کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6138535 | 1594219 | 2016 | 7 صفحه PDF | دانلود رایگان |
- The RNA2-ORF2-encoded polyproteins of ToMarV-M and ToChSV have a Q at the -1 position of the cleavage site.
- Multiple aa sequence comparison confirmed that this Q is conserved among other torradoviruses.
- Site-directed mutagenesis of the ToMarV-M RdRp or protease prevented accumulation of viral coat proteins and RNAs.
Torradoviruses, family Secoviridae, are emergent bipartite RNA plant viruses. RNA1 is ca. 7Â kb and has one open reading frame (ORF) encoding for the protease, helicase and RNA-dependent RNA polymerase (RdRp). RNA2 is ca. 5Â kb and has two ORFs. RNA2-ORF1 encodes for a putative protein with unknown function(s). RNA2-ORF2 encodes for a putative movement protein and three capsid proteins. Little is known about the replication and polyprotein processing strategies of torradoviruses. Here, the cleavage sites in the RNA2-ORF2-encoded polyproteins of two torradoviruses, Tomato marchitez virus isolate M (ToMarV-M) and tomato chocolate spot virus, were determined by N-terminal sequencing, revealing that the amino acid (aa) at the â1 position of the cleavage sites is a glutamine. Multiple aa sequence comparison confirmed that this glutamine is conserved among other torradoviruses. Finally, site-directed mutagenesis of conserved aas in the ToMarV-M RdRp and protease prevented substantial accumulation of viral coat proteins or RNAs.
Journal: Virology - Volume 498, November 2016, Pages 109-115