Isolation and molecular characterization of cathepsin L-like cysteine protease cDNAs from Western flower thrips (Frankliniella occidentalis)

A.G.J. Kuipers, M.A. Jongsma

    Research output: Contribution to journalArticleAcademicpeer-review

    7 Citations (Scopus)

    Abstract

    Cysteine proteases are predominant in thrips guts (TGs) and, therefore, a suitable target for selecting effective protease inhibitors against western flower thrips (Frankliniella occidentalis). We report the isolation of four full-length cysteine protease cDNA clones from thrips in a two-step PCR approach with degenerate oligonucleotides designed on conserved cathepsin L domains. At the deduced amino acid level, the clones possessed all functional and structural characteristics of cathepsin L, and showed high mutual identity and strong similarity with cathepsin L-like cysteine proteases from other insects and arthropods. Southern analysis indicated that a family of four closely related and 10 12 less-related genes encode the cathepsin L-like cysteine proteases in the thrips genome. Partial sequencing of genomic DNA demonstrated the presence of three introns in the coding DNA.
    Original languageEnglish
    Pages (from-to)65-75
    JournalComparative Biochemistry and Physiology. B, Biochemistry and Molecular Biology
    Volume139
    Issue number1
    DOIs
    Publication statusPublished - 2004

    Keywords

    • l-like enzyme
    • drosophila-melanogaster
    • cell-line
    • proteinase-inhibitors
    • functional expression
    • pichia-pastoris
    • gene family
    • cloning
    • beetle
    • purification

    Fingerprint Dive into the research topics of 'Isolation and molecular characterization of cathepsin L-like cysteine protease cDNAs from Western flower thrips (Frankliniella occidentalis)'. Together they form a unique fingerprint.

    Cite this