ArticlePLoS genetics2012
Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme.
Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
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- Experimental Evolution Studies in Φ6 Cystovirus.Viruses · 2024Review
- A meta-analysis highlights the idiosyncratic nature of tradeoffs in laboratory models of virus evolution.Virus evolution · 2024Article
- Flagellotropic Bacteriophages: Opportunities and Challenges for Antimicrobial Applications.International journal of molecular sciences · 2022Review
- Viral protein instability enhances host-range evolvability.PLoS genetics · 2022Article
- Selection for Phage Resistance Reduces Virulence of Shigella flexneri.Applied and environmental microbiology · 2022Article
- Viruses in astrobiology.Frontiers in microbiology · 2022Review
- Affinity Sedimentation and Magnetic Separation With Plant-Made Immunosorbent Nanoparticles for Therapeutic Protein Purification.Frontiers in bioengineering and biotechnology · 2022Article
- Heat adaptation of phage T7 under an extended genetic code.Virus evolution · 2021Article
- Trading-off and trading-up in the world of bacteria-phage evolution.Current biology : CB · 2020Article
- Profile of Paul E. Turner.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Gauging genetic diversity of generalists: A test of genetic and ecological generalism with RNA virus experimental evolution.Virus evolution · 2019Article
Corrections and comments
- Erratum issued
- Erratum issuedMcBride, Robert L [corrected to McBride, Robert C]
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The modulation of fitness by single mutational substitutions during environmental change is the most fundamental consequence of natural selection. The antagonistic tradeoffs of pleiotropic mutations that can be selected under changing environments therefore lie at the foundation of evolutionary biology. However, the molecular basis of fitness tradeoffs is rarely determined in terms of how these pleiotropic mutations affect protein structure. Here we use an interdisciplinary approach to study how antagonistic pleiotropy and protein function dictate a fitness tradeoff. We challenged populations of an RNA virus, bacteriophage Φ6, to evolve in a novel temperature environment where heat shock imposed extreme virus mortality. A single amino acid substitution in the viral lysin protein P5 (V207F) favored improved stability, and hence survival of challenged viruses, despite a concomitant tradeoff that decreased viral reproduction. This mutation increased the thermostability of P5. Crystal structures of wild-type, mutant, and ligand-bound P5 reveal the molecular basis of this thermostabilization--the Phe207 side chain fills a hydrophobic cavity that is unoccupied in the wild-type--and identify P5 as a lytic transglycosylase. The mutation did not reduce the enzymatic activity of P5, suggesting that the reproduction tradeoff stems from other factors such as inefficient capsid assembly or disassembly. Our study demonstrates how combining experimental evolution, biochemistry, and structural biology can identify the mechanisms that drive the antagonistic pleiotropic phenotypes of an individual point mutation in the classic evolutionary tug-of-war between survival and reproduction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.