English  |  正體中文  |  简体中文  |  Items with full text/Total items : 43312/67235
Visitors : 2167245      Online Users : 23
RC Version 5.0 © Powered By DSPACE, MIT. Enhanced by NTU/NCHU Library IR team.
National Chung Hsing University Institutional Repository - NCHUIR > 生命科學院 > 基因體暨生物資訊學研究所 > 依資料類型分類 > 期刊論文 >  Chicken heat shock protein 90 is a component of the putative cellular receptor complex of infectious bursal disease virus

Please use this identifier to cite or link to this item: http://nchuir.lib.nchu.edu.tw/handle/309270000/133521

標題: Chicken heat shock protein 90 is a component of the putative cellular receptor complex of infectious bursal disease virus
作者: Lin, T.W.;Lo, C.W.;Lai, S.Y.;Fan, R.J.;Lo, C.J.;Chou, Y.M.;Thiruvengadam, R.;Wang, A.H.J.;Wang, M.Y.
關鍵字: ion affinity-chromatography;crystal-structure;influenza-virus;binding;domain;capsid protein;hiv-1 entry;heat-shock;cells;particles;vp2
日期: 2007
Issue Date: 2012-12-14 10:00:14 (UTC+8)
關連: Journal of Virology, Volume 81, Issue 16, Page(s) 8730-8741.
摘要: Infectious bursal disease virus (IBDV) causes a highly contagious disease in young chicks and leads to significant economic losses in the poultry industry. The capsid protein VP2 of IBDV plays an important role in virus binding and cell recognition. VP2 forms a subviral particle (SVP) with immunogenicity similar to that of the IBDV capsid. In the present study, we first showed that SVP could inhibit IBDV infection to an IBDV-susceptible cell line, DF-1 cells, in a dose-dependent manner. Second, the localizations of the SVP on the surface of DF-1 cells were confirmed by fluorescence microscopy, and the specific binding of the SVP to DF-1 cells occurred in a dose-dependent manner. Furthermore, the attachment of SVP to DF-1 cells was inhibited by an SVP-induced neutralizing monoclonal antibody against IBDV but not by denatured-VP2-induced polyclonal antibodies. Third, the cellular factors in DF-1 cells involved in the attachment of SVP were purified by affinity chromatography using SVP bound on the immobilized Ni2+ ions. A dominant factor was identified as being chicken heat shock protein 90 (Hsp90) (cHsp90) by mass spectrometry. Results of biotinylation experiments and indirect fluorescence assays indicated that cHsp90 is located on the surface of DF-1 cells. Virus overlay protein binding assays and far-Western assays also concluded that cHsp90 interacts with IBDV and SVP, respectively. Finally, both Hsp90 and anti-Hsp90 can inhibit the infection of DF-1 cells by IBDV. Taken together, for the first time, our results suggest that cHsp90 is part of the putative cellular receptor complex essential for IBDV entry into DF-1 cells.
Relation: Journal of Virology
Appears in Collections:[依資料類型分類] 期刊論文
[依教師分類] 王敏盈

loading Web of Knowledge data....

Files in This Item:

File SizeFormat






聯絡網站維護人員:wyhuang@nchu.edu.tw,04-22840290 # 412。

DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU/NCHU Library IR team Copyright ©   - Feedback