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Journal of Virology, July 2005, p. 8113-8120, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8113-8120.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Novel Nuclear Export Signal-Interacting Protein, NESI, Critical for the Assembly of Hepatitis Delta Virus

Yun-Hsin Wang,1 Shin C. Chang,2 Cheng Huang,1 Ya-Ping Li,1 Chia-Huei Lee,1,{dagger} and Ming-Fu Chang1*

Institute of Biochemistry and Molecular Biology,1 Institute of Microbiology, National Taiwan University College of Medicine, Taipei, Taiwan2

Received 5 October 2004/ Accepted 14 February 2005

The process of host factor-mediated nucleocytoplasmic transport is critical for diverse cellular events in eukaryotes and the life cycle of viruses. We have previously identified a chromosome region maintenance 1-independent nuclear export signal (NES) at the C terminus of the large form of hepatitis delta antigen (HDAg), designated NES(HDAg-L) that is required for the assembly of hepatitis delta virus (HDV) (C.-H. Lee et al., J. Biol. Chem. 276:8142-8148, 2001). To look for interacting proteins of the NES(HDAg-L), yeast two-hybrid screening was applied using the GAL4-binding domain fused to the NES(HDAg-L) as bait. Among the positive clones, one encodes a protein, designated NESI [NES(HDAg-L) interacting protein] that specifically interacted with the wild-type NES(HDAg-L) but not with the export/package-defective HDAg-L mutant, NES*(HDAg-L), in which Pro-205 has been replaced by Ala. Northern blot analysis revealed NESI as the gene product of a 1.9-kb endogenous mRNA transcript that is present predominantly in human liver tissue. NESI consists of 467 amino acid residues and bears a putative actin-binding site and a bipartite nuclear localization signal. Specific interaction between HDAg-L and NESI was further confirmed by coimmunoprecipitation and immunofluorescence staining. Overexpression of antisense NESI RNAs inhibited the expression of NESI and abolished HDAg-L-mediated nuclear export and assembly of HDV genomic RNA. These data indicate a critical role of NESI in the assembly of HDV through interaction with HDAg-L.

* Corresponding author. Mailing address: Institute of Biochemistry and Molecular Biology, National Taiwan University College of Medicine, No. 1, Jen-Ai Road, First Section, Taipei 100, Taiwan. Phone: 886 2 23123456, ext. 8217. Fax: 886 2 23915295. E-mail: mfchang{at}ntumc.org.

{dagger} Present address: Fu Jen Catholic University School of Medicine, Taipei County, Taiwan, Republic of China.

Journal of Virology, July 2005, p. 8113-8120, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8113-8120.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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