Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 459, Issue 4, Pages 610-616Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.02.156
Keywords
NMR spectroscopy; Porcine sapovirus; RNA-dependent RNA polymerase; Viral protein genome-linked
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Funding
- Basic Science Research Program through National Research Foundation of Korea - Ministry of Education, Science, and Technology of Korea [NRF-2013R1A1A2009419, 2014R1A2A2A01004915]
- Ministry of Science, ICT and Future Planning [NRF-2014M2B2A4029302]
- National Research Foundation of Korea [2014R1A2A2A01004915] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 alpha-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. (C) 2015 Elsevier Inc. All rights reserved.
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