Coat protein interactions involved in tobacco mosaic tobamovirus cross-protection.
To investigate the molecular role of the tobacco mosaic tobamovirus (TMV) coat protein (CP) in conferring cross-protection, a potato X potexvirus (PVX) vector (S. Chapman, Plant J. 2, 549-557, 1992) was used to systemically express a set of TMV mutant CPs in Nicotiana benthamiana prior to challenge inoculation with TMV. PVX-expressed wild-type TMV CP delayed TMV accumulation for up to 2 weeks compared to unprotected plants or plants preinfected with the unmodified PVX vector. Similar delays in TMV accumulation were obtained using TMV CPs that were deficient in virion formation but competent to assemble into helical aggregates. In contrast, TMV CPs that were incapable of helical aggregation or unable to bind viral RNA did not delay the accumulation of TMV. Furthermore, TMV CPs with enhanced intersubunit interactions that favor helical aggregation produced significantly greater delays in the accumulation of challenge TMV than obtained from the wild-type CP. Thus the capabilities of TMV CP to interact with viral RNA and self-associate in a helical fashion appear to be essential to its ability to confer protection. Taken together, these findings support a model for CP-mediated resistance in which the protecting CP recoats the challenge virus RNA as it disassembles.
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Department of Plant Biology, University of Maryland, College Park, Maryland, 20742, USA.
Stubbs
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Culver
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D036022:Capsid Proteins; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010947:Plants, Toxic; D017863:Potexvirus / Q000502:physiology; D012367:RNA, Viral / Q000378:metabolism; D014026:Nicotiana / Q000821:virology; D014027:Tobacco Mosaic Virus / Q000472:pathogenicity / Q000502:physiology* / Q000648:ultrastructure; D014762:Viral Interference; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D019065:Virus Assembly
D036022:Capsid Proteins; C009496:H protein, Tobacco mosaic virus; D012367:RNA, Viral; D014764:Viral Proteins