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  • Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina
    Barlič, Ariana ...
    Equinatoxin-II is a eukaryotic pore-forming toxin belonging to the family of actinoporins. Its interaction with model membranes is largely modulated by thepresence of sphingomyelin. We have used ... large unilamellar vesicles and lipid monolayers to gain further information about this interaction. The coexistence of gel and liquid-crystal lipid phases in sphingomyelin/phosphatidylcholine mixtures and the coexistence of liquid-ordered and liquiddisordered lipid phases in phosphatidylcholine/cholesterol or sphingomyelin/phosphatidylcholine/cholesterol mixtures favor membrane insertion of equinatoxin-II. Phosphatidylcholine vesicles are not permeabilized by equinatoxin-II. However, the localized accumulation of phospholipase C-generated diacylglycerol createa conditions for toxin activity. By using epifluorescence microscopy of transferred monolayers, it seems that lipid packing defects arising at the interfaces between coexisting lipid phases may function as preferential binding sites for the toxin. The possible implications of such a mechanism in the assembly of a toroidal pore are discussed.
    Vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 279, št. 33, 2004, str. 34209-34216)
    Vrsta gradiva - članek, sestavni del
    Leto - 2004
    Jezik - angleški
    COBISS.SI-ID - 19243993

    Povezava(-e):

    http://www.jbc.org

vir: The Journal of biological chemistry. - ISSN 0021-9258 (Letn. 279, št. 33, 2004, str. 34209-34216)
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