Identification and characterization of digestive serine proteases from inhibitor-resistant Helicoverpa zea larval midgut

M. Volpicella, J.H.G. Cordewener, M.A. Jongsma, R. Gallerani, L.R. Ceci, M.J. Beekwilder

    Research output: Contribution to journalArticleAcademicpeer-review

    13 Citations (Scopus)

    Abstract

    Protease inhibitors mediate a natural form of plant defence against insects, by interfering with the digestive system of the insect. In this paper, affinity chromatography was used to isolate trypsins and chymotrypsins from Helicoverpa zea larvae, which had been raised on inhibitor-containing diet. Sensitivity of the fractions to inhibition by plant proteinase inhibitors was tested, and compared to the sensitivity of proteinases found in insects raised on diet to which no inhibitor had been added. The isolated chymotrypsin activity was found to be less sensitive to plant protease inhibitors. The sensitivity of the isolated trypsin activity was found to be intermediate between completely sensitive trypsins and completely insensitive forms that have been previously described. Mass spectrometry was used to identify one trypsin and two chymotrypsins in the partially purified protease fraction. The sequence features of these proteases are discussed in relation to their sensitivity to inhibitors. The results provide insight in the enzymes deployed by Helicoverpa larvae to overcome plant defence
    Original languageEnglish
    Pages (from-to)26-32
    JournalJournal of Chromatography. B, Analytical technologies in the biomedical and life sciences
    Volume833
    Issue number1
    DOIs
    Publication statusPublished - 2006

    Keywords

    • plant proteinase-inhibitors
    • soybean trypsin-inhibitor
    • agrotis-ipsilon
    • gut proteinases
    • complex
    • expression
    • induction
    • insects
    • tobacco
    • genes

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