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Functional analysis of cysteine residues of ECP elicitor proteins of the fungal tomato pathogen Cladosporium fulvum

Authors

  • Rianne Luderer,

    1. Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands
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  • Maarten J. D. De Kock,

    1. Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands
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  • Robert H. L. Dees,

    1. Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands
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    • Present address: Laboratory of Molecular Recognition and Antibody Technology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands.

  • Pierre J. G. M. De Wit,

    1. Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands
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  • Matthieu H. A. J. Joosten

    Corresponding author
    1. Laboratory of Phytopathology, Wageningen University, Binnenhaven 5, 6709 PD Wageningen, the Netherlands
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* Correspondence: E-mail: Matthieu.Joosten@fyto.dpw.wag-ur.nl

summary

A striking feature of all elicitor proteins of Cladosporium fulvum that are specifically recognized by tomato is that they contain an even number of cysteine residues. These cysteine residues are thought to be involved in disulphide bridges. In this study, a mutational analysis of the cysteine residues of ECP1, ECP2 and ECP5 was performed, to examine their role in stability and hypersensitive response-inducing activity of the proteins. We show that not all cysteine residues of the ECPs are critical for the hypersensitive response-inducing activity of the proteins, and we propose that the role of cysteine residues in the ECPs is more complex than anticipated.

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