HuR binding to AU-rich elements present in the 3' untranslated region of Classical swine fever virus.

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 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 duanyu3 of short-lived mRNAs. However, the presence of AREs in the duanyu3 of CSFV conserved in all known strains has never been reported. This study inspects a possible role of the ARE in the duanyu3 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 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 duanyu3 of CSFV in vitro and that the binding ability is conserved in strains irrespective of virulence. CONCLUSIONS:This study identified one of the CSFV duanyu3 binding proteins HuR is specifically binding to in the ARE region.

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