The molecular chaperone heat shock protein-90 positively regulates rotavirus infectionx

Dipanjan Dutta, Parikshit Bagchi, Arunachal Chatterjee, Mukti Kant Nayak, Anupam Mukherjee, Shiladitya Chattopadhyay, Shigeo Nagashima, Nobumichi Kobayashi, Satoshi Komoto, Koki Taniguchi, Mamta Chawla-Sarkar

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Abstract

Rotaviruses are the major cause of severe dehydrating gastroenteritis in children worldwide. In this study, we report a positive role of cellular chaperone Hsp90 during rotavirus infection. A highly specific Hsp90 inhibitor, 17-allylamono-demethoxygeldanamycin (17-AAG) was used to delineate the functional role of Hsp90. In MA104 cells treated with 17-AAG after viral adsorption, replication of simian (SA11) or human (KU) strains was attenuated as assessed by quantitating both plaque forming units and expression of viral genes. Phosphorylation of Akt and NFκB observed 2-4 hpi with SA11, was strongly inhibited in the presence of 17-AAG. Direct Hsp90-Akt interaction in virus infected cells was also reduced in the presence of 17-AAG. Anti-rotaviral effects of 17-AAG were due to inhibition of activation of Akt that was confirmed since, PI3K/Akt inhibitors attenuated rotavirus growth significantly. Thus, Hsp90 regulates rotavirus by modulating cellular signaling proteins. The results highlight the importance of cellular proteins during rotavirus infection and the possibility of targeting cellular chaperones for developing new anti-rotaviral strategies.

Original languageEnglish
Pages (from-to)325-333
Number of pages9
JournalVirology
Volume391
Issue number2
DOIs
Publication statusPublished - 01-09-2009

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All Science Journal Classification (ASJC) codes

  • Virology

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Dutta, D., Bagchi, P., Chatterjee, A., Nayak, M. K., Mukherjee, A., Chattopadhyay, S., Nagashima, S., Kobayashi, N., Komoto, S., Taniguchi, K., & Chawla-Sarkar, M. (2009). The molecular chaperone heat shock protein-90 positively regulates rotavirus infectionx. Virology, 391(2), 325-333. https://doi.org/10.1016/j.virol.2009.06.044