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- Title
Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells.
- Authors
Alegre-Cebollada, Jorge; Rodríguez-Crespo, Ignacio; Gavilanes, José G.; del Pozo, Álvaro Martínez
- Abstract
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.
- Subjects
STICHODACTYLIDAE; SEA anemones; TOXINS; FLUORESCENCE spectroscopy; FLOW cytometry; CYCLODEXTRINS; PERMEABILITY
- Publication
FEBS Journal, 2006, Vol 273, Issue 4, p863
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2006.05122.x