scholarly journals Mutations in the Region Encoding the Central Domain of Helper Component-Proteinase (HC-Pro) Eliminate Potato Virus X/Potyviral Synergism

Virology ◽  
1997 ◽  
Vol 231 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Xing Ming Shi ◽  
Heather Miller ◽  
Jeanmarie Verchot ◽  
James C. Carrington ◽  
Vicki Bowman Vance
2000 ◽  
Vol 90 (9) ◽  
pp. 944-950 ◽  
Author(s):  
S. Sonoda ◽  
H. Koiwa ◽  
K. Kanda ◽  
H. Kato ◽  
M. Shimono ◽  
...  

When Ipomoea nil was coinfected with Sweet potato feathery mottle virus (SPFMV), a member of the genus Potyvirus, and Potato virus X (PVX) typical symptoms caused by PVX were observed on those by SPFMV on the first upper true leaves at 14 days postinoculation (dpi). On the other hand, no PVX-induced symptoms were observed on the first upper true leaves at 14 dpi when plants were infected with PVX alone. In the case of coinfection with PVX and SPFMV, PVX RNA was detected not only in the inoculated cotyledonary leaves but also in the first upper true leaves at 14 dpi. In the case of single infection with PVX, PVX RNA was detected in the inoculated cotyledonary leaves but not in the first upper true leaves at 14 dpi. The accumulation of SPFMV remained unchanged, regardless of whether the inoculum consisted of SPFMV alone or a mixture of SPFMV and PVX. Although recombinant PVX engineered to express the helper component-proteinase (HC-Pro) of SPFMV (PVX.HC) enhanced symptoms severity in Nicotiana benthamiana, PVX.HC induced the synergism characterized by an enhanced viral movement in Ipomoea nil. Immunofluorescence microscopic examination revealed that the HC-Pro was present in phloem of SPFMV-infected I. nil. These results suggest that SPFMV HC-Pro acts as an enhancer of long distance movement for PVX in I. nil.


2021 ◽  
Author(s):  
Jun Jiang ◽  
Eric Yu ◽  
Clare L L Casteel

To establish successful infections, plant viruses compete with the host plants for limited resources and thus alter the physiological state of the plants. After successful infection, insect vectors are required for the transmission of some plant viruses to the next host plant. One of the largest groups of plant viruses, the potyvirus, can be transmitted by aphids. During transmission, the potyvirus protein helper component proteinase (HC-Pro) binds to the yet-to-be-defined aphid receptor on the stylet, as well as to the virus particles through the Asp-Ala-Gly (DAG) motif of the viral coat protein. Previously it was determined that a naturally occurring DAG motif in the non-aphid transmissible potexvirus, Potato aucuba mosaic potexvirus (PAMV), is functional when the HC-Pro is provided through co-infection with a potyvirus. Further, the DAG motif of PAMV can be successfully transferred to another non-aphid transmissible potexvirus, Potato virus X (PVX), to convey aphid transmission capabilities. We expand on this previous work by demonstrating, the DAG motif from two different potyviruses, Sugarcane mosaic virus and Turnip mosaic virus, as well as the DAG motif from the previous potexvirus PAMV, can be added to another non-aphid transmissible potexvirus, Foxtail mosaic virus (FoMV), to make it aphid transmissible. Transmission efficiency varied from less than 10% to over 80% depending on the DAG motif and host plant used in transmission, suggesting not all DAG motifs are equal for engineering aphid transmission. The underlying mechanisms mediating this variation still need to be explored.


2011 ◽  
Vol 24 (7) ◽  
pp. 787-797 ◽  
Author(s):  
Benoît Moury ◽  
Bernard Caromel ◽  
Elisabeth Johansen ◽  
Vincent Simon ◽  
Laura Chauvin ◽  
...  

The Nctbr and Nytbr genes in Solanum tuberosum determine hypersensitive reactions, characterized by necrotic reactions and restriction of the virus systemic movement, toward isolates belonging to clade C and clade O of Potato virus Y (PVY), respectively. We describe a new resistance from S. sparsipilum which possesses the same phenotype and specificity as Nctbr and is controlled by a dominant gene designated Ncspl. Ncspl maps on potato chromosome IV close or allelic to Nytbr. The helper component proteinase (HC-Pro) cistron of PVY was shown to control necrotic reactions and resistance elicitation in plants carrying Ncspl, Nctbr, and Nytbr. However, inductions of necrosis and of resistance to the systemic virus movement in plants carrying Ncspl reside in different regions of the HC-Pro cistron. Also, genomic determinants outside the HC-Pro cistron are involved in the systemic movement of PVY after induction of necroses on inoculated leaves of plants carrying Nytbr. These results suggest that the Nytbr resistance may have been involved in the recent emergence of PVY isolates with a recombination breakpoint near the junction of HC-Pro and P3 cistrons in potato crops. Therefore, this emergence could constitute one of the rare examples of resistance breakdown by a virus which was caused by recombination instead of by successive accumulation of nucleotide substitutions.


2013 ◽  
Vol 26 (7) ◽  
pp. 734-744 ◽  
Author(s):  
Tuuli Haikonen ◽  
Minna-Liisa Rajamäki ◽  
Jari P. T. Valkonen

Microtubules (MT) outline and maintain the overall shape of cells and can reorganize cellular membranes to serve as sites of RNA virus replication. Here, we provide data on involvement of an MT-associated protein in infection of plants with a potyvirus, Potato virus A (PVA), representing the largest family of plant-infecting RNA viruses. Our results showed that helper-component proteinase (HCpro)-interacting protein 2 (HIP2) of potato (Solanum tuberosum) is an MT-associated protein similar to Arabidopsis SPR2. Virus-induced silencing of HIP2 in Nicotiana benthamiana resulted in a spiral-like growth phenotype, similar to the Arabidopsis spr2 mutant, and the spr2 phenotype in Arabidopsis was complemented with potato HIP2. HCpro of PVA interacted with HIP2 of potato and tobacco (Nicotiana tabacum). The interaction was detected by bimolecular fluorescence complementation in PVA-infected leaves on MT and MT intersections at the cell cortex. HIP2-HCpro interaction was determined by the C-proximal α-helix-rich domain of HIP2, whereas the N-proximal putative TOG domain and the central coiled-coil domain of HIP2 controlled HIP2 dimerization and binding to MT. Accumulation of PVA was significantly reduced in the HIP2-silenced leaves of N. benthamiana, which indicates that HIP2-HCpro interactions are important for virus infection.


1999 ◽  
Vol 20 (3) ◽  
pp. 357-362 ◽  
Author(s):  
Susan M. Angell ◽  
David C. Baulcombe

Acta Naturae ◽  
2011 ◽  
Vol 3 (3) ◽  
pp. 40-46 ◽  
Author(s):  
M V Arkhipenko ◽  
E K Petrova ◽  
N A Nikitin ◽  
A D Protopopova ◽  
E V Dubrovin ◽  
...  

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