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http://purl.uniprot.org/citations/30006004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30006004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30006004http://www.w3.org/2000/01/rdf-schema#comment"Stress granules (SGs) are host translationally silent ribonucleo-proteins formed in cells in response to multiple types of environmental stress, including viral infection. We previously showed that the nuclear protein, 68-kDa Src-associated in mitosis protein (Sam68), is recruited to cytoplasm and form the Sam68-positive SGs at 6 hpi, but the Sam68-positive SGs disassembled beyond 12 hpi, suggesting that the SGs might be inhibited during the late stage of Enterovirus 71 (EV71) infection. However, the mechanism and function of this process remains poorly understood. Thus in this study, we demonstrated that EV71 initially induced SGs formation at the early stage of EV71 infection, and confirmed that 2Apro of EV71 was the key viral component that triggered SG formation. In contrast, SGs were diminished as EV71 infection proceeding. At the same time, arsenite-induced SGs were also blocked at the late stage of EV71 infection. This disruption of SGs was caused by viral protease 3Cpro-mediated G3BP1 cleavage. Furthermore, we demonstrated that over-expression of G3BP1-SGs negatively impacted viral replication at the cytopathic effect (CPE), protein, RNA, and viral titer levels. Our novel finding may not only help us to better understand the mechanism how EV71 interacts with the SG response, but also provide mechanistic linkage between cellular stress responses and innate immune activation during EV71 infection."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.org/dc/terms/identifier"doi:10.1016/j.virusres.2018.07.006"xsd:string
http://purl.uniprot.org/citations/30006004http://purl.org/dc/terms/identifier"doi:10.1016/j.virusres.2018.07.006"xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Cao H."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Cao H."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Cheng L."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Cheng L."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Li P."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Song B."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Song B."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Zhang H."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/30006004http://purl.uniprot.org/core/author"Xu J."xsd:string