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Characterization of cucumber mosaic virus. III. Localization of sequences in the movement protein controlling systemic infection in cucurbits
Year:
1997
Source of publication :
Virology
Authors :
Gal-On, Amit
;
.
Volume :
230
Co-Authors:
Kaplan, I.B., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States
Gal-On, A., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States, Department of Virology, Institute of Plant Protection, Volcani Center, Bet Dagan, 50250, Israel
Palukaitis, P., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States
Facilitators :
From page:
343
To page:
349
(
Total pages:
7
)
Abstract:
Cucumber mosaic virus (CMV), generated from biologically active cDNA clones of Fny-CMV RNA 1 plus 2 and Sny-CMV RNA 3, derived from the Fny-and Sny-strains of CMV, was able to infect tobacco but not squash plants systemically. In squash, viral RNA, movement protein, and coat protein all accumulated in the inoculated cotyledons. The lack of systemic infection was associated with a reduced rate of cell-to-cell movement within the cotyledons. The restricted movement mapped to two sequence changes in the codons of amino acids 51 and 240 of the Sny-CMV 3a gene. These same sequence changes previously were shown to be associated with high levels of 3a protein accumulation and chronic vs acute, cyclic infection typical of Sny-CMV vs Fny-CMV [Gal-On et al. (1996). Virology 226, 354-361]. Fny-CMV, mutated in the codons of 3a gene amino acids 51 and 240, was still able to infect several solanaceous hosts (tobacco, tomato, and pepper) systemically, but did not elicit a typical CMV systemic infection on any of several cucurbit hosts (cucumber, melon, or squash). The significance of the location of amino acid positions 51 and 240 in the 3a movement protein is discussed.
Note:
Related Files :
Cucumber mosaic virus
Cucumis sativus
Plant Viral Movement Proteins
vegetables
virus transmission
Show More
Related Content
More details
DOI :
10.1006/viro.1997.8468
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29711
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:49
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Scientific Publication
Characterization of cucumber mosaic virus. III. Localization of sequences in the movement protein controlling systemic infection in cucurbits
230
Kaplan, I.B., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States
Gal-On, A., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States, Department of Virology, Institute of Plant Protection, Volcani Center, Bet Dagan, 50250, Israel
Palukaitis, P., Department of Plant Pathology, Cornell University, Ithaca, NY 14853-4203, United States
Characterization of cucumber mosaic virus. III. Localization of sequences in the movement protein controlling systemic infection in cucurbits
Cucumber mosaic virus (CMV), generated from biologically active cDNA clones of Fny-CMV RNA 1 plus 2 and Sny-CMV RNA 3, derived from the Fny-and Sny-strains of CMV, was able to infect tobacco but not squash plants systemically. In squash, viral RNA, movement protein, and coat protein all accumulated in the inoculated cotyledons. The lack of systemic infection was associated with a reduced rate of cell-to-cell movement within the cotyledons. The restricted movement mapped to two sequence changes in the codons of amino acids 51 and 240 of the Sny-CMV 3a gene. These same sequence changes previously were shown to be associated with high levels of 3a protein accumulation and chronic vs acute, cyclic infection typical of Sny-CMV vs Fny-CMV [Gal-On et al. (1996). Virology 226, 354-361]. Fny-CMV, mutated in the codons of 3a gene amino acids 51 and 240, was still able to infect several solanaceous hosts (tobacco, tomato, and pepper) systemically, but did not elicit a typical CMV systemic infection on any of several cucurbit hosts (cucumber, melon, or squash). The significance of the location of amino acid positions 51 and 240 in the 3a movement protein is discussed.
Scientific Publication
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