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An Ry ‐mediated resistance response in potato requires the intact active site of the NIa proteinase from potato virus Y
Author(s) -
Mestre Pere,
Brigneti Gianinna,
Baulcombe David C.
Publication year - 2000
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2000.00834.x
Subject(s) - tobacco etch virus , potato virus y , elicitor , potyvirus , biology , hypersensitive response , virus , potato virus x , cleavage (geology) , virology , enzyme , biochemistry , plant virus , plant disease resistance , gene , paleontology , fracture (geology)
Summary Ry confers extreme resistance to all strains of potato virus Y (PVY). To identify the elicitor of the Ry ‐mediated resistance against PVY in potato, we expressed each of the PVY‐encoded proteins in leaves of PVY‐resistant ( Ry ) and ‐susceptible ( ry ) plants. For most of the proteins tested, there was no evident response. However, when the NIa proteinase was expressed in leaves of Ry plants, there was a hypersensitive response (HR). Proteinase active site mutants failed to induce the Ry ‐mediated response. The HR was also induced by the NIa proteinase from pepper mottle virus (PepMoV), which has the same cleavage specificity as the PVY enzyme, but not by the tobacco etch virus (TEV) or the potato virus A (PVA) proteinases that cleave different peptide motifs. Based on these results, we propose that Ry ‐mediated resistance requires the intact active site of the NIa proteinase. Although the structure of the active proteinase could have elicitor activity, it is possible that this proteinase releases an elicitor by cleavage of a host‐encoded protein. Alternatively, the proteinase could inactivate a negative regulator of the Ry ‐mediated resistance response.