Cellular Nuclear Export Factors TAP and Aly Are Required for HDAg-L-mediated Assembly of Hepatitis Delta Virus

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题名:	Cellular Nuclear Export Factors TAP and Aly Are Required for HDAg-L-mediated Assembly of Hepatitis Delta Virus
作者:	Huang, HC (Huang, Hsiu-Chen) Lee, CP (Lee, Chung-Pei) Liu, HK (Liu, Hui-Kang) Chang, MF (Chang, Ming-Fu) Lai, YH (Lai, Yu-Heng) Lee, YC (Lee, Yu-Ching) Huang, C (Huang, Cheng)
贡献者:	化學系
关键词:	MESSENGER-RNA EXPORT FRAGMENT-LENGTH-POLYMORPHISM HUMAN PRIMARY HEPATOCYTES SIGNAL-INTERACTING PROTEIN B SURFACE-ANTIGEN LARGE FORM REPLICATION DOMAIN IDENTIFICATION TRANSPORT
日期:	2016-12-09
上传时间:	2017-02-10 14:15:21 (UTC+8)
摘要:	Hepatitis delta virus (HDV) is a satellite virus of hepatitis B virus (HBV). HDV genome encodes two forms of hepatitis delta antigen (HDAg), small HDAg (HDAg-S), which is required for viral replication, and large HDAg (HDAg-L), which is essential for viral assembly. HDAg-L is identical to HDAg-S except that it bears a 19-amino acid extension at the C terminus. Both HDAgs contain a nuclear localization signal (NLS), but only HDAg-L contains a CRM1-independent nuclear export signal at its C terminus. The nuclear export activity of HDAg-L is important for HDV particle formation. However, the mechanisms of HDAg-L-mediated nuclear export of HDV ribonucleoprotein are not clear. In this study, the host cellular RNA export complex TAP-Aly was found to form a complex with HDAg-L, but not with an export-defective HDAg-Lmutant, in which Pro(205) was replaced by Ala. HDAg-L was found to colocalize with TAP and Aly in the nucleus. The C-terminal domain of HDAg-L was shown to directly interact with the N terminus of TAP, whereas an HDAg-L mutant lacking the NLS failed to interact with full-length TAP. In addition, small hairpin RNA-mediated down-regulation of TAP or Aly reduced nuclear export of HDAg-L and assembly of HDV virions. Furthermore, a peptide, TAT-HDAg-L(198-210), containing the 10-amino acid TAT peptide and HDAg-L(198-210), inhibited the interaction between HDAg-L and TAP and blocked HDV virion assembly and secretion. These data demonstrate that formation and release of HDV particles are mediated by TAP and Aly.
關聯:	JOURNAL OF BIOLOGICAL CHEMISTRY 卷: 291 期: 50 頁碼:26226-26238
显示于类别:	[化學系所] 期刊論文

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