ArticleThe Journal of biological chemistry2011
Active participation of cellular chaperone Hsp90 in regulating the function of rotavirus nonstructural protein 3 (NSP3).
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 14 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- Review
- Advances in the development of antivirals for rotavirus infection.Frontiers in immunology · 2023Review
- Induction of Cell Death in the Human Acute Lymphoblastic Leukemia Cell Line Reh by Infection with Rotavirus Isolate Wt1-5.Biomedicines · 2020Article
- Assessing the oncolytic potential of rotavirus on mouse myeloma cell line Sp2/0-Ag14.Biomedica : revista del Instituto Nacional de Salud · 2020Article
- Biphasic regulation of RNA interference during rotavirus infection by modulation of Argonaute2.Cellular microbiology · 2019Article
- Hsp90 Chaperones Bluetongue Virus Proteins and Prevents Proteasomal Degradation.Journal of virology · 2019Article
- Rotavirus Infection Alters Splicing of the Stress-Related Transcription Factor XBP1.Journal of virology · 2019Article
- The Host Heat Shock Protein MRJ/DNAJB6 Modulates Virus Infection.Frontiers in microbiology · 2019Review
- Protein disulfide isomerases as potential therapeutic targets for influenza A and B viruses.Virus research · 2018Article
- Species A rotavirus NSP3 acquires its translation inhibitory function prior to stable dimer formation.PloS one · 2017Article
- Review
- Article
- Article
- Broad action of Hsp90 as a host chaperone required for viral replication.Biochimica et biophysica acta · 2012Review
Corrections and comments
- Retraction · 2020-09-25Concerns/Issues about Data · Concerns/Issues about Image · Upgrade/Update of Prior Notice(s) ·
- Expression of concern · 2019-10-11Concerns/Issues about Data · Concerns/Issues about Results and/or Conclusions · Updated to Retraction ·
- Expression of concern
- Retracted
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat shock protein 90 (Hsp90) has been reported to positively regulate rotavirus replication by modulating virus induced PI3K/Akt and NFκB activation. Here, we report the active association of Hsp90 in the folding and stabilization of rotavirus nonstructural protein 3 (NSP3). In pCD-NSP3-transfected cells, treatment with Hsp90 inhibitor (17-N,N-dimethylethylenediamine-geldanamycin (17DMAG)) resulted in the proteasomal degradation of NSP3. Sequence analysis and deletion mutations revealed that the region spanning amino acids 225-258 within the C-terminal eIF4G-binding domain of NSP3 is a putative Hsp90 binding region. Co-immunoprecipitation and mammalian two-hybrid experiments revealed direct interaction of the C-terminal 12-kDa domain of Hsp90 (C90) with residues 225-258 of NSP3. NSP3-Hsp90 interaction is important for the formation of functionally active mature NSP3, because full-length NSP3 in the presence of the Hsp90 inhibitor or NSP3 lacking the amino acid 225-258 region did not show NSP3 dimers following in vitro coupled transcription-translation followed by chase. Disruption of residues 225-258 within NSP3 also resulted in poor RNA binding and eIF4G binding activity. In addition, inhibition of Hsp90 by 17DMAG resulted in reduced nuclear translocation of poly(A)-binding protein and translation of viral proteins. These results highlight the crucial role of Hsp90 chaperone in the regulation of assembly and functionality of a viral protein during the virus replication and propagation in host cells.
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