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Viral Genome-Linked Protein (VPg) Controls Accumulation and Phloem-Loading of a Potyvirus in Inoculated Potato Leaves

February 2002 , Volume 15 , Number  2
Pages  138 - 149

Minna-Liisa Rajamäki and Jari P. T. Valkonen

Department of Plant Biology, Genetics Centre, SLU, P.O. Box 7080, S-750 07 Uppsala, Sweden; and Institute of Biotechnology, University of Helsinki, Finland

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Accepted 8 October 2001.

The viral protein covalently linked to the 5′ end of the plus-sense, single-stranded RNA genome of potyviruses (genus Potyvirus) can be an avirulence determinant in incompatible potyvirus-host combinations in which the resistance prevents systemic virus infection. The mechanism is not well known. This study shows that virus strain-specific resistance to systemic infection with Potato virus A (PVA) in Solanum commersonii is overcome by a single amino acid (aa) substitution, His118Tyr, in the viral genome-linked protein (VPg). Virus localization and other experiments revealed that Tyr118 controls phloem loading of PVA. The critical boundary may be constituted in phloem parenchyma, companion cells, or both. Tyr118 also controls the cellular level of virus accumulation in infected leaves, including phloem cells. Amino acid substitutions at three additional positions of the central part (aa 116) and C terminus (aa 185) of the VPg and of the N terminus of the 6K2 protein (aa 5) affect virus accumulation and rate of systemic infection but are not sufficient for phloem loading of PVA. These data, together with previous studies, indicate that the PVA VPg aa residues crucial for systemic infection are host specific. Also, our data and previous studies on other potyvirus-host species combinations indicate that the central part of the VPg is a domain with universal importance to virus-host interactions required for systemic invasion of plants with potyviruses.

© 2002 The American Phytopathological Society