Suppression of thermotolerance in mumps virus-infected cells is caused by lack of HSP27 induction contributed by STAT-1.

作者: Shin-ichi Yokota , Noriko Yokosawa , Toru Kubota , Tamaki Okabayashi , Satoru Arata

DOI: 10.1074/JBC.M305701200

关键词:

摘要: Viral infection modulates the regulation of apoptosis in host cells. Here, we report a novel mechanism by which human cells infected with mumps virus become susceptible to caused extracellular stresses. Mumps stimulates proteasome-dependent degradation STAT-1 action viral accessory protein V, resulting severe decrease We exposed virus-infected and uninfected heat chemical stress. The failed acquire resistance apoptotic stimuli (thermotolerance) after exposure these mild induction HSP27 stress was dramatically suppressed cells, but HSP70 not affected. required for transcriptional activation gene, cDNA transfection restored thermotolerance. Phosphorylated shock factor-1 (HSF-1) phosphorylated on neither tyrosine nor serine residues were co-transported nucleus response Furthermore, overexpression unphosphorylatable mutants also thermotolerance These lines evidence indicate that requires addition activated HSF-1. worked independent its phosphorylation. Thus, HSP27-dependent is through destruction STAT-1. lack should allow be eliminated might defense against infection.

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