Solution structure of the porcine sapovirus VPg core reveals a stable three-helical bundle with a conserved surface patch

Biochemical and Biophysical Research Communications
Hyo-Jeong HwangChul Won Lee

Abstract

Viral protein genome-linked (VPg) proteins play a critical role in the life cycle of vertebrate and plant positive-sense RNA viruses by acting as a protein primer for genome replication and as a protein cap for translation initiation. Here we report the solution structure of the porcine sapovirus VPg core (VPg(C)) determined by multi-dimensional NMR spectroscopy. The structure of VPg(C) is composed of three α-helices stabilized by several conserved hydrophobic residues that form a helical bundle core similar to that of feline calicivirus VPg. The putative nucleotide acceptor Tyr956 within the first helix of the core is completely exposed to solvent accessible surface to facilitate nucleotidylation by viral RNA polymerase. Comparison of VPg structures suggests that the surface for nucleotidylation site is highly conserved among the Caliciviridae family, whereas the backbone core structures are different. These structural features suggest that caliciviruses share common mechanisms of VPg-dependent viral replication and translation.

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Citations

Apr 23, 2016·Viruses·Elizabeth Royall, Nicolas Locker
Nov 9, 2017·Viruses·Ji-Hye LeeKyung Hyun Kim
Apr 22, 2017·Frontiers in Plant Science·Manuel MirasMiguel A Aranda
Nov 26, 2015·International Journal of Biological Macromolecules·R B MariuttiR K Arni

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