10.5061/DRYAD.CM86089
Maddamsetti, Rohan
Old Dominion University
Johnson, Daniel T.
University of California, San Diego
Spielman, Stephanie J.
Rowan University
Petrie, Katherine L.
University of California, San Diego
Marks, Debora S.
Division of Biological SciencesUniversity of California San Diego La
Jolla California
Meyer, Justin R.
University of California, San Diego
Data from: Gain-of-function experiments in bacteriophage lambda uncover
residues under diversifying selection in nature
Dryad
dataset
2018
Host Shift
Synthetic biology
Gain-of-Function
Genomic Epidemiology
Natural Variation
2018-08-15T12:13:26Z
2018-08-15T12:13:26Z
en
https://doi.org/10.1111/evo.13586
940001905 bytes
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CC0 1.0 Universal (CC0 1.0) Public Domain Dedication
Viral gain-of-function mutations frequently evolve during laboratory
experiments. Whether the specific mutations that evolve in the lab also
evolve in nature and whether they have the same impact on evolution in the
real world is unknown. We studied a model virus, bacteriophage λ, that
repeatedly evolves to exploit a new host receptor under typical laboratory
conditions. Here we demonstrate that two residues of λ’s J protein are
required for the new function. In natural λ variants, these amino acid
sites are highly diverse and evolve at high rates. Insertions and
deletions at these locations are associated with phylogenetic patterns
indicative of ecological diversification. Our results show that viral
evolution in the laboratory mirrors that in nature and that laboratory
experiments can be coupled with protein sequence analyses to identify the
causes of viral evolution in the real world. Furthermore, our results
provide evidence for widespread host-shift evolution in lambdoid viruses.
DRYAD-J-alignment-Evolution