A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69B

Miaoying Tian, Edgar Huitema, Luis da Cunha, Trudy Torto-Alalibo, Sophien Kamoun

    Research output: Contribution to journalArticle

    209 Citations (Scopus)

    Abstract

    The oomycetes form one of several lineages within the eukaryotes that independently evolved a parasitic lifestyle and consequently are thought to have developed alternative mechanisms of pathogenicity. The oomycete Phytophthora infestans causes late blight, a ravaging disease of potato and tomato. Little is known about processes associated with P. infestans pathogenesis, particularly the suppression of host defense responses. We describe and functionally characterize an extracellular protease inhibitor, EPI1, from P. infestans. EPI1 contains two domains with significant similarity to the Kazal family of serine protease inhibitors. Database searches suggested that Kazal-like proteins are mainly restricted to animals and apicomplexan parasites but appear to be widespread and diverse in the oomycetes. Recombinant EPI1 specifically inhibited subtilisin A among major serine proteases and inhibited and interacted with the pathogenesis-related P69B subtilisin-like serine protease of tomato in intercellular fluids. The epi1 and P69B genes were coordinately expressed and up-regulated during infection of tomato by P. infestans. Inhibition of tomato proteases by EPI1 could form a novel type of defense-counterdefense mechanism between plants and microbial pathogens. In addition, this study points to a common virulence strategy between the oomycete plant pathogen P. infestans and several mammalian parasites, such as the apicomplexan Toxoplasma gondii.

    Original languageEnglish
    Pages (from-to)26370-26377
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume279
    Issue number25
    Publication statusPublished - 18 Jun 2004

    Cite this

    Tian, Miaoying ; Huitema, Edgar ; da Cunha, Luis ; Torto-Alalibo, Trudy ; Kamoun, Sophien. / A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69B. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 25. pp. 26370-26377.
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    abstract = "The oomycetes form one of several lineages within the eukaryotes that independently evolved a parasitic lifestyle and consequently are thought to have developed alternative mechanisms of pathogenicity. The oomycete Phytophthora infestans causes late blight, a ravaging disease of potato and tomato. Little is known about processes associated with P. infestans pathogenesis, particularly the suppression of host defense responses. We describe and functionally characterize an extracellular protease inhibitor, EPI1, from P. infestans. EPI1 contains two domains with significant similarity to the Kazal family of serine protease inhibitors. Database searches suggested that Kazal-like proteins are mainly restricted to animals and apicomplexan parasites but appear to be widespread and diverse in the oomycetes. Recombinant EPI1 specifically inhibited subtilisin A among major serine proteases and inhibited and interacted with the pathogenesis-related P69B subtilisin-like serine protease of tomato in intercellular fluids. The epi1 and P69B genes were coordinately expressed and up-regulated during infection of tomato by P. infestans. Inhibition of tomato proteases by EPI1 could form a novel type of defense-counterdefense mechanism between plants and microbial pathogens. In addition, this study points to a common virulence strategy between the oomycete plant pathogen P. infestans and several mammalian parasites, such as the apicomplexan Toxoplasma gondii.",
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    A Kazal-like extracellular serine protease inhibitor from Phytophthora infestans targets the tomato pathogenesis-related protease P69B. / Tian, Miaoying; Huitema, Edgar; da Cunha, Luis; Torto-Alalibo, Trudy; Kamoun, Sophien.

    In: Journal of Biological Chemistry, Vol. 279, No. 25, 18.06.2004, p. 26370-26377.

    Research output: Contribution to journalArticle

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    AU - Tian, Miaoying

    AU - Huitema, Edgar

    AU - da Cunha, Luis

    AU - Torto-Alalibo, Trudy

    AU - Kamoun, Sophien

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