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Volume 74,
Issue 5,
1993
Volume 74, Issue 5, 1993
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Inhibition of in vitro Cotranslational Disassembly of Tobacco Mosaic Virus by Monoclonal Antibodies to the Viral Coat Protein
More LessIt has been shown by others that translation of tobacco mosaic virus (TMV) RNA may begin before uncoating of particles is complete. We provide evidence that this cotranslational disassembly can be inhibited by incubating TMV treated at pH 8 with certain monoclonal antibodies (MAbs) specific for TMV coat protein. The most efficient inhibition was achieved by incubation with some anti-metatope MAbs known to bind to the TMV extremity that becomes disassembled first and contains the 5′ end of the RNA, as well as with some anti-cryptotope MAbs that bind only to dissociated coat protein subunits.
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Wild-Type Coat Protein Gene of Tobacco Mosaic Virus Mutant Ni 2519
More LessTobacco mosaic virus mutant Ni 2519 has a selected temperature-sensitive defect in the spreading of local lesions, and additional reported defects in virus assembly and in host range. Here we show that the temperature-sensitive local lesion-spreading defect (which maps in the assembly origin within the gene encoding protein p30) is probably independent of mutations in the pseudoassembly origin or of host range defects resulting from other mutations in the coat protein. One new host range mutant has been isolated.
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The 5′ end Generated in the in vitro Self-Cleavage Reaction of Avocado Sunblotch Viroid RNAs is Present in Naturally Occurring Linear Viroid Molecules
More LessThe 5′ termini of linear forms of avocado sunblotch viroid (ASBVd) isolated from infected tissue have been determined by primer extension analyses. According to the different termini identified, four main populations of linear viroid molecules were found. One of them had the same 5′ end as the one produced in the in vitro self-cleavage reaction of ASBVd dimeric transcripts mediated by a hammerhead structure, suggesting a possible involvement of this in vitro reaction in the in vivo replication mechanism of ASBVd.
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