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Viral Mutations

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material...

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Updated: Jun 14, 2025

Reverse Genetics Mediated Recovery of Infectious Murine Norovirus

Reverse Genetics Mediated Recovery of Infectious Murine Norovirus

Published on: June 24, 2012

Human Rhinovirus B14 with Non-functional Drug-binding Pockets Recovers Infectivity through Stereochemically

Juan Carlos Gil-Redondo¹, Luis Valiente¹, Valentín Riomoros-Barahona¹

¹Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid 28049 Madrid, Spain.

Journal of Molecular Biology

|June 1, 2025

Summary

This summary is machine-generated.

Human rhinovirus (RV) mutations impairing capsid flexibility and infectivity were studied. Viruses recovered infectivity through specific mutations restoring flexibility, offering insights for antiviral drug development.

Keywords:

antiviral drugs capsid compensatory mutations structure virus

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Published on: November 1, 2011

Area of Science:

Virology
Structural Biology
Drug Discovery

Background:

Human rhinovirus (RV) is a common pathogen causing colds and exacerbating respiratory illnesses.
No effective anti-RV drugs or vaccines are currently available.
Targeting the RV capsid offers a potential therapeutic strategy.

Purpose of the Study:

To investigate the impact of mutations in a druggable pocket of the RV capsid.
To understand the mechanisms of viral infectivity recovery after capsid mutation.
To explore the potential for developing anti-RV drugs based on capsid constraints.

Main Methods:

Site-directed mutagenesis of amino acid residues in the RV capsid.
Serial infection of human host cells to assess viral infectivity.
Viral progeny sequencing to identify genetic changes.
All-atom molecular dynamics simulations.
Atomic force microscopy to determine capsid mechanical elasticity.

Main Results:

Replacing small residues with larger ones in the druggable pocket impaired RV infectivity.
Mutant RVs recovered infectivity not through second-site mutations, but via reversion/pseudo-reversion to smaller residues.
These mutations reduced capsid conformational flexibility, which was restored upon infectivity recovery.
The RV capsid's druggable pocket exhibits stereochemical constraints crucial for flexibility.

Conclusions:

The RV capsid's druggable pocket has biological constraints on volume and flexibility.
Restoring capsid flexibility is essential for infectivity recovery, achieved through specific same-site mutations.
These findings provide a basis for designing novel anti-RV drugs targeting these constraints.