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Journal of Virology, August 2007, p. 8730-8741, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00332-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus{triangledown}

Ta-Wei Lin,1,{dagger} Chi-Wen Lo,1,{dagger} Su-Yuan Lai,2 Ruey-Jane Fan,1 Chao-Jung Lo,1 Yu-mei Chou,1 Rekha Thiruvengadam,1 Andrew H.-J. Wang,3* and Min-Ying Wang1*

Graduate Institute of Biotechnology, National Chung Hsing University, Taichung 40227, Taiwan,1 Department of Food Science, Central Taiwan University of Science and Technology, Taichung 40605, Taiwan,2 Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan3

Received 14 February 2007/ Accepted 14 May 2007

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.

* Corresponding author. Mailing address: Graduate Institute of Biotechnology, National Chung Hsing University, Taichung 40227, Taiwan. Phone for Min-Ying Wang: 886-4-2285-6697. Fax: 886-4-2285-3527. E-mail: mywang{at}dragon.nchu.edu.tw. Phone for Andrew H.-J. Wang: 886-2-2788-1981. Fax: 886-2-2788-2043. E-mail: ahjwang{at}gate.sinica.edu.tw

{triangledown} Published ahead of print on 23 May 2007.

{dagger} T.-W.L. and C.-W.L. contributed equally to this work.

Journal of Virology, August 2007, p. 8730-8741, Vol. 81, No. 16
0022-538X/07/$08.00+0     doi:10.1128/JVI.00332-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Delgui, L., Gonzalez, D., Rodriguez, J. F. (2009). Infectious bursal disease virus persistently infects bursal B-lymphoid DT40 cells. J. Gen. Virol. 90: 1148-1152 [Abstract] [Full Text]  


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