Evolutionary interplay between structure, energy and epistasis in the coat protein of the ϕX174 phage family.

ABSTRACT: Viral capsids are structurally constrained by interactions among the amino acids (AAs) of their constituent proteins. Therefore, epistasis is expected to evolve among physically interacting sites and to influence the rates of substitution. To study the evolution of epistasis, we focused on the major structural protein of the ϕX174 phage family by first reconstructing the ancestral protein sequences of 18 species using a Bayesian statistical framework. The inferred ancestral reconstruction differed at eight AAs, for a total of 256 possible ancestral haplotypes. For each ancestral haplotype and the extant species, we estimated, in silico, the distribution of free energies and epistasis of the capsid structure. We found that free energy has not significantly increased but epistasis has. We de

SUBMITTER: Redondo RA 

PROVIDER: S-EPMC5310724 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature