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http://purl.uniprot.org/citations/29117567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29117567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/29117567http://www.w3.org/2000/01/rdf-schema#comment"Flaviviruses are enveloped, positive-sensed single-stranded RNA viruses that remodel host membranes, incorporating both viral and host factors facilitating viral replication. In this study, we identified a key role for the membrane-bending host protein Reticulon 3.1 (RTN3.1A) during the replication cycle of three flaviviruses: West Nile virus (WNV), Dengue virus (DENV), and Zika virus (ZIKV). We observed that, during infection, RTN3.1A is redistributed and recruited to the viral replication complex, a recruitment facilitated via the WNV NS4A protein, however, not DENV or ZIKV NS4A. Critically, small interfering RNA (siRNA)-mediated knockdown of RTN3.1A expression attenuated WNV, DENV, and ZIKV replication and severely affected the stability and abundance of the NS4A protein, coinciding with a significant alternation and reduction of viral membrane structures in the endoplasmic reticulum. These observations identified a crucial role of RTN3.1A for the viral remodelling of host membranes during efficient flavivirus replication and the stabilization of viral proteins within the endoplasmic reticulum."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.10.055"xsd:string
http://purl.uniprot.org/citations/29117567http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2017.10.055"xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Simmons C.P."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Simmons C.P."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Mackenzie J.M."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Mackenzie J.M."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Aktepe T.E."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Aktepe T.E."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Liebscher S."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Liebscher S."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Prier J.E."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/author"Prier J.E."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/pages"1639-1654"xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/pages"1639-1654"xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/title"The host protein reticulon 3.1A is utilized by flaviviruses to facilitate membrane remodelling."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/title"The host protein reticulon 3.1A is utilized by flaviviruses to facilitate membrane remodelling."xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/29117567http://purl.uniprot.org/core/volume"21"xsd:string