資料載入中.....
|
請使用永久網址來引用或連結此文件:
https://irlib.pccu.edu.tw/handle/987654321/41918
|
題名: | Tat-enhanced delivery of the C terminus of HDAg-L inhibits assembly and secretion of hepatitis D virus |
作者: | Huang, HC (Huang, Hsiu-Chen) Lu, HF (Lu, Hsu-Feng) Lai, YH (Lai, Yu-Heng) Lee, CP (Lee, Chung-Pei) Liu, HK (Liu, Hui-Kang) Huang, C (Huang, Cheng) |
貢獻者: | 化學系所 |
關鍵詞: | NUCLEAR EXPORT SIGNAL DELTA-VIRUS B-VIRUS FUSION PROTEINS MESSENGER-RNA LARGE FORM ANTIGEN REPLICATION CELLS IDENTIFICATION |
日期: | 2018-02 |
上傳時間: | 2019-01-21 15:26:12 (UTC+8) |
摘要: | Hepatitis D virus (HDV) contains a single-stranded circular RNA genome that encodes two forms of hepatitis delta antigen (HDAg), the small delta antigen (HDAg-S) and the large delta antigen (HDAg-L). The two proteins have an identical amino acid sequence, except that HDAg-L has a 19-amino-acid extension at the C terminus. The domain spanning amino acid residues 198-210 of the HDAg-L (HDAg-L(198-210)) contains a nuclear export signal (NES), which is important for the nuclear export of HDV ribonucleoprotein to the cytoplasm. In this study, we established a cell permeable TAT-HA-HDAg-L(198-210) fusion protein using an E. coli protein expression system, to determine its function during HDV infection. The cytotoxicity of the TAT-HA-HDAg-L(198-210) fusion protein was investigated using an MTT assay, while a GST pull-down assay revealed that the TAT-HA-HDAg-L (198-210) fusion protein interfered with the interaction between HDAg-L and clathrin heavy chain (CHC). In addition, the cellular distribution of HDAg-L, in the presence of HBsAg, was observed by immunofluorescence staining and the TAT-HA-HDAg-L(198-210) fusion protein was found to impede the nuclear export of HDAg-L. Furthermore, assembly of HDV virus-like particles (VLPs) was decreased by the expression of the TAT-HDAg-L (198-210) fusion protein. The TAT-HA-HDAg-L(198-210) fusion protein also inhibited virus particle assembly and HDV secretion in a mouse model. These results suggest that the TAT-HA-HDAg-L(198-210) fusion protein inhibits the nuclear export of HDAg-L and competes with the C terminus of HDAg-L for interaction with CHC, and may have potential as a therapeutic agent for HDV infection. |
關聯: | Antiviral Research卷 150, 頁 69 - 78 February 2018 |
顯示於類別: | [化學系所] 期刊論文
|
文件中的檔案:
檔案 |
描述 |
大小 | 格式 | 瀏覽次數 |
index.html | | 0Kb | HTML | 154 | 檢視/開啟 |
|
在CCUR中所有的資料項目都受到原著作權保護.
|