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Structural basis for the replication of genomic RNA of porcine enteric sapovirus by VPg (LB243)
Author(s) -
Min Hye Jung,
Hwang HyoJeong,
Kim JeongSun,
Lee Chul Won
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.lb243
Subject(s) - rna , sapovirus , biology , viral replication , chemistry , genetics , microbiology and biotechnology , virus , gene , rotavirus
Structural basis for the replication of genomic RNA of porcine enteric sapovirus by VPg Hye Jung Min, Hyo‐Jeong Hwang, Jeong‐Sun Kim, and Chul Won Lee Department of Chemistry, Chonnam National University, Gwangju 500‐757, Korea. Viral protein genome‐linked (VPg) plays a critical role in the life cycle of vertebrate and plant positive‐sense (+) RNA viruses by acting as a protein primer for RNA synthesis. The replication of the viruses is primed by the VPg protein by attaching to the 5’‐end of the viral RNA genome. Here we show the solution structure of VPg of porcine enteric sapovirus (PSV) determined by multi‐dimensional NMR spectroscopy. The structure of VPg comprises three helices (denoted α1, α2, and α3) which were tightly packed together through hydrophobic interactions formed by several hydrophobic residues to form a three‐helix bundle structure. The orientation and length of three helices of PSV VPg are similar to those of feline calicivirus (FCV) VPg with similar core structure formed by conserved hydrophobic residues. The tyrosine residue (Tyr956) within the conserved motif for nucleotide acceptor is exposed to the solvent surface to facilitate nucleotidylation by viral RNA polymerases. These results may provide the molecular basis for the replication of positive‐RNA viruses.