2017
DOI: 10.1038/srep45590
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A furoviral replicase recruits host HSP70 to membranes for viral RNA replication

Abstract: 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 gene… Show more

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Cited by 15 publications
(22 citation statements)
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“…They can regulate viral life cycles both positively and negatively, and depending on the virus, they affect VRC formation, virus movement and coat protein homeostasis, among other processes. Three recent studies showed that unrelated plant viruses hijack HSP70 to greatly enhance virus replication [44-46].…”
Section: Resultsmentioning
confidence: 99%
“…They can regulate viral life cycles both positively and negatively, and depending on the virus, they affect VRC formation, virus movement and coat protein homeostasis, among other processes. Three recent studies showed that unrelated plant viruses hijack HSP70 to greatly enhance virus replication [44-46].…”
Section: Resultsmentioning
confidence: 99%
“…Northern blotting was performed as previously described (Yang et al, 2017). In brief, 3 lg total RNA from a sample was loaded into a well of a 1.5% formaldehyde containing agarose gel and separated through electrophoresis.…”
Section: Northern Blot Analysismentioning
confidence: 99%
“…The YTH assay was conducted using the Matchmaker Gold Yeast Two-Hybrid System and the Yeastmaker Yeast Transformation System 2 (Clontech, Mountain View, CA, USA) as previously described (Yang et al, 2017).…”
Section: Yeast Two-hybrid (Yth) Assaymentioning
confidence: 99%
“…Both in vivo and in vitro the viral replicase interacts with heat shock protein 70 (HSP70), a highly conserved molecular chaperone in plants, and the region of amino acid 167-333 is responsible for the interaction. Subcellular assays showed that the viral replicase could recruit HSP70 from the cytoplasm or nucleus to the granular inclusion-like structures on the intracellular membrane system, suggesting that the replicase could recruit HSP70s into the viral replication complex (VRC) to promote viral replication (Yang et al 2017).…”
Section: Rna1mentioning
confidence: 99%