title: RNA interaction and cleavage of poly(C)-binding protein 2 by hepatitis A virus protease.
abstract: The poly(rC)-binding protein PCBP2 has multiple functions in post-transcriptional control of host and viral gene expression. Since it interacts with picornaviral RNA structures, it was proposed that PCBP2 regulates viral genome translation and replication. The hepatitis A virus (HAV), an atypical picornavirus, contains an unusual pyrimidine-rich tract (pY1) with unknown functions. Using in vivo and in vitro assays, we provide direct evidence that PCBP2 interacts with pY1 and that binding is mediated by KH domains 1 and 3. Proteolytic cleavage by the viral protease 3C generates a C-terminally truncated polypeptide with highly reduced RNA affinity. The results suggest that during HAV infection PCBP2 cleavage might specifically down-regulate viral protein synthesis, thereby giving way to viral RNA synthesis.
authors.affiliation: Institute of Medical Molecular Biology, University of Lübeck, Germany.
authors.forename: Bo
authors.initials: B
authors.lastname: Zhang
authors.forename: Simone
authors.initials: S
authors.lastname: Seitz
authors.forename: Yuri
authors.initials: Y
authors.lastname: Kusov
authors.forename: Roland
authors.initials: R
authors.lastname: Zell
authors.forename: Verena
authors.initials: V
authors.lastname: Gauss-Müller
mesh_terms: D001665:Binding Sites; D030041:Hepatitis A virus / Q000737:chemistry* / Q000201:enzymology*; D011485:Protein Binding; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C501903:PCBP2 protein, human; D016601:RNA-Binding Proteins; D012313:RNA