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  • Binding specificity of ostreolysin A6 towards Sf9 insect cell lipids

    Author(s)
    Novak, M
    Krpan, T
    Panevska, A
    Shewell, LK
    Day, CJ
    Jennings, MP
    Guella, G
    Sepčić, K
    Griffith University Author(s)
    Jennings, Michael P.
    Day, Christopher J.
    Shewell, Lucy K.
    Year published
    2020
    Metadata
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    Abstract
    Oyster mushrooms (Pleurotus spp.) have recently been shown to produce insecticidal bi-component protein complexes based on the aegerolysin proteins. A role for these proteins is thus indicated for defence and protection of the mushroom, and we propose their use as new environmentally friendly bioinsecticides. These aegerolysin-based protein complexes permeabilise artificial lipid vesicles through aegerolysin binding to an insect-specific sphingolipid, ceramide phosphoethanolamine (CPE), and they are cytotoxic for the Spodoptera frugiferda (Sf9) insect cell line. Tandem mass spectrometry analysis of the Sf9 lipidome uncovered ...
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    Oyster mushrooms (Pleurotus spp.) have recently been shown to produce insecticidal bi-component protein complexes based on the aegerolysin proteins. A role for these proteins is thus indicated for defence and protection of the mushroom, and we propose their use as new environmentally friendly bioinsecticides. These aegerolysin-based protein complexes permeabilise artificial lipid vesicles through aegerolysin binding to an insect-specific sphingolipid, ceramide phosphoethanolamine (CPE), and they are cytotoxic for the Spodoptera frugiferda (Sf9) insect cell line. Tandem mass spectrometry analysis of the Sf9 lipidome uncovered lipids not previously reported in the literature, including in particular C14 sphingosine-based CPE molecular species, which comprised ~4 mol% of the whole lipidome. Further analysis of the lipid binding specificity of an aegerolysin from P. ostreatus, ostreolysin A6 (OlyA6), to lipid vesicles composed of commercial lipids, to lipid vesicles composed of the total lipid extract from Sf9 cells, and to HPLC-separated Sf9 cell lipid fractions containing ceramides, confirmed CPE as the main OlyA6 receptor, but also highlighted the importance of membrane cholesterol for formation of strong and stable interactions of OlyA6 with artificial and natural lipid membranes. Binding assays performed with glycan arrays and surface plasmon resonance, which included invertebrate-specific glycans, excluded these saccharides as potential additional OlyA6 receptors.
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    Journal Title
    Biochimica et Biophysica Acta - Biomembranes
    Volume
    1862
    Issue
    9
    DOI
    https://doi.org/10.1016/j.bbamem.2020.183307
    Subject
    Biochemistry and Cell Biology
    Other Biological Sciences
    Chemical Engineering
    Aegerolysin
    Ceramide phosphoethanolamine
    Insect glycans
    Lipidome
    Mass spectrometry
    Publication URI
    http://hdl.handle.net/10072/400483
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