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

• DOI: 10.1074/jbc.m111.231878
• Publication Date: 2011-04-14T00:17:01Z
• Authors: Dipanjan Dutta; Shiladitya Chatto...; Parikshit Bagchi; Umesh Chandra Halder; Satabdi Nandi; Anupam Mukherjee; Nobumichi Kobayashi; Koki Taniguchi; Mamta Chawla-Sarkar
• Keywords: EIF4G; Poly(N-isopropylacrylamide); Chaperone (clinical); Viral protein

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 folding stabilization nonstructural 3 (NSP3). In pCD-NSP3-transfected cells, treatment with inhibitor (17-N,N-dimethylethylenediamine-geldanamycin (17DMAG)) resulted proteasomal degradation NSP3. Sequence analysis deletion mutations revealed that region spanning amino acids 225-258 within C-terminal eIF4G-binding domain NSP3 is a putative binding region. Co-immunoprecipitation mammalian two-hybrid experiments direct interaction 12-kDa (C90) residues NSP3-Hsp90 important for formation functionally mature NSP3, because full-length presence or lacking acid did not show dimers following vitro coupled transcription-translation followed chase. Disruption also poor RNA eIF4G activity. addition, inhibition 17DMAG reduced nuclear translocation poly(A)-binding translation viral proteins. These results highlight crucial role chaperone regulation assembly functionality during propagation host cells.