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Updated: Jun 11, 2025

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Electrostatic interactions and structural transformations in viral shells.

Ivan Yu Golushko1, Daria S Roshal1, Olga V Konevtsova1

  • 1Faculty of Physics, Southern Federal University, Rostov-on-Don, Russia. rochal_s@yahoo.fr.

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Summary
This summary is machine-generated.

Electrostatic interactions influence viral capsid structure, altering size, shape, and protein subunit conformation. This study models these effects, explaining capsid faceting and spike distribution in viruses like bacteriophage P22.

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Area of Science:

  • Structural biology
  • Biophysics
  • Computational modeling

Background:

  • Viral capsids are protein shells protecting genetic material.
  • Environmental factors like pH can induce structural changes in viral capsids.
  • Electrostatic interactions between proteins play a crucial role in capsid assembly and stability.

Purpose of the Study:

  • To model the impact of electrostatic interactions on viral capsid structure and dynamics.
  • To explain capsid faceting and subunit deformation using a biophysical model.
  • To investigate the role of electrostatic and elastic forces in coronavirus shell morphology.

Main Methods:

  • Development of a 2D elastic shell model with embedded point charges representing proteins.
  • Analysis of electrostatic interactions and their influence on capsid geometry.
  • Comparative study using examples of bacteriophage P22, Nudarelia capensis omega virus (NωV), and coronaviruses.

Main Results:

  • Modification of electrostatic interactions alters capsid size, shape, and induces hexamer deformations.
  • The model explains the transition of hexamers from skewed to regular shapes during capsid faceting.
  • Electrostatic and elastic effects successfully account for the distribution of spikes on coronavirus shells.

Conclusions:

  • Electrostatic interactions are a key determinant of viral capsid structure and conformational changes.
  • The proposed model provides a mechanistic explanation for capsid morphology and subunit organization.
  • The findings offer insights into viral assembly, stability, and potential therapeutic targets.