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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張明富 | |
| dc.contributor.author | Ya-Lun Chiu | en |
| dc.contributor.author | 邱雅倫 | zh_TW |
| dc.date.accessioned | 2021-06-13T00:27:59Z | - |
| dc.date.available | 2012-08-08 | |
| dc.date.copyright | 2007-08-08 | |
| dc.date.issued | 2007 | |
| dc.date.submitted | 2007-07-26 | |
| dc.identifier.citation | 1 Rizzetto, M., Canese, M. G., Arico, S., Crivelli, O., Trepo, C., Bonino, F. and Verme, G. (1977) Immunofluorescence detection of new antigen-antibody system (delta/anti-delta) associated to hepatitis B virus in liver and in serum of HBsAg carriers. Gut 18, 997-1003
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/28888 | - |
| dc.description.abstract | D型肝炎病毒(hepatitis delta virus; HDV)是個球狀的RNA病毒，其病毒顆粒的外套(envelope)由HBV的表面抗原與細胞膜組成，內部則為約1.7 kb單股負向的環狀RNA基因體及其轉譯產生的兩種delta抗原，分別為小型delta抗原(HDAg-S)，含195個胺基酸（約24kDa）；以及大型delta抗原(HDAg-L)，含214個胺基酸（約27 kDa）。在HDV的病毒生活史中，小型delta抗原為病毒複製所必須，而大型delta抗原可與HBV的表面抗原結合，對病毒顆粒的包裹是重要的。
本實驗室先前的研究發現，大型delta抗原C端第198至210個胺基酸為proline-rich的核輸出訊號(nuclear export signal; NES)，命名為NES(HDAg-L)，此NES藉由CRM1-independent pathway進行大型delta抗原的細胞核輸出，且宿主蛋白質NESI 【NES(HDAg-L)-interacting protein】，可調控病毒基因體-抗原複合體的核輸出及病毒顆粒的包裹。 NESI蛋白質具有467個胺基酸（約53kDa），經由序列分析，其第4至13個胺基酸可能會與肌動蛋白（actin）結合，而第193至209個胺基酸可能為核位訊號（nuclear localization signal; NLS）。先前的研究證實NESI胺基酸1-185片段可與肌動蛋白結合，且knock down NESI的表現可觀察到細胞的移動能力增加，但其分子機制未明。本論文利用免疫沈澱法再次證明NESI與肌動蛋白間的專一性結合，並以GST pull-down assay發現NESI N端的30個胺基酸為兩者的交互作用所必須。而帶有肌動蛋白結合區突變的NESI蛋白質則喪失與肌動蛋白的能力，顯示其actinin-type actin binding domain 之consensus sequence對NESI-actin複合體形成的重要性。以免疫螢光染色觀察到NESI分布在細胞核中及細胞質裡靠近核的位置，且在細胞質的NESI與F-actin有共位現象(co-localization)，但是在活體外（in vitro）結合實驗中，並沒有觀察到NESI(1-30)胜肽與純化的F-actin共同沈降，對溶液中G-actin與F-actin的動態平衡也沒有明顯影響。 | zh_TW |
| dc.description.abstract | Hepatitis delta virus (HDV) is a spherical RNA virus, which is enveloped by the surface antigens of the hepatitis B virus. Inside the viral particles, HDV contains a single-stranded, negative sense, circular RNA genome of 1.7 kb and its only known products, small delta antigen (HDAg-S) and large delta antigen (HDAg-L). Previous studies from our laboratory identified a novel proline-rich nuclear export signal at the C-terminus of HDAg-L, designated NES(HDAg-L). In addition, host protein NESI which specifically interacts with NES(HDAg-L) participated in nuclear export of HDV RNP complex and virus assembly. NESI consists of 467 amino acid residues. It bears a putative actin binding site and a bipartite nuclear localization signal. Association of NESI(1-185) and actin was demonstrated in our laboratory. In addition, In NESI-knockdown cells, the cell mobility was increased in the scratch assay. However, regulations of the putative actin-binding domain from amino acid residues 4 to 13 in the cell mobility are unclear.
In this study, the specific interaction between NESI and actin was further confirmed by co-immuoprecipitation analysis. GST pull-down assay indicates that the N-terminal 30 amino acid residues are required for NESI to interact with actin. The actin-binding ability of NESI protein was lost when mutations were introduced into the actin binding domain. These results indicate that the consensus sequence of the actinin-type actin binding domain is important for NESI-actin complex formation. Immunofluorescence staining demonstrated that NESI localized in the nucleus and the perinuclear region. The cytoplasmic NESI co-localized with F-actin. However, no co-sedimentation of NESI(1-30) peptide with purified F-actin was detected, and no significant changes in the equilibrium between G-actin and F-actin was observed in a in vitro binding assay. These results suggest that, unlike alpha-actinin, NESI may not function as F-actin bundling. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T00:27:59Z (GMT). No. of bitstreams: 1 ntu-96-R94442005-1.pdf: 1111717 bytes, checksum: be6cfcbdd8fa0fd0fdab085b0e6becfb (MD5) Previous issue date: 2007 | en |
| dc.description.tableofcontents | 中文摘要.................i
英文摘要.................ii 縮寫表...................iii 緒論.....................1 實驗材料來源.............14 實驗方法.................18 實驗結果.................31 討論.....................34 圖表.....................37 參考文獻.................50 | |
| dc.language.iso | zh-TW | |
| dc.subject | 核輸出訊息 | zh_TW |
| dc.subject | D型肝炎 | zh_TW |
| dc.subject | 肌動蛋白 | zh_TW |
| dc.subject | actin | en |
| dc.subject | HDV | en |
| dc.subject | NESI | en |
| dc.subject | NES | en |
| dc.title | 核輸出訊息結合蛋白質NESI之肌動蛋白結合區之功能分析 | zh_TW |
| dc.title | Functional analysis of the putative actin-binding domain of NESI protein | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 95-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 李芳仁,李明學 | |
| dc.subject.keyword | D型肝炎,肌動蛋白,核輸出訊息, | zh_TW |
| dc.subject.keyword | HDV,actin,NES,NESI, | en |
| dc.relation.page | 59 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2007-07-26 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 生物化學暨分子生物學研究所 | zh_TW |
| 顯示於系所單位： | 生物化學暨分子生物學科研究所 | |
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| ntu-96-1.pdf 未授權公開取用 | 1.09 MB | Adobe PDF |
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