Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/50386
DC FieldValueLanguage
dc.contributor.authorLee, C.C.en_US
dc.contributor.author徐堯煇zh_TW
dc.contributor.authorHo, Y.N.en_US
dc.contributor.authorHu, R.H.en_US
dc.contributor.authorYen, Y.T.en_US
dc.contributor.authorWang, Z.C.en_US
dc.contributor.authorLee, Y.C.en_US
dc.contributor.authorHsu, Y.H.en_US
dc.contributor.authorMeng, M.H.en_US
dc.contributor.author孟孟孝zh_TW
dc.date2011zh_TW
dc.date.accessioned2014-06-06T08:49:25Z-
dc.date.available2014-06-06T08:49:25Z-
dc.identifier.issn0022-538Xzh_TW
dc.identifier.urihttp://hdl.handle.net/11455/50386-
dc.description.abstractBamboo mosaic virus (BaMV) is a positive-sense RNA virus belonging to the genus Potexvirus. Open reading frame 1 (ORF1) encodes the viral replication protein that consists of a capping enzyme domain, a helicase-like domain (HLD), and an RNA-dependent RNA polymerase domain from the N to C terminus. ORF5 encodes the viral coat protein (CP) required for genome encapsidation and the virus movement in plants. In this study, application of a yeast-two hybrid assay detected an interaction between the viral HLD and CP. However, the interaction did not affect the NTPase activity of the HLD. To identify the critical amino acids of CP interacting with the HLD, a random mutational library of CP was created using error-prone PCR, and the mutations adversely affecting the interaction were screened by a bacterial two-hybrid system. As a result, the mutations A209G and N210S in CP were found to weaken the interaction. To determine the significance of the interaction, the mutations were introduced into a BaMV infectious clone, and the mutational effects on viral replication, movement, and genome encapsidation were investigated. There was no effect on accumulations of BaMV CP and genomic RNAs within protoplasts; however, the virus cell-to-cell movement in plants was restricted. Sequence alignment revealed that A209 of BaMV CP is conserved in many potexviruses. Mutation of the corresponding residue in Foxtail mosaic virus CP also reduced the viral HLD-CP interaction and restricted the virus movement, suggesting that interaction between CP and a widely conserved HLD in the potexviral replication protein is crucial for viral trafficking through plasmodesmata.en_US
dc.language.isoen_USzh_TW
dc.relationJournal of Virologyen_US
dc.relation.ispartofseriesJournal of Virology, Volume 85, Issue 22, Page(s) 12022-12031.en_US
dc.relation.urihttp://dx.doi.org/10.1128/jvi.05595-11en_US
dc.subjectcell-to-cellen_US
dc.subjecttriple-gene-blocken_US
dc.subjectnicotiana-benthamianaen_US
dc.subjectendoplasmic-reticulumen_US
dc.subjectrnaen_US
dc.subjectpotexvirusen_US
dc.subjecttransporten_US
dc.subjectplasmodesmataen_US
dc.subjectassociationen_US
dc.subjectactivationen_US
dc.titleThe Interaction between Bamboo Mosaic Virus Replication Protein and Coat Protein Is Critical for Virus Movement in Plant Hostsen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1128/jvi.05595-11zh_TW
item.fulltextno fulltext-
item.languageiso639-1en_US-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
Appears in Collections:生物科技學研究所
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