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Related Experiment Videos

Envelope glycoprotein interactions in coronavirus assembly

D J Opstelten1, M J Raamsman, K Wolfs

  • 1Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands.

The Journal of Cell Biology
|October 1, 1995
PubMed
Summary
This summary is machine-generated.

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Mouse hepatitis virus (MHV) M and S proteins form complexes in infected cells, crucial for viral assembly. These interactions occur in pre-Golgi compartments, influencing viral protein sorting and coat formation.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Coronaviruses assemble via budding into smooth membranes of the ER-to-Golgi intermediate compartment.
  • Understanding the roles of viral membrane glycoproteins in virion envelope formation is essential for comprehending coronavirus assembly.

Purpose of the Study:

  • To investigate the association between the M and S proteins of mouse hepatitis virus (MHV) during virion envelope formation.
  • To elucidate the site and kinetics of M and S protein complex formation and its implications for viral assembly.

Main Methods:

  • Coimmunoprecipitation analysis to detect M and S protein interactions.
  • Pulse-chase experiments to study protein synthesis and complex formation kinetics.
  • Coexpression systems and biochemical assays to analyze M/S complex formation in different cellular contexts.

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Main Results:

  • MHV M and S proteins specifically interact to form heteromultimeric complexes in infected cells.
  • M/S complex formation occurs in pre-Golgi compartments, likely the ER-to-Golgi intermediate compartment.
  • M/S complexes colocalize with Golgi resident proteins and acquire Golgi-specific modifications, but are retained in the Golgi, not transported to the cell surface.
  • The association of S protein with M protein retains it in the Golgi, suggesting M/S complexes do not determine the budding site.

Conclusions:

  • The self-association of MHV envelope glycoproteins into higher-order complexes plays a role in sorting viral membrane proteins.
  • These M/S complexes are critical for driving the formation of the viral lipoprotein coat during virus assembly.
  • The findings indicate that envelope glycoprotein complexes may not dictate the site of coronavirus budding.