Specific cysteine protease inhibitors act as deterrents of Western flower thrips Frankliniella occidentalis (Pergande) in transgenic potato

N.S. Outchkourov, J. de Kogel, A. de Bruin, M. Abrahamson, M.A. Jongsma

    Research output: Contribution to journalArticleAcademicpeer-review

    34 Citations (Scopus)

    Abstract

    In this study, the effects of the accumulation of cysteine protease inhibitors on the food preferences of adult female western flower thrips, Frankliniella occidentalis (Pergande), were investigated. Representative members of the cystatin and thyropin gene families (stefin A, cystatin C, kininogen domain 3 and equistatin) were expressed in potato (Solanum tuberosum) cv. Impala, Kondor and Line V plants. In choice assays, a strong time- and concentration-dependent deterrence from plants expressing stefin A and equistatin was observed. Cystatin C and kininogen domain 3 were not found to be active. All tested inhibitors were equally or more active than stefin A at inhibiting the proteolytic activity of thrips, but, in contrast with stefin A, they were all expressed in potato as partially degraded proteins. The resistance of cysteine protease inhibitors against degradation in planta by endogenous plant proteases may therefore be relevant in explaining the observed differences in the deterrence of thrips. The results demonstrate that, when given a choice, western flower thrips will select plants with low levels of certain cysteine protease inhibitors. The novel implications of the defensive role of plant cysteine protease inhibitors as both deterrents and antimetabolic proteins are discussed
    Original languageEnglish
    Pages (from-to)439-448
    JournalPlant Biotechnology Journal
    Volume2
    Issue number5
    DOIs
    Publication statusPublished - 2004

    Fingerprint

    Thysanoptera
    Cysteine Proteinase Inhibitors
    Cystatin A
    cysteine proteinase inhibitors
    cystatins
    Frankliniella occidentalis
    Solanum tuberosum
    genetically modified organisms
    potatoes
    Kininogens
    Cystatin C
    Cystatins
    Food Preferences
    Proteins
    Peptide Hydrolases
    Aepyceros melampus
    Plantae
    food choices
    Genes
    proteinases

    Keywords

    • pichia-pastoris
    • nicotiana-attenuata
    • escherichia-coli
    • oostatic factor
    • cystatin-c
    • expression
    • resistance
    • proteinases
    • equistatin
    • cloning

    Cite this

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    title = "Specific cysteine protease inhibitors act as deterrents of Western flower thrips Frankliniella occidentalis (Pergande) in transgenic potato",
    abstract = "In this study, the effects of the accumulation of cysteine protease inhibitors on the food preferences of adult female western flower thrips, Frankliniella occidentalis (Pergande), were investigated. Representative members of the cystatin and thyropin gene families (stefin A, cystatin C, kininogen domain 3 and equistatin) were expressed in potato (Solanum tuberosum) cv. Impala, Kondor and Line V plants. In choice assays, a strong time- and concentration-dependent deterrence from plants expressing stefin A and equistatin was observed. Cystatin C and kininogen domain 3 were not found to be active. All tested inhibitors were equally or more active than stefin A at inhibiting the proteolytic activity of thrips, but, in contrast with stefin A, they were all expressed in potato as partially degraded proteins. The resistance of cysteine protease inhibitors against degradation in planta by endogenous plant proteases may therefore be relevant in explaining the observed differences in the deterrence of thrips. The results demonstrate that, when given a choice, western flower thrips will select plants with low levels of certain cysteine protease inhibitors. The novel implications of the defensive role of plant cysteine protease inhibitors as both deterrents and antimetabolic proteins are discussed",
    keywords = "pichia-pastoris, nicotiana-attenuata, escherichia-coli, oostatic factor, cystatin-c, expression, resistance, proteinases, equistatin, cloning",
    author = "N.S. Outchkourov and {de Kogel}, J. and {de Bruin}, A. and M. Abrahamson and M.A. Jongsma",
    year = "2004",
    doi = "10.1111/j.1467-7652.2004.00088.x",
    language = "English",
    volume = "2",
    pages = "439--448",
    journal = "Plant Biotechnology Journal",
    issn = "1467-7644",
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    }

    Specific cysteine protease inhibitors act as deterrents of Western flower thrips Frankliniella occidentalis (Pergande) in transgenic potato. / Outchkourov, N.S.; de Kogel, J.; de Bruin, A.; Abrahamson, M.; Jongsma, M.A.

