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Volume 68,
Issue 10,
1987
Volume 68, Issue 10, 1987
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The Complete Nucleotide Sequence of Tobacco Rattle Virus RNA-1
More LessSUMMARYThe complete nucleotide sequence of tobacco rattle virus (TRV) strain SYM RNA-1 was determined from a series of overlapping cDNA clones. cDNA prepared by primer extension was used to determine the exact 5′ terminus. The RNA sequence was 6791 nucleotides in length and contained four open reading frames (ORFs). The ORF nearest the 5′ terminus coded for a polypeptide of predicted mol. wt. 134000 (134K) and terminated at an opal (UGA) stop codon. Readthrough of this stop codon would result in the production of a protein of 194K. The gene for a 29K polypeptide started one base beyond the 194K stop codon and, in turn, was followed by the gene for a 16K protein at the 3′ end of RNA-1. Amino acid comparisons of the 194K protein with the putative replicase of tobacco mosaic virus showed three regions of strong homology, suggesting that the 134K and 194K proteins were similarly involved in virus replication. The 5′ terminal sequences of both genome RNA species of TRV strains ORY, N5 and PRN together with that of-SYM RNA-2 were also determined. Alignments of these sequences showed that there was a 22 base repeated sequence close to the 5′ terminus in all these RNA species. It was also shown that the 5′ terminus of RNA-1 was homologous with the same region in RNA-2.
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Expression of the Middle Component RNA of Cowpea Mosaic Virus in vivo
More LessSUMMARYUpon infection of cowpea mesophyll protoplasts with cowpea mosaic virus (CPM V), the only M RNA-encoded proteins detected so far have been the two capsid proteins VP37 and VP23. We now report the detection of a M r 60000 (60K) precursor to both capsid proteins in infected protoplasts cultured in the presence of zinc ions. Furthermore a M RNA-encoded 48K protein was detected in the membrane fraction of infected cells using antisera raised against synthetic peptides. The results obtained indicate that, just like the bottom component RNA, the M RNA of CPMV is translated in vivo into a polyprotein from which proteins are derived by proteolytic cleavage.
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Identification of Viral Structural Proteins in the Nucleoplasm of Potato Yellow Dwarf Virus-infected Cells
More LessSUMMARYAntiserum raised against purified potato yellow dwarf virus (PYDV) reacted specifically with all five viral structural proteins in immunoblots and also with ultrathin sections of infected tobacco cells. In these sections viral proteins were detected with gold-labelled anti-IgG antibodies and gold particles were predominantly located over the nucleoplasm and over PYDV virus particles either at the periphery of nuclei or in the cytoplasm. Control sections of uninfected or healthy cells were not labelled. The results suggest that the nucleoplasm is the only site of accumulation of PYDV structural proteins.
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ICTV Virus Taxonomy Profile: Rhabdoviridae 2022
Peter J. Walker, Juliana Freitas-Astúa, Nicolas Bejerman, Kim R. Blasdell, Rachel Breyta, Ralf G. Dietzgen, Anthony R. Fooks, Hideki Kondo, Gael Kurath, Ivan V. Kuzmin, Pedro Luis Ramos-González, Mang Shi, David M. Stone, Robert B. Tesh, Noël Tordo, Nikos Vasilakis, Anna E. Whitfield and ICTV Report Consortium
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