Heat shock protein 70 is necessary for Rice stripe virus infection in plants.
Heat shock proteins 70 (HSP70s) are a highly conserved family of genes in eukaryotes, and are involved in a remarkable variety of cellular processes. In many plant positive-stranded RNA viruses, HSP70 participates in the construction of a viral replication complex and plays various roles during viral infection. Here, we found increased expression of HSP70 following infection by Rice stripe virus (RSV), a negative-stranded RNA virus, in both rice (the natural host) and Nicotiana benthamiana (an experimental host). Heat treatment of N. benthamiana (Nb) plants enhanced viral infection, whereas RSV infection was retarded and viral RNAs accumulated at a low level when HSP70 was silenced. In both bimolecular fluorescence complement and in vitro pull-down assays, the N-terminus of RSV RNA-dependent RNA polymerase (RdRp) interacted and co-localized with the HSP70s of both plants (OsHSP70 and NbHSP70). The localization of the N-terminus of RdRp when expressed alone was not obviously different from when it was co-expressed with OsHSP or NbHSP, and vice versa. RSV infection also had no effect on the localization of host HSP70. These results demonstrate that host HSP70 is necessary for RSV infection and probably plays a role in viral replication by interacting with viral RdRp, which provides the first evidence of an interacting host protein related to RSV replication, which has been little studied to date.
College of Plant Protection, Nanjing Agricultural University, Nanjing, 210095, China; State Key Laboratory Breeding Base for Sustainable Control of Plant Pest and Disease, Ministry of China Key Laboratory of Biotechnology in Plant Protection, Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, 310021, China.
Shanshan
S
Jiang
Yuwen
Y
Lu
Kunfeng
K
Li
Lin
L
Lin
Hongying
H
Zheng
Fei
F
Yan
Jianping
J
Chen
D012321:DNA-Directed RNA Polymerases / Q000737:chemistry / Q000378:metabolism; D018506:Gene Expression Regulation, Plant / Q000187:drug effects; D020868:Gene Silencing / Q000187:drug effects; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D018869:Heat-Shock Response / Q000187:drug effects / Q000235:genetics; D008969:Molecular Sequence Data; D012275:Oryza / Q000187:drug effects / Q000235:genetics / Q000821:virology*; D010935:Plant Diseases / Q000821:virology*; D018515:Plant Leaves / Q000187:drug effects / Q000821:virology; D010940:Plant Proteins / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects; D021381:Protein Transport / Q000187:drug effects; D011794:Quercetin / Q000494:pharmacology; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D029364:Tenuivirus / Q000187:drug effects / Q000502:physiology*; D014026:Nicotiana / Q000187:drug effects / Q000235:genetics / Q000821:virology*
D018840:HSP70 Heat-Shock Proteins; D010940:Plant Proteins; D012333:RNA, Messenger; D012367:RNA, Viral; D011794:Quercetin; D012321:DNA-Directed RNA Polymerases
HSP70; Rice stripe virus; interaction; viral replication