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Gain‐of‐function experiments with bacteriophage lambda uncover residues under diversifying selection in nature
Author(s) -
Maddamsetti Rohan,
Johnson Daniel T.,
Spielman Stephanie J.,
Petrie Katherine L.,
Marks Debora S.,
Meyer Justin R.
Publication year - 2018
Publication title -
evolution
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.84
H-Index - 199
eISSN - 1558-5646
pISSN - 0014-3820
DOI - 10.1111/evo.13586
Subject(s) - biology , bacteriophage , phylogenetic tree , viral evolution , function (biology) , gain of function , evolutionary biology , experimental evolution , molecular evolution , selection (genetic algorithm) , mutation , genetics , host (biology) , computational biology , rate of evolution , diversification (marketing strategy) , natural selection , genome , gene , escherichia coli , marketing , artificial intelligence , computer science , business
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.