    In: Plant Biotechnology Journal, Vol. 2, No. 5, 2004, p. 439-448.

    Research output: Contribution to journalArticleAcademicpeer-review

    TY - JOUR

    T1 - Specific cysteine protease inhibitors act as deterrents of Western flower thrips Frankliniella occidentalis (Pergande) in transgenic potato

    AU - Outchkourov, N.S.

    AU - de Kogel, J.

    AU - de Bruin, A.

    AU - Abrahamson, M.

    AU - Jongsma, M.A.

    PY - 2004

    Y1 - 2004

    N2 - In this study, the effects of the accumulation of cysteine protease inhibitors on the food preferences of adult female western flower thrips, Frankliniella occidentalis (Pergande), were investigated. Representative members of the cystatin and thyropin gene families (stefin A, cystatin C, kininogen domain 3 and equistatin) were expressed in potato (Solanum tuberosum) cv. Impala, Kondor and Line V plants. In choice assays, a strong time- and concentration-dependent deterrence from plants expressing stefin A and equistatin was observed. Cystatin C and kininogen domain 3 were not found to be active. All tested inhibitors were equally or more active than stefin A at inhibiting the proteolytic activity of thrips, but, in contrast with stefin A, they were all expressed in potato as partially degraded proteins. The resistance of cysteine protease inhibitors against degradation in planta by endogenous plant proteases may therefore be relevant in explaining the observed differences in the deterrence of thrips. The results demonstrate that, when given a choice, western flower thrips will select plants with low levels of certain cysteine protease inhibitors. The novel implications of the defensive role of plant cysteine protease inhibitors as both deterrents and antimetabolic proteins are discussed

    AB - In this study, the effects of the accumulation of cysteine protease inhibitors on the food preferences of adult female western flower thrips, Frankliniella occidentalis (Pergande), were investigated. Representative members of the cystatin and thyropin gene families (stefin A, cystatin C, kininogen domain 3 and equistatin) were expressed in potato (Solanum tuberosum) cv. Impala, Kondor and Line V plants. In choice assays, a strong time- and concentration-dependent deterrence from plants expressing stefin A and equistatin was observed. Cystatin C and kininogen domain 3 were not found to be active. All tested inhibitors were equally or more active than stefin A at inhibiting the proteolytic activity of thrips, but, in contrast with stefin A, they were all expressed in potato as partially degraded proteins. The resistance of cysteine protease inhibitors against degradation in planta by endogenous plant proteases may therefore be relevant in explaining the observed differences in the deterrence of thrips. The results demonstrate that, when given a choice, western flower thrips will select plants with low levels of certain cysteine protease inhibitors. The novel implications of the defensive role of plant cysteine protease inhibitors as both deterrents and antimetabolic proteins are discussed

    KW - pichia-pastoris

    KW - nicotiana-attenuata

    KW - escherichia-coli

    KW - oostatic factor

    KW - cystatin-c

    KW - expression

    KW - resistance

    KW - proteinases

    KW - equistatin

    KW - cloning

    U2 - 10.1111/j.1467-7652.2004.00088.x

    DO - 10.1111/j.1467-7652.2004.00088.x

    M3 - Article

    VL - 2

    SP - 439

    EP - 448

    JO - Plant Biotechnology Journal

    JF - Plant Biotechnology Journal

    SN - 1467-7644

    IS - 5

    ER -