To investigate the expression and function of JEV prM-E and E proteins in insect cells.
  • To determine the influence of the prM protein on the folding, localization, and assembly of the JEV E protein.
  • To explore the potential of JEV E protein self-assembly and fusion activity for antiviral screening.

Main Methods:

  • Expression of JEV prM-E and E proteins in Sf9 insect cells using baculovirus and transient expression systems.
  • Analysis of protein expression via Western blotting and immunofluorescence microscopy.
  • Observation of cytopathic effects, including syncytial formation.
  • Characterization of secreted particles using sucrose gradient sedimentation, electron microscopy, and immunoelectron microscopy.

Main Results:

  • Both prM-E and E proteins induced syncytial formation in Sf9 cells, irrespective of the expression system.
  • In the presence of prM, E protein localized to the endoplasmic reticulum; without prM, E protein was found on the cell surface.
  • Secreted E protein, with or without prM, formed virus-like particles (VLPs) in the culture medium.
  • JEV E protein demonstrated fusion ability, either via cell surface expression or VLP formation, even without prM.

Conclusions:

  • The JEV E protein can independently fold, assemble, and exhibit fusion activity, forming VLPs in the absence of the prM chaperone.
  • The observed syncytial formation upon co-expression of prM-E provides a basis for a novel antiviral screening approach targeting JEV.
  • This study offers insights into JEV assembly mechanisms and proposes a new platform for identifying JEV inhibitors.

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