Aim: To explore the effects of HSP90 on rotavirus (RV) replication. Materials & methods: The interaction between NSP2 and HSP90 was analyzed by immunoprecipitation assay, and co-localization confirmed by an immunofluorescence assay. The viral titer was measured by immunofluorescence assay and viral protein expression investigated by western blotting. Results: The interaction between NSP2 and HSP90 was confirmed. Knockdown of HSP90 using siRNA resulted in a decrease in NSP2 expression and virus titer. HSP90 inhibitor 17-AAG significantly decreased NSP2 and NSP5 expression, as well as the virus titer, while proteasome inhibitor MG132 restored the protein amount and the viral titer. Conclusion: HSP90 is involved in rotavirus replication, and inhibition of HSP90 promotes the degradation of NSP2 through the proteasome pathway.
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Hu et al. (2024) studied this question.
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