December
1999
, Volume
12
, Number
12
Pages
1,074
-
1,081
Authors
Minna-Liisa
Rajamäki
and
Jari P. T.
Valkonen
Affiliations
Department of Plant Biology, Genetic Centre, SLU, PO Box 7080, S-750 07 Uppsala, Sweden; and Institute of Biotechnology, Viikki Biocenter, PO Box 56, FIN-00014 University of Helsinki, Finland
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Accepted 1 September 1999.
Abstract
Infection with the isolate PVA-M of potato virus A (PVA; genus Potyvirus) is restricted to the inoculated leaves of Nicandra physaloides (Solanaceae), whereas the isolate PVA-B11 infects plants systemically by 10 days post inoculation. Resistance to systemic infection was shown to develop during plant growth. A recombinant virus (B11-M) in which a 1,208-nucleotide sequence of the full-length cDNA clone of PVA-B11 was replaced with the corresponding sequence from PVA-M displayed a phenotype similar to that of PVA-M. The replaced sequence contained four amino acid differences between the two isolates: one in the 6K2 protein and three in the viral genome-linked protein (VPg). Site-directed mutagenesis of the cDNA clones and inoculation of the mutants to N. physaloides indicated that the amino acid substitutions of Met5Val in the 6K2 protein or Leu185Ser in the VPg permitted vascular movement and systemic infection. However, resistance was only partially overcome by these changes, since systemic infection proceeded at a slower rate than with PVA-B11. The amino acid substitution Val116Met in the VPg alone was sufficient to overcome resistance and recover the phenotype of the isolate PVA-B11. These data indicated that both the 6K2 protein and the VPg were avirulence determinants of PVA-M in N. physaloides and suggested a possibly coordinated function of them in the vascular movement of PVA.
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© 1999 The American Phytopathological Society