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Detergent‐resistant membranes are platforms for actinoporin pore‐forming activity on intact cells
Author(s) -
AlegreCebollada Jorge,
RodríguezCrespo Ignacio,
Gavilanes José G.,
Pozo Álvaro Martínez
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05122.x
Subject(s) - raft , membrane , sea anemone , flow cytometry , pore forming toxin , vesicle , microbiology and biotechnology , biophysics , lysis , lipid raft , cytolysis , biology , cholera toxin , cell membrane , propidium iodide , ganglioside , toxin , biochemistry , chemistry , programmed cell death , apoptosis , in vitro , cytotoxicity , ecology , microbial toxins , organic chemistry , copolymer , polymer
Sticholysin II is a pore‐forming toxin produced by the sea anemone Stichodactyla helianthus . We studied its cytolytic activity on COS‐7 cells. Fluorescence spectroscopy and flow cytometry revealed that the toxin permeabilizes cells to propidium cations in a dose‐dependent and time‐dependent manner. This permeabilization is impaired by preincubation of cells with cyclodextrin. Isolation of detergent‐resistant cellular membranes showed that sticholysin II colocalizes with caveolin‐1 in fractions corresponding to raft‐like domains. The interaction of sticholysin II with such domains is only lipid dependent as it also occurs in the absence of any other membrane‐associated protein. Toxin binding to raft‐like lipid vesicles inhibited cell permeabilization. The results suggest that sticholysin II promotes pore formation in COS‐7 cells through interaction with membrane domains which behave like cellular rafts.