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Viral Mutations

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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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Related Experiment Video

Updated: Jun 29, 2025

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay

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Published on: September 14, 2014

Viral Receptor-Binding Protein Evolves New Function through Mutations That Cause Trimer Instability and Functional

Hannah M Strobel¹, Sweetzel D Labador¹, Dwaipayan Basu^2,3

¹School of Biological Sciences, University of California San Diego, La Jolla, CA, USA.

Molecular Biology and Evolution

|April 8, 2024

Summary

Protein evolution can lead to instability, which may unexpectedly drive new functions. This study shows unstable bacteriophage proteins evolved new host ranges by altering receptor binding.

Keywords:

bacteriophage experimental evolution nongenetic heterogeneity novelty protein evolution receptor-binding protein

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Last Updated: Jun 29, 2025

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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

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Isolation of Fidelity Variants of RNA Viruses and Characterization of Virus Mutation Frequency

Isolation of Fidelity Variants of RNA Viruses and Characterization of Virus Mutation Frequency

Published on: June 16, 2011

Area of Science:

Evolutionary biology
Molecular biology
Biochemistry

Background:

Protein mutations conferring new activity often decrease stability.
Instability was traditionally viewed as a detrimental cost of protein evolution.
Recent evidence suggests unstable conformations may facilitate evolutionary transitions.

Purpose of the Study:

To investigate if protein instability can potentiate the evolution of new protein activity.
To examine the role of instability in the host-range evolution of a bacteriophage receptor-binding protein.

Main Methods:

Comparative analysis of bacteriophage lambda receptor-binding protein before and after host-range evolution.
Structural modeling to predict conformational changes.
In vitro oligomeric state analysis to assess protein stability and interactions.

Main Results:

The evolved receptor-binding protein is less stable than the ancestral form.
Instability is linked to mutations disrupting protein trimer formation.
The evolved protein may adopt multiple conformations with distinct receptor preferences.

Conclusions:

Protein instability, particularly in receptor-binding proteins, may play a crucial role in viral host-range expansion.
This challenges the conventional view of instability as solely deleterious in protein evolution.
Unstable protein conformations could be key mediators of adaptive evolution in viruses.