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Destabilizing mutations encode nongenetic variation that drives evolutionary innovation.

Katherine L Petrie^1,2, Nathan D Palmer³, Daniel T Johnson³

¹Division of Biological Sciences, University of California (UC) San Diego, La Jolla, CA 92093, USA. kpetrie@ucsd.edu jrmeyer@ucsd.edu.

Science (New York, N.Y.)

|March 31, 2018

Summary

Mutations in bacteriophage lambda's J gene allow it to infect new hosts by altering its receptor binding. This demonstrates how protein variation can drive evolutionary innovation by enabling new functions.

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Area of Science:

Evolutionary biology
Molecular biology
Virology

Background:

Evolutionary innovations often arise from gene repurposing, but the underlying mechanisms are debated.
Bacteriophage lambda (λ) utilizes its J protein for host recognition, binding to the LamB receptor.

Purpose of the Study:

To investigate the mechanisms by which bacteriophage lambda's host-recognition gene J evolves new functions.
To explore how mutations in gene J facilitate adaptation to new receptors.

Main Methods:

Identifying mutations in bacteriophage lambda's J gene.
Assessing the adsorption of mutant phages to native (LamB) and new (OmpF) receptors.
Analyzing the structural and functional consequences of mutations on the J protein and phage particle.

Main Results:

Mutations in gene J enhance adsorption to the native LamB receptor and enable binding to the OmpF receptor.
These mutations destabilize the phage lambda particle, inducing conformational bistability in the J protein.
This bistability results in progeny phages with multiple phenotypes, each adapted to different receptors.

Conclusions:

Nongenetic protein variation, through mechanisms like conformational bistability, can catalyze evolutionary innovation.
A single genotype manifesting multiple phenotypes may be a common driver of evolution.
This study provides a model for understanding how viruses adapt and evolve new host ranges.