scholarly journals Chicken Heat Shock Protein 90 Is a Component of the Putative Cellular Receptor Complex of Infectious Bursal Disease Virus

2007 ◽  
Vol 81 (16) ◽  
pp. 8730-8741 ◽  
Author(s):  
Ta-Wei Lin ◽  
Chi-Wen Lo ◽  
Su-Yuan Lai ◽  
Ruey-Jane Fan ◽  
Chao-Jung Lo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Infectious Bursal Disease Virus ◽  
Heat Shock Protein 90 ◽  
Infectious Bursal Disease ◽  
Cellular Receptor ◽  
Dependent Manner ◽  
Receptor Complex ◽  
Bursal Disease ◽  
Dose Dependent

ABSTRACT 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.

scholarly journals Inhibition of infectious bursal disease virus infection by artificial microRNAs targeting chicken heat-shock protein 90

2012 ◽  
Vol 93 (4) ◽  
pp. 876-879 ◽  
Author(s):  
Weifeng Yuan ◽  
Xinyu Zhang ◽  
Xiaoli Xia ◽  
Huaichang Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Infectious Bursal Disease Virus ◽  
Heat Shock Protein 90 ◽  
Infectious Bursal Disease ◽  
Cellular Receptor ◽  
Receptor Complex ◽  
Rt Pcr ◽  
Transfected Cells ◽  
Bursal Disease

Infectious bursal disease virus (IBDV) causes an important disease in young chickens. Chicken heat-shock protein 90 (cHsp90) has been shown to be a functional component of the cellular receptor complex for IBDV infection. This study demonstrates the inhibitory effect of vector-expressed anti-cHsp90α microRNA (miRNA) on IBDV infection. The reporter vectors pcHsp90α-EGFP and pcHsp90β-EGFP were constructed to facilitate effective miRNA selection. Two anti-cHsp90α and one anti-cHsp90β miRNA-expression vectors were constructed for a stable transfection study. Poly(A)-tailed RT-PCR detected sequence-specific miRNA transcription in transfected cells. Semiquantitative RT-PCR showed inhibition of cHsp90 transcription in transfected cells. A virus-titration assay showed that the anti-cHsp90α miRNA, but not the anti-cHsp90β miRNA, had inhibitory effects on IBDV infection. These results suggest that cHsp90α is a functional component of the cellular receptor complex for IBDV infection, and that anti-cHsp90α miRNA could be used as an anti-IBDV reagent.

scholarly journals Chicken Heat Shock Protein 70 Is an Essential Host Protein for Infectious Bursal Disease Virus Infection In Vitro

Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 664
Author(s):  
Yufang Meng ◽  
Xiaoxue Yu ◽  
Chunxue You ◽  
Wenjuan Zhang ◽  
Yingfeng Sun ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Disease Virus ◽  
Heat Shock Protein 70 ◽  
Infectious Bursal Disease Virus ◽  
Host Protein ◽  
Infectious Bursal Disease ◽  
Economic Losses ◽  
Small Interfering Rnas ◽  
Bursal Disease

Infectious bursal disease virus (IBDV) infection causes pathogenicity and mortality in chickens, leading to huge economic losses in the poultry industry worldwide. Studies of host-virus interaction can help us to better understand the viral pathogenicity. As a highly conservative host factor, heat shock protein 70 (Hsp70) is observed to be involved in numerous viral infections. However, there is little information about the role of chicken Hsp70 (cHsp70) in IBDV infection. In the present study, the increased expression of cHsp70 was observed during IBDV-infected DF-1 cells. Further studies revealed that Hsp70 had similar locations with the viral double-stranded RNA (dsRNA), and the result of pull-down assay showed the direct interaction between cHsp70 with dsRNA, viral proteins (vp)2 and 3, indicating that maybe cHsp70 participates in the formation of the replication and transcription complex. Furthermore, overexpression of cHsp70 promoted IBDV production and knockdown of cHsp70 using small interfering RNAs (siRNA) and reducedviral production, implying the necessity of cHsp70 in IBDV infection. These results reveal that cHsp70 is essential for IBDV infection in DF-1 cells, suggesting that targeting cHsp70 may be applied as an antiviral strategy.

scholarly journals Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

2002 ◽  
Vol 172 (2) ◽  
pp. 283-293 ◽  
Author(s):  
BK Brar ◽  
J Railson ◽  
A Stephanou ◽  
RA Knight ◽  
DS Latchman
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cardiac Myocytes ◽  
Primary Cultures ◽  
Heat Shock Protein 90 ◽  
Mitogen Activated Protein Kinase ◽  
Dependent Manner ◽  
Maximal Increase ◽  
Mitogen Activated Protein ◽  
Hsp90 Protein

We have previously demonstrated that urocortin protects cultured cardiac myocytes from ischaemic and reoxygenation injury and decreases the infarct size in the rat heart exposed to regional ischaemia and reperfusion. Urocortin-mediated cardioprotection is via activation of the mitogen-activated protein kinase (MAP kinase, MEK1/2) pathway. In addition, it is well documented that heat shock protein (hsp) 70 and hsp90 are cardioprotective against lethal stress. In this study we show, for the first time, that urocortin induces the expression of hsp90 but not hsp70 in primary cultures of rat neonatal cardiac myocytes. Levels of hsp90 protein increase by 1.5-fold over untreated cells within 10 min of urocortin treatment and are sustained for 24 h with a maximal increase of 2.5-fold at 60 min (P<0.05 at all time points). The increase in hsp90 expression by urocortin was not inhibited by actinomycin D, and urocortin failed to increase hsp90 promoter activity. Urocortin induction of hsp90 was inhibited by the MEK1/2 inhibitor PD98059 (P<0.001) and by cycloheximide, and both inhibitors abrogate urocortin-mediated cardioprotection (P<0.05 for cycloheximide, P<0.001 for PD98059). Hence, MEK1/2 and protein synthesis are involved in the cardioprotective effect of urocortin against hypoxic-mediated cell death, possibly due to an increase in expression of hsp90 protein. This is the first report of heat shock protein induction by urocortin or any other member of the corticotrophin-releasing hormone family.

