title: HuR binding to AU-rich elements present in the 3' untranslated region of Classical swine fever virus.
abstract: BACKGROUND
  Classical swine fever virus (CSFV) is the member of the genus Pestivirus under the family Flaviviridae. The 5' untranslated region (UTR) of CSFV contains the IRES, which is a highly structured element that recruits the translation machinery. The 3' UTR is usually the recognition site of the viral replicase to initiate minus-strand RNA synthesis. Adenosine-uridine rich elements (ARE) are instability determinants present in the 3' UTR of short-lived mRNAs. However, the presence of AREs in the 3' UTR of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the 3' UTR of CSFV.
  
  
  RESULTS
  Using RNA pull-down and LC/MS/MS assays, this study identified at least 32 possible host factors derived from the cytoplasmic extracts of PK-15 cells that bind to the CSFV 3' UTR, one of which is HuR. HuR is known to bind the AREs and protect the mRNA from degradation. Using recombinant GST-HuR, this study demonstrates that HuR binds to the ARE present in the 3' UTR of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence.
  
  
  CONCLUSIONS
  This study identified one of the CSFV 3' UTR binding proteins HuR is specifically binding to in the ARE region.
authors: Graduate Institute of Biotechnology, National Chung Hsing University, Taichung, 402, Taiwan.
authors: Muthukumar
authors: M
authors: Nadar
authors: Meng-Yu
authors: MY
authors: Chan
authors: Shi-Wei
authors: SW
authors: Huang
authors: Chin-Cheng
authors: CC
authors: Huang
authors: Joseph T
authors: JT
authors: Tseng
authors: Ching-Hsiu
authors: CH
authors: Tsai
mesh_terms: D020413:3' Untranslated Regions; D000818:Animals; D000954:Antigens, Surface / Q000378:metabolism*; D001665:Binding Sites; D002460:Cell Line; D006692:Classical Swine Fever Virus / Q000235:genetics*; D051959:ELAV Proteins; D000067780:ELAV-Like Protein 1; D024202:Electrophoretic Mobility Shift Assay; D054884:Host-Pathogen Interactions; D011485:Protein Binding; D012367:RNA, Viral / Q000235:genetics* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D013552:Swine
chemical_list: D020413:3' Untranslated Regions; D000954:Antigens, Surface; D051959:ELAV Proteins; D000067780:ELAV-Like Protein 1; C098770:ELAVL1 protein, human; D012367:RNA, Viral; D016601:RNA-Binding Proteins