https://scholars.lib.ntu.edu.tw/handle/123456789/431074
標題: | A Novel Chromosome Region Maintenance 1-independent Nuclear Export Signal of the Large Form of Hepatitis Delta Antigen That Is Required for the Viral Assembly | 作者: | Lee C.-H. SHIN CHANG Wu C.H.H. MING-FU CHANG |
公開日期: | 2001 | 卷: | 276 | 期: | 11 | 起(迄)頁: | 8142-8148 | 來源出版物: | Journal of Biological Chemistry | 摘要: | Hepatitis delta virus (HDV) is a satellite virus of hepatitis B virus, as it requires hepatitis B virus for virion production and transmission. We have previously demonstrated that sequences within the C-terminal 19-amino acid domain flanking the isoprenylation motif of the large hepatitis delta antigen (HDAg-L) are important for virion assembly. In this study, site-directed mutagenesis and immunofluorescence staining demonstrated that in the absence of hepatitis B virus surface antigen (HBsAg), the wild-type HDAg-L was localized in the nuclei of transfected COS7 cells. Nevertheless, in the presence of HBsAg, the HDAg-L became both nuclei- and cytoplasm-distributed in about half of the cells. An HDAg-L mutant with a substitution of Pro-205 to alanine could neither form HDV-like particles nor shift the subcellular localization in the presence of HBsAg. In addition, nuclear trafficking of HDAg-L in heterokaryons indicated that HDAg-L is a nucleocytoplasmic shuttling protein. A proline-rich HDAg peptide spanning amino acid residues 198 to 210, designated NES(HDAg-L), can function as a nuclear export signal (NES) in Xenopus oocytes. Pro-205 is critical for the NES function. Furthermore, assembly of HDV is insensitive to leptomycin B, indicating that the NES(HDAg-L) directs nuclear export of HDAg-L to the cytoplasm via a chromosome region maintenance 1-independent pathway. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035896539&doi=10.1074%2fjbc.M004477200&partnerID=40&md5=e1f6994cb8f1397e12a238d19c386d2b https://scholars.lib.ntu.edu.tw/handle/123456789/431074 |
DOI: | 10.1074/jbc.M004477200 | SDG/關鍵字: | Amino acids; Antigens; Chromosomes; Cytology; Fluorescence; Immunology; Mutagenesis; Immunofluorescence; Virion transmission; Viruses; hepatitis B surface antigen; hepatitis delta antigen; hepatitis antigen; hepatitis B surface antigen; hepatitis delta antigen; hepatitis delta virus large antigen; leptomycin B; unsaturated fatty acid; animal cell; article; cell strain COS7; Hepatitis delta virus; nonhuman; priority journal; protein localization; protein protein interaction; signal transduction; virus assembly; virus cell interaction; active transport; animal; cell line; chromosome; cytoplasm; drug effect; Hepatitis delta virus; human; metabolism; mouse; physiology; Animalia; Hepatitis B virus; Hepatitis delta virus; Nes; Satellite Viruses; delta virus; Active Transport, Cell Nucleus; Animals; Cell Line; Chromosomes; Cytoplasm; Fatty Acids, Unsaturated; Hepatitis Antigens; Hepatitis B Surface Antigens; Hepatitis delta Antigens; Hepatitis Delta Virus; Humans; Mice; Virus Assembly |
顯示於: | 生物化學暨分子生物學科研究所 |
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