Some characteristics of a cellular receptor for virulent infectious bursal disease virus by using flow cytometry

1998 ◽  
Vol 143 (12) ◽  
pp. 2327-2341 ◽  
Author(s):  
M. Ogawa ◽  
T. Yamaguchi ◽  
A. Setiyono ◽  
T. Ho ◽  
H. Matsuda ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Infectious Bursal Disease ◽  
Cellular Receptor ◽  
Bursal Disease

scholarly journals Expression and therapeutic relevance of heat-shock protein 90 in pancreatic endocrine tumors

2011 ◽  
Vol 19 (3) ◽  
pp. 217-232 ◽  
Author(s):  
Philipp Mayer ◽  
Andreas Harjung ◽  
Marco Breinig ◽  
Lars Fischer ◽  
Volker Ehemann ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Line ◽  
Therapeutic Effects ◽  
Endocrine Tumors ◽  
Human Pancreas ◽  
Dependent Manner ◽  
Hsp90 Inhibitors ◽  
Pancreatic Endocrine Tumors ◽  
Dose Dependent

Pancreatic endocrine tumors (PET) represent a heterogenous group of neoplasms. Although surgical resection is considered a safe and effective treatment for many PET, therapeutic options for inoperable and progressive PET are limited. The expression of heat-shock protein (HSP) 90 was investigated in 120 clinically and pathomorphologically well-characterized PET from 84 patients using immunohistochemistry. In addition, in 19 snap–frozen PET and in three healthy pancreatic tissues, we performed immunoblot analyses, and in 15 snap–frozen PET and in three healthy pancreatic tissues, we investigated the expression of HSP90 isoforms by means of semiquantitative RT-PCR. Functional tests were conducted using the human pancreas carcinoid cell line BON and the mouse insulinoma cell line β-TC-3. HSP90 was expressed in 95% of the PET patients. The transcript levels of the HSP90 isoforms HSP90α, HSP90β, glucose-related protein 94, and TNF receptor-associated protein 1 were significantly increased in PET compared with non-neoplastic pancreatic tissues. The treatment of the cell lines BON and β-TC-3 with the HSP90 inhibitors 17-allylamino-17-demethoxygeldanamycin and 17-dimethylaminoethylamino-17-demethoxy-geldanamycin resulted in significant, dose-dependent reduction of cell viability, cell cycle arrest, and increased apoptosis. Furthermore, HSP90 inhibition induced the degradation and inactivation of several oncogenetic HSP90 client proteins in a time- and dose-dependent manner. HSP90 inhibitors increased the therapeutic effects of doxorubicin and 5-fluorucacil in BON and β-TC-3 cells. HSP90 is expressed in the vast majority of PET and its inhibition reveals significant treatment effects in vitro. Thus, HSP90 qualifies as a promising new target.

scholarly journals Characteristics of Bursal T Lymphocytes Induced by Infectious Bursal Disease Virus

2000 ◽  
Vol 74 (19) ◽  
pp. 8884-8892 ◽  
Author(s):  
In-Jeong Kim ◽  
Seung Kwon You ◽  
Hyungee Kim ◽  
Hung-Yeuh Yeh ◽  
Jagdev M. Sharma
Keyword(s):  
T Cells ◽  
T Cell ◽  
B Cells ◽  
T Lymphocytes ◽  
Disease Virus ◽  
Infectious Bursal Disease Virus ◽  
Infectious Bursal Disease ◽  
Dependent Manner ◽  
Bursal Disease

ABSTRACT Infectious bursal disease virus (IBDV) is an avian lymphotropic virus that causes immunosuppression. When specific-pathogen-free chickens were exposed to a pathogenic strain of IBDV (IM), the virus rapidly destroyed B cells in the bursa of Fabricius. Extensive viral replication was accompanied by an infiltration of T cells in the bursa. We studied the characteristics of intrabursal T lymphocytes in IBDV-infected chickens and examined whether T cells were involved in virus clearance. Flow cytometric analysis of single-cell suspensions of the bursal tissue revealed that T cells were first detectable at 4 days postinoculation (p.i.). At 7 days p.i., 65% of bursal cells were T cells and 7% were B cells. After virus infection, the numbers of bursal T cells expressing activation markers Ia and CD25 were significantly increased (P < 0.03). In addition, IBDV-induced bursal T cells produced elevated levels of interleukin-6-like factor and nitric oxide-inducing factor in vitro. Spleen and bursal cells of IBDV-infected chickens had upregulated gamma interferon gene expression in comparison with virus-free chickens. In IBDV-infected chickens, bursal T cells proliferated in vitro upon stimulation with purified IBDV in a dose-dependent manner (P < 0.02), whereas virus-specific T-cell expansion was not detected in the spleen. Cyclosporin A treatment, which reduced the number of circulating T cells and compromised T-cell mitogenesis, increased viral burden in the bursae of IBDV-infected chickens. The results suggest that intrabursal T cells and T-cell-mediated responses may be important in viral clearance and promoting recovery from infection.

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