scholarly journals Chimeric Virus Made from crTMV RNA and the Coat Protein of Potato Leafroll Virus is Targeted to the Nucleolus and Can Infect Nicotiana benthamiana Mechanically

2020 ◽  
Vol 9 (2) ◽  
pp. 11
Author(s):  
Konstantin O. Butenko ◽  
Inna A. Chaban ◽  
Eugene V. Skurat ◽  
Olga A. Kondakova ◽  
Yuri F. Drygin
Keyword(s):  
Coat Protein ◽  
Nicotiana Benthamiana ◽  
Cellular Localization ◽  
Plant Pathogens ◽  
Rna Virus ◽  
Potato Leafroll Virus ◽  
Genetically Engineered ◽  
Chimeric Virus ◽  
Recombinant Viruses ◽  
Leafroll Virus

A genetically engineered chimeric virus crTMV-CP-PLRV composed of the crucifer-infecting tobacco mosaic virus (crTMV) RNA and the potato leafroll virus (PLRV) coat protein (CP) was obtained by agroinfiltration of Nicotiana benthamiana with the binary vector pCambia-crTMV-CPPLRV. The significant levels of the chimeric virus enabled direct visualization of crTMV-CP-PLRV in the cell and to investigate the mechanism of the pathogenesis. Localization of the crTMV-CP-PLRV in plant cells was examined by immunoblot techniques, as well as light, and transmission electron microscopy. The chimera can transfer between vascular and nonvascular tissues. The chimeric virus inoculum is capable to infect N. benthamiana mechanically. The distinguishing feature of the chimeric virus, the RNA virus with the positive genome, was found to localize in the nucleolus. We also investigated the role of the N-terminal sequence of the PLRV P3 coat protein in the cellular localization of the virus. We believe that the gene of the PLRV CP can be substituted with genes from other challenging-to-study plant pathogens to produce other useful recombinant viruses.

scholarly journals Nucleotide sequence of the potato leafroll virus coat protein gene

1989 ◽  
Vol 17 (4) ◽  
pp. 1768-1768 ◽  
Author(s):  
B. Prill ◽  
E. Maiss ◽  
U. Timpe ◽  
R. Casper
Keyword(s):  
Nucleotide Sequence ◽  
Coat Protein ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Potato Leafroll Virus ◽  
Virus Coat Protein ◽  
Virus Coat ◽  
Leafroll Virus

scholarly journals Host-Dependent Requirement for the Potato leafroll virus 17-kDa Protein in Virus Movement

2002 ◽  
Vol 15 (10) ◽  
pp. 1086-1094 ◽  
Author(s):  
Lawrence Lee ◽  
Peter Palukaitis ◽  
Stewart M. Gray
Keyword(s):  
Amino Acids ◽  
Solanum Tuberosum ◽  
Nicotiana Benthamiana ◽  
Systemic Infection ◽  
Potato Leafroll Virus ◽  
Virus Movement ◽  
Wild Type ◽  
Mature Leaves ◽  
Leafroll Virus ◽  
Virus Distribution

The requirement for the 17-kDa protein (P17) of Potato leafroll virus (PLRV) in virus movement was investigated in four plant species: potato (Solanum tuberosum), Physalis floridana, Nicotiana benthamiana, and N. clevelandii. Two PLRV P17 mutants were characterized, one that does not translate the P17 and another that expresses a P17 missing the first four amino acids. The P17 mutants were able to replicate and accumulate in agroinoculated leaves of potato and P. floridana, but they were unable to move into vascular tissues and initiate a systemic infection in these plants. In contrast, the P17 mutants were able to spread systemically from inoculated leaves in both Nicotiana spp., although the efficiency of infection was reduced relative to wild-type PLRV. Examination of virus distribution in N. benthamiana plants using tissue immunoblotting techniques revealed that the wild-type PLRV and P17 mutants followed a similar movement pathway out of the inoculated leaves. Virus first moved upward to the apical tissues and then downward. The P17 mutants, however, infected fewer phloem-associated cells, were slower than wild-type PLRV in moving out of the inoculated tissue and into apical tissues, and were unable to infect any mature leaves present on the plant at the time of inoculation.

Chimeric Virus as a Source of the Potato Leafroll Virus Antigen

2017 ◽  
Vol 59 (11-12) ◽  
pp. 469-481 ◽  
Author(s):  
Eugene V. Skurat ◽  
Konstantin O. Butenko ◽  
Olga A. Kondakova ◽  
Nikolai A. Nikitin ◽  
Olga V. Karpova ◽  
...  
Keyword(s):  
Potato Leafroll Virus ◽  
Virus Antigen ◽  
Chimeric Virus ◽  
Leafroll Virus

scholarly journals Nucleotide Sequences of Coat Protein and 17K Protein Genes for a Potato Leafroll Virus Japanese Isolate.

1993 ◽  
Vol 59 (2) ◽  
pp. 204-208 ◽  
Author(s):  
Kazusato OHSHIMA ◽  
Takaaki NAKAYA ◽  
Takeshi MATSUMURA ◽  
Eishiro SHIKATA ◽  
Ikuo KIMURA
Keyword(s):  
Coat Protein ◽  
Potato Leafroll Virus ◽  
Nucleotide Sequences ◽  
Japanese Isolate ◽  
Leafroll Virus

scholarly journals Suppression of Bamboo Mosaic Virus Accumulation by a Putative Methyltransferase in Nicotiana benthamiana

2009 ◽  
Vol 83 (11) ◽  
pp. 5796-5805 ◽  
Author(s):  
Chun-Wei Cheng ◽  
Yi-Yuong Hsiao ◽  
Hui-Chuan Wu ◽  
Chi-Mau Chuang ◽  
Jao-Shien Chen ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Nicotiana Benthamiana ◽  
Rna Virus ◽  
Infectious Clone ◽  
Inhibitory Effect ◽  
Amino Acid Residues ◽  
Virus Induced Gene Silencing ◽  
Innate Defense ◽  
Predicted Signal Peptide

ABSTRACT Bamboo mosaic virus (BaMV) is a 6.4-kb positive-sense RNA virus belonging to the genus Potexvirus of the family Flexiviridae. The 155-kDa viral replicase, the product of ORF1, comprises an N-terminal S-adenosyl-l-methionine (AdoMet)-dependent guanylyltransferase, a nucleoside triphosphatase/RNA 5′-triphosphatase, and a C-terminal RNA-dependent RNA polymerase (RdRp). To search for cellular factors potentially involved in the regulation of replication and/or transcription of BaMV, the viral RdRp domain was targeted as bait to screen against a leaf cDNA library of Nicotiana benthamiana using a yeast two-hybrid system. A putative methyltransferase (PNbMTS1) of 617 amino acid residues without an established physiological function was identified. Cotransfection of N. benthamiana protoplasts with a BaMV infectious clone and the PNbMTS1-expressing plasmid showed a PNbMTS1 dosage-dependent inhibitory effect on the accumulation of BaMV coat protein. Deletion of the N-terminal 36 amino acids, deletion of a predicted signal peptide or transmembrane segment, or mutations in the putative AdoMet-binding motifs of PNbMTS1 abolished the inhibitory effect. In contrast, suppression of PNbMTS1 by virus-induced gene silencing in N. benthamiana increased accumulation of the viral coat protein as well as the viral genomic RNA. Collectively, PNbMTS1 may function as an innate defense protein against the accumulation of BaMV through an uncharacterized mechanism.

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