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Nucleic Acids Research Advance Access originally published online on November 14, 2008
Nucleic Acids Research 2009 37(1):47-59; doi:10.1093/nar/gkn901
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Nucleic Acids Research, 2009, Vol. 37, No. 1 47-59
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Far upstream element binding protein 2 interacts with enterovirus 71 internal ribosomal entry site and negatively regulates viral translation

Jing-Yi Lin1,2,3, Mei-Ling Li1,5 and Shin-Ru Shih1,2,3,4,*

1Research Center for Emerging Viral Infections, 2Department of Medical Biotechnology and Laboratory Science, 3Graduate Program in Biomedical Science, Chang Gung University, Tao-Yuan, 4Division of Biotechnology and Pharmaceutical Research, National Health Research Institutes, Zhunan, Taiwan and 5Department of Molecular Genetics, Microbiology and Immunology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ, USA

*To whom correspondence should be addressed. Tel: +886 3 2118800 (ext. 5497); Fax: +886 3 2118174; Email: srshih{at}mail.cgu.edu.tw

Received July 28, 2008. Revised October 25, 2008. Accepted October 27, 2008.

An internal ribosomal entry site (IRES) that directs the initiation of viral protein translation is a potential drug target for enterovirus 71 (EV71). Regulation of internal initiation requires the interaction of IRES trans-acting factors (ITAFs) with the internal ribosomal entry site. Biotinylated RNA-affinity chromatography and proteomic approaches were employed to identify far upstream element (FUSE) binding protein 2 (FBP2) as an ITAF for EV71. The interactions of FBP2 with EV71 IRES were confirmed by competition assay and by mapping the association sites in both viral IRES and FBP2 protein. During EV71 infection, FBP2 was enriched in cytoplasm where viral replication occurs, whereas FBP2 was localized in the nucleus in mock-infected cells. The synthesis of viral proteins increased in FBP2-knockdown cells that were infected by EV71. IRES activity in FBP2-knockdown cells exceeded that in the negative control (NC) siRNA-treated cells. On the other hand, IRES activity decreased when FBP2 was over-expressed in the cells. Results of this study suggest that FBP2 is a novel ITAF that interacts with EV71 IRES and negatively regulates viral translation.


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[Abstract] [Full Text] [PDF]


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