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Correlation between Binding Affinity and Necrosis-Inducing Activity of Mutant AVR9 Peptide Elicitors1

Miriam Kooman-Gersmann2, 3, Ralph Vogelsang2, 4, Paul Vossen, Henno W. van den Hooven, Eve Mahé, Guy Honée, and Pierre J.G.M. de Wit*

Department of Phytopathology, Wageningen Agricultural University, Binnenhaven 9, P.O. Box 8025, 6700 EE Wageningen, The Netherlands (M.K.-G., R.V., P.V., G.H., P.J.G.M.d.W.); Laboratory of Biochemistry, Wageningen Agricultural University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands (H.W.v.d.H.); and Institut National de la Santé et de la Recherche Médicale U 376, Arnaud de Villeneuve, 371 rue du Doyen G. Giraud, 34295 Montpellier, France (E.M.)

The race-specific peptide elicitor AVR9 of the fungus Cladosporium fulvum induces a hypersensitive response only in tomato (Lycopersicon esculentum) plants carrying the complementary resistance gene Cf-9 (MoneyMaker-Cf9). A binding site for AVR9 is present on the plasma membranes of both resistant and susceptible tomato genotypes. We used mutant AVR9 peptides to determine the relationship between elicitor activity of these peptides and their affinity to the binding site in the membranes of tomato. Mutant AVR9 peptides were purified from tobacco (Nicotiana clevelandii) inoculated with recombinant potato virus X expressing the corresponding avirulence gene Avr9. In addition, several AVR9 peptides were synthesized chemically. Physicochemical techniques revealed that the peptides were correctly folded. Most mutant AVR9 peptides purified from potato virus X::Avr9-infected tobacco contain a single N-acetylglucosamine. These glycosylated AVR9 peptides showed a lower affinity to the binding site than the nonglycosylated AVR9 peptides, whereas their necrosis-inducing activity was hardly changed. For both the nonglycosylated and the glycosylated mutant AVR9 peptides, a positive correlation between their affinity to the membrane-localized binding site and their necrosis-inducing activity in MoneyMaker-Cf9 tomato was found. The perception of AVR9 in resistant and susceptible plants is discussed.

1   This research was supported by the Netherlands Technology Foundation and coordinated by the Life Sciences Foundation through a grant provided to M.K.-G. and P.J.G.M.d.W. R.V. was supported by a European Molecular Biology Organization Long-Term Fellowship and a Human Capital and Mobility grant (no. CHRX-CT93-0170) supplied by the European Commission (EC), and H.W.v.d.H. was supported by a EC Biotech grant (no. BIO4 CT96 0515). E.M. acknowledges support from European Union-Training and Mobility of Researchers (grant no. CHGE-CT94-0061).
2   M.K.-G. and R.V. contributed equally to this publication.
3   Present address: Novartis, S & G Seeds, Westeinde 62, P.O. Box 16, 1600 AA Enkhuizen, The Netherlands.
4   Present address: Promega GmbH, High-Tech-Park, Schildkrötstrasse 15, 68199 Mannheim, Germany.
*   Corresponding author; e-mail pierre.dewit{at}medew.fyto.wau.nl; fax 31-317-483412.

Plant Physiol. (1998) 117: 609-618
Copyright Clearance Center:   0032-0889/98/117/0609/10
© 1998 American Society of Plant Physiologists




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