title: First-step mutations for adaptation at elevated temperature increase capsid stability in a virus.
abstract: The relationship between mutation, protein stability and protein function plays a central role in molecular evolution. Mutations tend to be destabilizing, including those that would confer novel functions such as host-switching or antibiotic resistance. Elevated temperature may play an important role in preadapting a protein for such novel functions by selecting for stabilizing mutations. In this study, we test the stability change conferred by single mutations that arise in a G4-like bacteriophage adapting to elevated temperature. The vast majority of these mutations map to interfaces between viral coat proteins, suggesting they affect protein-protein interactions. We assess their effects by estimating thermodynamic stability using molecular dynamic simulations and measuring kinetic stability using experimental decay assays. The results indicate that most, though not all, of the observed mutations are stabilizing.
authors: Department of Physics, University of Idaho, Moscow, Idaho, United States of America.
authors: Kuo Hao
authors: KH
authors: Lee
authors: Craig R
authors: CR
authors: Miller
authors: Anna C
authors: AC
authors: Nagel
authors: Holly A
authors: HA
authors: Wichman
authors: Paul
authors: P
authors: Joyce
authors: F Marty
authors: FM
authors: Ytreberg
mesh_terms: D000220:Adaptation, Biological / Q000235:genetics* / Q000502:physiology; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics*; D019277:Entropy; D019143:Evolution, Molecular; D017914:Microviridae / Q000235:genetics* / Q000502:physiology*; D056004:Molecular Dynamics Simulation; D009154:Mutation; D011487:Protein Conformation; D055550:Protein Stability; D013696:Temperature
chemical_list: D036022:Capsid Proteins