Exaptation of Inactivated Host Enzymes for Structural Roles in Orthopoxviruses and Novel Folds of Virus Proteins Revealed by Protein Structure Modeling
Pascal Mutz, Wolfgang Resch, Guilhem Faure, Tatiana G. Senkevich, Eugene V. Koonin, Bernard Moss
Abstract
Protein structures are more strongly conserved in evolution than are amino acid sequences. Comparative structural analysis is particularly important for inferring the origins of viral proteins that typically evolve at high rates. We used a powerful protein structure modeling method, namely, AlphaFold2, to model the structures of all orthopoxvirus proteins and compared them to all available protein structures. Multiple cases of recruitment of host enzymes for structural roles in viruses, accompanied by the disruption of catalytic sites, were discovered. However, many viral proteins appear to have evolved unique structural folds.
Topics & Concepts
BiologyGeneGenomeVirusOrthopoxvirusDNA virusGeneticsDNAVirologyVacciniaRecombinant DNABacteriophages and microbial interactionsPoxvirus research and outbreaksPlant Virus Research Studies