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- W2056514580 endingPage "e1002726" @default.
- W2056514580 startingPage "e1002726" @default.
- W2056514580 abstract "Host factors play crucial roles in the replication of plus-strand RNA viruses. In this report, a heat shock protein 90 homologue of Nicotiana benthamiana, NbHsp90, was identified in association with partially purified replicase complexes from BaMV-infected tissue, and shown to specifically interact with the 3' untranslated region (3' UTR) of BaMV genomic RNA, but not with the 3' UTR of BaMV-associated satellite RNA (satBaMV RNA) or that of genomic RNA of other viruses, such as Potato virus X (PVX) or Cucumber mosaic virus (CMV). Mutational analyses revealed that the interaction occurs between the middle domain of NbHsp90 and domain E of the BaMV 3' UTR. The knockdown or inhibition of NbHsp90 suppressed BaMV infectivity, but not that of satBaMV RNA, PVX, or CMV in N. benthamiana. Time-course analysis further revealed that the inhibitory effect of 17-AAG is significant only during the immediate early stages of BaMV replication. Moreover, yeast two-hybrid and GST pull-down assays demonstrated the existence of an interaction between NbHsp90 and the BaMV RNA-dependent RNA polymerase. These results reveal a novel role for NbHsp90 in the selective enhancement of BaMV replication, most likely through direct interaction with the 3' UTR of BaMV RNA during the initiation of BaMV RNA replication." @default.
- W2056514580 created "2016-06-24" @default.
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- W2056514580 date "2012-05-24" @default.
- W2056514580 modified "2023-10-15" @default.
- W2056514580 title "Hsp90 Interacts Specifically with Viral RNA and Differentially Regulates Replication Initiation of Bamboo mosaic virus and Associated Satellite RNA" @default.
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- W2056514580 doi "https://doi.org/10.1371/journal.ppat.1002726" @default.
- W2056514580 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3359997" @default.
- W2056514580 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22654666" @default.
- W2056514580 hasPublicationYear "2012" @default.
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