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Encephalomyocarditis virus (EMCV) causes encephalitis, myocarditis, neuropathy, reproductive disorders, and diabetes in animals. EMCV is known to induce cell autophagy; however, the molecular mechanisms underlying this remain unclear. Here, we show that the type III-transmembrane protein, transmembrane protein 39A (TMEM39A), plays a critical role in EMCV replication. We showed that EMCV GS01 strain infection upregulated TMEM39A expression. Importantly, EMCV induced autophagy in a range of host cells. The autophagy chemical inhibitor, 3-MA, inhibited EMCV replication and reduced TMEM39A expression. This is the first study demonstrating TMEM39A promoting the replication of EMCV via autophagy. Overall, we show that TMEM39A plays a positive regulatory role in EMCV proliferation and that TMEM39A expression is dependent on the autophagy pathway.
Encephalomyocarditis virus (EMCV) is a small, non-enveloped, single stranded RNA virus which infects a wide variety of mammalian species, and has zoonotic importance. Many host proteins are known to regulate EMCV proliferation by interacting with its structural or nonstructural proteins, but the regulatory role and mechanism of heat shock protein 90β (HSP90β), in EMCV infection has not been reported yet. Here, we report that overexpression of HSP90β significantly promotes the growth and proliferation of EMCV in vitro. On the contrary, down-regulation of HSP90β by RNAi or geldanamycin inhibits EMCV replication. HSP90β suppresses IFN-β responses in the RLRs pathway by targeting the expression of the key adaptor molecules MAVS, TBK1, and IRF3, but not MDA5. This study demonstrates the firsthand information that HSP90β plays a positive role in viral proliferation by inhibiting EMCV induced IFN-β production. Collectively, the results reveal new insights into HSP90β-assisted progression of EMCV infection.
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