scholarly journals Formation of Potato Virus A-Induced RNA Granules and Viral Translation Are Interrelated Processes Required for Optimal Virus Accumulation

2015 ◽  
Vol 11 (12) ◽  
pp. e1005314 ◽  
Author(s):  
Anders Hafrén ◽  
Andres Lõhmus ◽  
Kristiina Mäkinen
1979 ◽  
Vol 56 (8) ◽  
pp. 367-371 ◽  
Author(s):  
R. P. Singh ◽  
M. E. Drew ◽  
E. M. Smith ◽  
R. H. Bagnall
Keyword(s):  

2017 ◽  
Vol 36 (7) ◽  
pp. 1728-1738 ◽  
Author(s):  
Alexander L. Ksenofontov ◽  
Eugeny N. Dobrov ◽  
Natalia V. Fedorova ◽  
Marina V. Serebryakova ◽  
Andrei N. Prusov ◽  
...  

2004 ◽  
Vol 17 (3) ◽  
pp. 322-329 ◽  
Author(s):  
Benoît Moury ◽  
Caroline Morel ◽  
Elisabeth Johansen ◽  
Laurent Guilbaud ◽  
Sylvie Souche ◽  
...  

The recessive resistance genes pot-1 and pvr2 in Lycopersicon hirsutum and Capsicum annuum, respectively, control Potato virus Y (PVY) accumulation in the inoculated leaves. Infectious cDNA molecules from two PVY isolates differing in their virulence toward these resistances were obtained using two different strategies. Chimeras constructed with these cDNA clones showed that a single nucleotide change corresponding to an amino acid substitution (Arg119His) in the central part of the viral protein genome-linked (VPg) was involved in virulence toward the pot-1 resistance. On the other hand, 15 nucleotide changes corresponding to five putative amino acid differences in the same region of the VPg affected virulence toward the pvr21 and pvr22 resistances. Substitution models identified six and five codons within the central and C terminal parts of the VPg for PVY and for the related potyvirus Potato virus A, respectively, which undergo positive selection. This suggests that the role of the VPg-encoding region is determined by the protein and not by the viral RNA apart from its protein-encoding capacity.


1990 ◽  
Vol 128 (2) ◽  
pp. 112-124 ◽  
Author(s):  
P. M. Boonekamp ◽  
H. Pomp ◽  
G. C. Gussenhoven

2020 ◽  
Vol 276 ◽  
pp. 197823
Author(s):  
Gabriel Robles-Luna ◽  
Nicolás Furman ◽  
María Florencia Barbarich ◽  
Nicolás Carlotto ◽  
Alejandra Attorresi ◽  
...  

2008 ◽  
Vol 89 (6) ◽  
pp. 1509-1518 ◽  
Author(s):  
Anders Hafrén ◽  
Kristiina Mäkinen

In order to be able to analyse post-translational modifications and protein interactions of viral genome-linked protein VPg taking place during potato virus A (PVA) infection, an affinity tag-based purification system was developed by inserting a sequence encoding a six-histidine and haemagglutinin (HisHA) tag to the 3′ end of the VPg coding sequence within the infectious cDNA clone of PVA. The engineered virus was fully functional and the HisHA tag-encoding sequence remained stable in the PVA genome throughout the infection process. Purification under denaturing conditions resulted in a protein sample that contained multiple VPg and NIa forms carrying post-translational modifications that altered their isoelectric points. Non-modified tagged VPg (pI 8) was a minor product in the protein sample derived from total leaf proteins, but when the replication-associated membranes were used as starting material, its relative amount increased. Further characterization demonstrated that some of the PVA VPg isoforms were modified by multiple phosphorylation events. Purity of the proteins derived from the native purifications with either of the tags was evaluated. A clearly purer VPg sample was obtained by performing tandem affinity purification utilizing both tags sequentially. NIb, CI and HC-Pro co-purified in an affinity-tagged VPg-dependent manner, indicating that the system was able to isolate protein complexes operating during PVA infection.


Sign in / Sign up

Export Citation Format

Share Document