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

被引:16
|
作者
Yang, Jian [1 ]
Zhang, Fen [1 ,2 ]
Cai, Nian-Jun [1 ,2 ]
Wu, Ne [1 ,3 ]
Chen, Xuan [1 ,3 ]
Li, Jing [1 ]
Meng, Xiang-Feng [4 ]
Zhu, Tong-Quan [4 ]
Chen, Jian-Ping [1 ]
Zhang, Heng-Mu [1 ,2 ]
机构
[1] Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, MOA & Zhejiang Key Lab Plant Protect & Biotechnol, State Key Lab Breeding Base Zhejiang Sustain Pest, Hangzhou 310021, Zhejiang, Peoples R China
[2] Zhejiang Normal Univ, Coll Chem & Life Sci, Jinhua 321004, Peoples R China
[3] Zhejiang Agr & Forest Univ, Linan 311300, Peoples R China
[4] Zhumadian Acad Agr Sci, Zhumadian 463000, Peoples R China
来源
SCIENTIFIC REPORTS | 2017年 / 7卷
关键词
WHEAT-MOSAIC-VIRUS; MOLECULAR CHAPERONE; NICOTIANA-BENTHAMIANA; TRITICUM-AESTIVUM; PROTEIN; HEAT; HEAT-SHOCK-PROTEIN-70; EXPRESSION; INFECTION; GENE;
D O I
10.1038/srep45590
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页数:15
相关论文
共 50 条
  • [1] A furoviral replicase recruits host HSP70 to membranes for viral RNA replication
    Jian Yang
    Fen Zhang
    Nian-Jun Cai
    Ne Wu
    Xuan Chen
    Jing Li
    Xiang-Feng Meng
    Tong-Quan Zhu
    Jian-Ping Chen
    Heng-Mu Zhang
    Scientific Reports, 7
  • [2] Proteomics analysis of the tombusvirus replicase: Hsp70 molecular chaperone is associated with the replicase and enhances viral RNA replication
    Serva, S
    Nagy, PD
    JOURNAL OF VIROLOGY, 2006, 80 (05) : 2162 - 2169
  • [3] Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes
    Lopez, Victor
    Cauvi, David M.
    Arispe, Nelson
    De Maio, Antonio
    CELL STRESS & CHAPERONES, 2016, 21 (04): : 609 - 616
  • [4] Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes
    Victor Lopez
    David M. Cauvi
    Nelson Arispe
    Antonio De Maio
    Cell Stress and Chaperones, 2016, 21 : 609 - 616
  • [5] HSP70 inhibitor blocks virus replication
    Sarah Crunkhorn
    Nature Reviews Drug Discovery, 2016, 15 (1) : 18 - 18
  • [6] Differential Roles of Hsp70 and Hsp90 in the Assembly of the Replicase Complex of a Positive-Strand RNA Plant Virus
    Mine, Akira
    Hyodo, Kiwamu
    Tajima, Yuri
    Kusumanegara, Kusumawaty
    Taniguchi, Takako
    Kaido, Masanori
    Mise, Kazuyuki
    Taniguchi, Hisaaki
    Okuno, Tetsuro
    JOURNAL OF VIROLOGY, 2012, 86 (22) : 12091 - 12104
  • [7] Dengue Virus Infection Activates Cellular Chaperone Hsp70 in THP-1 Cells: Downregulation of Hsp70 by siRNA Revealed Decreased Viral Replication
    Padwad, Y. S.
    Mishra, K. P.
    Jain, Monika
    Chanda, S.
    Ganju, L.
    VIRAL IMMUNOLOGY, 2010, 23 (06) : 557 - 565
  • [8] Progranulin Recruits HSP70 to β-Glucocerebrosidase and Is Therapeutic Against Gaucher Disease
    Jian, Jinlong
    Tian, Qing-Yun
    Hettinghouse, Aubryanna
    Zhao, Shuai
    Liu, Helen
    Wei, Jianlu
    Grunig, Gabriele
    Zhang, Wujuan
    Setchell, Kenneth D. R.
    Sun, Ying
    Overkleeft, Herman S.
    Chan, Gerald L.
    Liu, Chuan-Ju
    EBIOMEDICINE, 2016, 13 : 212 - 224
  • [9] Oligomerization of Hsp70 upon insertion into lipid membranes
    Armijo, Gabrielle
    Cauvi, David
    Okerblom, Jonathan
    Lopez, Victor
    Gonzales, Derek
    Arispe, Nelson
    De Maio, Antonio
    FASEB JOURNAL, 2014, 28 (01):
  • [10] Heat shock protein 70 (Hsp70) mediates Zika virus entry, replication, and egress from host cells
    Pujhari, Sujit
    Brustolin, Marco
    Macias, Vanessa M.
    Nissly, Ruth H.
    Nomura, Masashi
    Kuchipudi, Suresh V.
    Rasgon, Jason L.
    EMERGING MICROBES & INFECTIONS, 2019, 8 (01): : 8 - 16