Active Participation of Cellular Chaperone Hsp90 in Regulating the Function of Rotavirus Nonstructural Protein 3 (NSP3)

Dutta, Dipanjan; Chattopadhyay, Shiladitya; Bagchi, Parikshit; Halder, Umesh Chandra; Nandi, Satabdi; Mukherjee, Anupam; Kobayashi, Nobumichi; Taniguchi, Koki; Chawla‐Sarkar, Mamta

doi:10.1074/jbc.m111.231878

Cited by 30 publications

(36 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hsp90 physically interacts with LT and Hsp90 inhibition with GA or radicicol leads to its degradation in cells. Similarly, for rotavirus, nonstructural protein 3 (NSP3) also requires Hsp90 for folding and stabilization [66]. NSP3 shuts off cellular translation by relocalizing the cytoplasmic poly(A) binding protein (PABP-C1) to the nucleus, thereby evicting it from translation initiation complexes in infected cells [67-69].…”

Section: Viral Non-structural Proteins As Hsp90 Clientsmentioning

confidence: 99%

“…NSP3 shuts off cellular translation by relocalizing the cytoplasmic poly(A) binding protein (PABP-C1) to the nucleus, thereby evicting it from translation initiation complexes in infected cells [67-69]. Inhibition of Hsp90 by 17-AAG or 17-DMAG resulted in reduced NSP3 translation and abolishes nuclear translocation of PABP-C1, thus suppressing viral replication [66, 70]. …”

Section: Viral Non-structural Proteins As Hsp90 Clientsmentioning

confidence: 99%

See 1 more Smart Citation

Broad action of Hsp90 as a host chaperone required for viral replication

Geller

Taguwa

Frydman

2012

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

202

212

View full text Add to dashboard Cite

Viruses are intracellular pathogens responsible for a vast number of human diseases. Due to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for their replication. Recent work has shown that the molecular chaperone Hsp90 is nearly universally required for viral protein homeostasis. As observed for many endogenous cellular proteins, numerous different viral proteins have been shown to require Hsp90 for their folding, assembly, and maturation. Importantly, the unique characteristics of viral replication cause viruses to be hypersensitive to Hsp90 inhibition, thus providing a novel therapeutic avenue for the development of broad-spectrum antiviral drugs. The major developments in this emerging field are hereby discussed.

show abstract

Section: Viral Non-structural Proteins As Hsp90 Clientsmentioning

confidence: 99%

Section: Viral Non-structural Proteins As Hsp90 Clientsmentioning

confidence: 99%

Broad action of Hsp90 as a host chaperone required for viral replication

Geller

Taguwa

Frydman

2012

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

202

212

View full text Add to dashboard Cite

show abstract

“…The cells were fixed at 0 hpi, 3 hpi and 9 hpi with 4% paraformaldehyde (w/v in PBS) for 10 mins at room temperature and permeabilized with 0.1% Triton-X-100 for 15 mins at 4°C. The remaining protocol was followed as described previously [29], [30]. The slides were examined either under a confocal or a fluorescence microscope (Carl Zeiss, Gottingen, Germany).…”

Section: Methodsmentioning

confidence: 99%

“…Full-length NSP3 and VP6 from RV-SA11 which has been cloned previously into the pCDNA6 (Invitrogen, USA) in our lab were used here [29]. The vectors were transfected into 293 cells using the Lipofectamine 2000 tranfection reagent (Invitrogen, USA) according to the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

Identification of Cellular Calcium Binding Protein Calmodulin as a Regulator of Rotavirus A Infection during Comparative Proteomic Study

et al. 2013

Self Cite

View full text Add to dashboard Cite

Rotavirus (RV) being the major diarrhoegenic virus causes around 527000 children death (<5years age) worldwide. In cellular environment, viruses constantly adapt and modulate to survive and replicate while the host cell also responds to combat the situation and this results in the differential regulation of cellular proteins. To identify the virus induced differential expression of proteins, 2D-DIGE (Two-dimensional Difference Gel Electrophoresis) based proteomics was used. For this, HT-29 cells were infected with RV strain SA11 for 0 hours, 3 hours and 9 hours post infection (hpi), differentially expressed spots were excised from the gel and identified using MALDI-TOF/TOF mass spectrometry. 2D-DIGE based proteomics study identified 32 differentially modulated proteins, of which 22 were unique. Some of these were validated in HT-29 cell line and in BALB/c mice model. One of the modulated cellular proteins, calmodulin (CaM) was found to directly interact with RV protein VP6 in the presence of Ca2+. Ca2+-CaM/VP6 interaction positively regulates RV propagation since both CaM inhibitor (W-7) and Ca2+ chelator (BAPTA-AM) resulted in decreased viral titers. This study not only identifies differentially modulated cellular proteins upon infection with rotavirus in 2D-DIGE but also confirmed positive engagement of cellular Ca2+/CaM during viral pathogenesis.

show abstract

“…Both NSP1 and NSP4 have counteracting functions to maintain cellular homeostasis. Thus, an overall study reveals how viruses employ multifunctional viral proteins to modulate the innate host immune defense such as apoptosis and pro inflammatory responses for their own benefit Dutta et al, 2011;Bagchi et al, 2013 . iii Metabolic regulation of Giardia lamblia during oxidative stressed conditions.…”

Section: El Tor Variant V Choleramentioning

confidence: 99%

International Collaborative Research on Infectious Diseases by Japanese Universities and Institutes in Asia and Africa, with a Special Emphasis on J-GRID

Shinoda¹,

Imamura²,

Mizuno³

et al. 2015

Biocontrol Sci.

View full text Add to dashboard Cite

In developed countries including Japan, malignant tumor cancer , heart disease and cerebral apoplexy are major causes of death, but infectious diseases are still responsible for a high number of deaths in developing countries, especially among children aged less than 5 years. World Health Statistics published by WHO reports a high percentage of mortality from infectious diseases in children, and many of these diseases may be subject to transmission across borders and could possibly invade Japan. This review article outlines project of J-GRID and CRCOUI which the authors carried out collaboratively with NICED staff members.

show abstract

Active Participation of Cellular Chaperone Hsp90 in Regulating the Function of Rotavirus Nonstructural Protein 3 (NSP3)

Cited by 30 publications

References 58 publications

Broad action of Hsp90 as a host chaperone required for viral replication

Broad action of Hsp90 as a host chaperone required for viral replication

Identification of Cellular Calcium Binding Protein Calmodulin as a Regulator of Rotavirus A Infection during Comparative Proteomic Study

International Collaborative Research on Infectious Diseases by Japanese Universities and Institutes in Asia and Africa, with a Special Emphasis on J-GRID

Contact Info

Product

Resources

About