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A structural analysis of M protein in coronavirus assembly and morphology

Benjamin W Neuman1, Gabriella Kiss, Andreas H Kunding

  • 1School of Biological Sciences, University of Reading, RG6 6AJ, UK. b.w.neuman@reading.ac.uk

Journal of Structural Biology
|December 7, 2010
PubMed

Insights

Coronavirus M protein structure dictates virus assembly and shape. Different M protein conformations influence membrane curvature, affecting virion size and spike arrangement. Other viral components also regulate these processes.

Area of Science:

  • Virology
  • Structural Biology
  • Biophysics

Background:

  • The M protein is crucial for coronavirus assembly, mediating the formation of new virus particles.
  • Understanding M protein's role in virus structure is key to comprehending viral replication.

Purpose of the Study:

  • To investigate the relationship between M protein structure, organization, and coronavirus shape/size.
  • To elucidate the mechanisms by which M protein regulates membrane curvature during virus assembly.

Main Methods:

  • Cryo-electron microscopy and tomography were employed to visualize M protein structures.
  • Statistical analysis was used to correlate M protein conformation with virion characteristics.

Main Results:

  • The M protein exists in at least two distinct conformations.
  • One M conformer regulates membrane curvature, influencing virion shape.
  • Elongated M protein correlates with rigidity and clustered spikes, while compact M protein is linked to flexibility and lower spike density.
  • S protein, N protein, and genomic RNA interact with M protein to modulate virion size and variation.

Conclusions:

  • M protein conformation is a key determinant of coronavirus morphology.
  • Interactions between M protein and other viral components fine-tune virion assembly and size.
  • These findings offer insights into the fundamental mechanisms of coronavirus assembly.

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