A furoviral replicase recruits host HSP70 to membranes for viral RNA replication

• Published in: Scientific reports Vol. 7; no. 1; p. 45590
• Main Authors: Yang, Jian, Zhang, Fen, Cai, Nian-Jun, Wu, Ne, Chen, Xuan, Li, Jing, Meng, Xiang-Feng, Zhu, Tong-Quan, Chen, Jian-Ping, Zhang, Heng-Mu
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 03.04.2017; Nature Publishing Group
• Subjects: 13/89; 14/19; 631/326/596/2557; 631/449/2661/2666; 82/1; 82/80; Cell Membrane - metabolism; Cell Membrane - virology; Cereals; Chaperones; Cytoplasm; Gene Expression Regulation, Viral; HSP70 Heat-Shock Proteins - metabolism; Hsp70 protein; Humanities and Social Sciences; Infections; multidisciplinary; Nicotiana - enzymology; Nicotiana - genetics; Nicotiana - virology; Nuclei; Plant Diseases - virology; Potyvirus - physiology; Replicase; Replication; Ribonucleic acid; RNA; RNA, Viral - genetics; RNA-Dependent RNA Polymerase - metabolism; Science; Triticum - enzymology; Triticum - genetics; Triticum - virology; Viral infections; Virus Replication
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep45590

Many host factors have been identified to be involved in viral infection. However, although furoviruses cause important diseases of cereals worldwide, no host factors have yet been identified that interact with furoviral genes or participate in the viral infection cycle. In this study, both TaHSP70 and NbHSP70 were up-regulated in Chinese wheat mosaic furovirus (CWMV)-infected plants. Their overexpression and inhibition were correlated with the accumulation of viral genomic RNAs, suggesting that the HSP70 genes could be necessary for CWMV infection. The subcellular distributions of TaHSP70 and NbHSP70 were significantly affected by CWMV infection or by infiltration of RNA1 alone. Further assays showed that the viral replicase encoded by CWMV RNA1 interacts with both TaHSP70 and NbHSP70 in vivo and vitro and that its region aa167–333 was responsible for the interaction. Subcellular assays showed that the viral replicase could recruit both TaHSP70 and NbHSP70 from the cytoplasm or nucleus to the granular aggregations or inclusion-like structures on the intracellular membrane system, suggesting that both HSP70s may be recruited into the viral replication complex (VRC) to promote furoviral replication. This is the first host factor identified to be involved in furoviral infection, which extends the list and functional scope of HSP70 chaperones.