Influence of salt and viral protein charge distribution on encapsidation of single-stranded viral RNA molecules

TL;DR

This study uses a mean-field model to show how salt concentration and protein charge distribution influence viral RNA encapsidation and stability, highlighting the importance of charge delocalization for assembly in high-salt environments.

Contribution

It reveals the critical role of salt concentration and charge distribution in viral assembly, emphasizing how charge delocalization enhances stability in high-salt solutions.

Findings

High salt suppresses viral RNA encapsidation.

Charge delocalization in proteins increases stability in high-salt conditions.

Electrostatic interactions are key to viral assembly dynamics.

Abstract

We examine the limits on viral composition that are set by the electrostatic interactions effected by the charge on the viral proteins, the single-stranded viral RNA molecule and monovalent salt ions in the solution. Within the mean-field model of viral energetics we demonstrate the prime importance of the salt concentration for the assembly of a virus. We find that the encapsidation of the viral RNA molecule is thermodynamically suppressed in solutions with high concentrations of monovalent salt. This effect is significantly less important in viruses with proteins whose charge distribution protrudes into the interior of the capsid, leading to an increase in the stability of such viruses in solutions with high salt concentrations. The delocalization of positive charge on the capsid protein arms thus profoundly increases reliability of viral assembly in high-salt solutions.