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Release of coronavirus E protein in membrane vesicles from virus-infected cells and E protein-expressing cells

J Maeda1, A Maeda, S Makino

  • 1Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, Texas 78712, USA.

Virology
|November 2, 1999
PubMed

Insights

The coronavirus E protein drives viral envelope production and release. This integral membrane protein can form lipid vesicles independently, even without the M protein, simplifying coronavirus assembly.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The coronavirus E protein is a critical component in viral assembly.
  • Co-expression of M and E proteins leads to virus-like particle formation.

Purpose of the Study:

  • To investigate the role and release mechanism of the mouse hepatitis virus (MHV) E protein.
  • To determine if E protein can drive coronavirus envelope production independently.

Main Methods:

  • Expressing MHV E protein in mammalian cells.
  • Analyzing the release of E protein in lipid vesicles.
  • Comparing the buoyant density of E-protein vesicles with MHV.

Main Results:

  • MHV E protein was released as an integral membrane protein within lipid vesicles from E-protein-expressing cells.
  • These E-protein-containing vesicles were released from MHV-infected cells.
  • The vesicles showed a slightly lower buoyant density compared to intact MHV.

Conclusions:

  • Coronavirus E protein alone can induce the production and release of viral envelopes.
  • The M protein is not essential for E protein-driven envelope formation and release.

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