The effect of breaking dormancy of potato tubers by Rindite or Gibberellic acid on the detection of potato virus A by ‘A6’-test leaves

1970 ◽  
Vol 13 (2) ◽  
pp. 101-113 ◽  
Author(s):  
J. A. De Bokx
Nature ◽  
1961 ◽  
Vol 190 (4775) ◽  
pp. 547-548 ◽  
Author(s):  
P. B. MATHUR

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.


2014 ◽  
Vol 11 (1) ◽  
pp. 71-80 ◽  
Author(s):  
MA Ali ◽  
KM Nasiruddin ◽  
MS Haque ◽  
SM Faisal

Virus elimination in potato through meristem culture followed by thermotherapy and virus indexing was studied. Three levels of thermotherapy, viz. 27±1°C (control), 30±1°C and 35±1°C, sixteen combinations of BAP (Benzyl Amino Purine) plus GA3 (gibberellic Acid) concentrations viz. 0.0+0.0 (control), 0.0+0.2, 0.0+0.4, 0.0+0.6, 1.5+0.0, 1.5+0.2, 1.5+0.4, 1.5+0.6, 3.0+0.0, 3.0+0.2, 3.0+0.4, 3.0+0.6 , 4.5+0.0, 4.5+ 0.2, 4.5+0.4 and 4.5+0.6 were used in this study in three potato varieties viz. Diamant, Heera and Lalpakri. Among the thermo therapies, 27±1°C showed the highest (24.55) survival response followed by 30±1°C, 35±1°C, respectively. The poorest (20.47) survival response of meristem derived plantlets was noticed in 35±1°C which gave the highest percentage (43.79) of virus free plantlets followed by 30±1°C. The best (25.85%) survival response was found in Lalpakri and the lowest (19.08%) survivality was recorded in Diamant. The highest (33.27) percentage of PVY (Potato Virus Y) free plantlets was observed in Heera. The combined treatment 3.0 mg L-1 BAP and 0.2 mg L-1 GA3 showed the highest (63.39) percentage of virus free plantlet production followed by 4.5 mg L-1 BAP and 0.2 mg L-1 GA3DOI: http://dx.doi.org/10.3329/sja.v11i1.18376 SAARC J. Agri., 11(1): 71-80 (2013)


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

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.


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