VPg of tobacco etch potyvirus is a host genotype-specific determinant for long-distance movement
Autor: | Andrew D. Lellis, Mary C. Schaad, James C. Carrington |
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Rok vydání: | 1997 |
Předmět: |
Genes
Viral Nicotiana tabacum Molecular Sequence Data Potyvirus Immunology RNA-binding protein Sequence alignment Microbiology Genome Viral Proteins Capsid Virology Endopeptidases Tobacco Coding region Amino Acid Sequence Peptide sequence Viral Structural Proteins Genetics Base Sequence biology Chimera Viral Core Proteins RNA-Binding Proteins biology.organism_classification Plants Toxic Insect Science Sequence Alignment Research Article |
Zdroj: | Journal of Virology. 71:8624-8631 |
ISSN: | 1098-5514 0022-538X |
DOI: | 10.1128/jvi.71.11.8624-8631.1997 |
Popis: | The V20 cultivar of Nicotiana tabacum was shown previously to exhibit a strain-specific restriction of long-distance movement of tobacco etch potyvirus (TEV). In V20, both TEV-HAT and TEV-Oxnard strains are capable of genome amplification and cell-to-cell movement, but only TEV-Oxnard is capable of systemic infection by vasculature-dependent long-distance movement. To investigate the basis for host-specific movement of TEV, chimeric virus genomes were assembled from TEV-HAT and TEV-Oxnard. Viruses containing the TEV-Oxnard coding regions for HC-Pro and/or capsid protein (CP), two proteins that are known to be essential for TEV long-distance movement, failed to infect V20 systemically. In contrast, chimeric viruses encoding the TEV-Oxnard VPg domain of NIa were able to infect V20 systemically. The critical region controlling the infection phenotype in V20 was mapped to a 67-nucleotide segment containing 10-nucleotide differences, but only five amino acid differences, between TEV-HAT and TEV-Oxnard. In V20 coinfection experiments, a restricted strain had no effect on systemic infection by a long-distance movement-competent chimeric strain, suggesting that the restricted strain was not inducing a generalized systemic resistance response. These data suggest that the VPg domain, which is covalently attached to the 5' end of genomic RNA, interacts either directly or indirectly with host components to facilitate long-distance movement. |
Databáze: | OpenAIRE |
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