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Protein interactions during coronavirus assembly

V P Nguyen1, B G Hogue

  • 1Division of Molecular Virology, Baylor College of Medicine, Houston, Texas 77030, USA.

Journal of Virology
|November 26, 1997
PubMed
Summary

Bovine coronavirus (BCV) assembly involves interactions between membrane (M), spike (S), and hemagglutinin esterase (HE) proteins. These viral proteins form complexes in the Golgi, crucial for coronavirus envelope formation and replication.

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Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Coronaviruses, like other enveloped viruses, assemble at intracellular membranes, specifically the ER-Golgi intermediate compartment.
  • Viral assembly relies on precise protein localization and interactions, including protein-protein and protein-RNA binding.

Purpose of the Study:

  • To investigate the interactions among bovine coronavirus (BCV) structural proteins (M, S, HE) essential for viral assembly.
  • To elucidate the temporal dynamics and localization of these protein interactions during the viral lifecycle.

Main Methods:

  • Co-immunoprecipitation assays in BCV-infected cells to detect protein complexes.
  • Kinetic analysis of protein synthesis and complex formation.
  • Transient co-expression and double-labeling immunofluorescence in transfected cells.

Main Results:

  • Complexes of M, S, and HE proteins were identified in infected cells.
  • S and HE proteins rapidly complexed with M protein post-synthesis; M-S-HE heterocomplexes formed more slowly.
  • HE dimerization was observed within M-S-HE complexes, which formed before HE oligosaccharide processing in the Golgi.

Conclusions:

  • Specific interactions between M, S, and HE proteins are critical for coronavirus assembly.
  • Protein oligomerization and conformational changes, particularly HE dimerization, likely facilitate the formation of functional M-S-HE complexes.
  • These interactions occur in a premedial Golgi compartment, preceding further protein modifications.

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