A conserved domain in the coronavirus membrane protein tail is important for virus assembly

Ariel L Arndt1, Blake J Larson, Brenda G Hogue

  • 1School of Life Sciences, The Biodesign Institute, P.O. Box 875401, Arizona State University, Tempe, AZ 85287-5401, USA.

Journal of Virology
|August 20, 2010
PubMed

Insights

The conserved domain of coronavirus M proteins is crucial for viral envelope formation. Mutations in this domain, particularly affecting charge and specific residues, disrupt virus assembly and particle production.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Coronavirus membrane (M) proteins are essential for virus assembly, mediating interactions with other viral proteins like spike (S) and nucleocapsid (N).
  • The M protein possesses a conserved domain (CD) in its carboxy-terminal endodomain, following the third transmembrane (TM) domain, whose function is critical for viral processes.

Purpose of the Study:

  • To investigate the functional importance of the conserved domain (CD) within the mouse hepatitis virus M protein.
  • To elucidate the role of specific amino acid residues and M-M interactions in viral envelope formation and assembly.

Main Methods:

  • Utilized genetic analysis and transient-expression assays to study a panel of M protein mutants.
  • Generated mutant viruses with specific amino acid substitutions and assessed their ability to form virus-like particles (VLPs) and infectivity.

Main Results:

  • Charge reversal mutations at E(121) were not tolerated, with substitutions reverting to neutral charges in recovered viruses.
  • Mutations in the conserved domain (SWWS) resulted in severely impaired viral phenotypes and failed VLP assembly.
  • N protein coexpression partially rescued VLP production for certain M mutants, suggesting a stabilizing role.

Conclusions:

  • The conserved domain of the M protein is vital for viral envelope formation, primarily by mediating essential M-M interactions.
  • The nucleocapsid (N) protein may play a supportive role in stabilizing M protein complexes during the virus assembly process.

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