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Sticholysin II (sticholysin + ii)

Distribution by Scientific Domains
Chemistry100%

Selected Abstracts

Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells

FEBS JOURNAL, Issue 4 2006
Jorge Alegre-Cebollada
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. [source]

Crystallization and preliminary X-ray diffraction studies of the water-soluble state of the pore-forming toxin sticholysin II from the sea anemone Stichodactyla helianthus

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2002
José M. Mancheño
Sticholysin II (StnII) is a potent cytolytic protein produced by the sea anemone Stichodactyla helianthus. StnII belongs to the actinoporin family, a group of proteins which are characterized by their ability to spontaneously interact with biological membranes. The cytolytic character of these proteins is currently explained in terms of a molecular mechanism involving the formation of transmembrane pores. StnII has been crystallized using the hanging-drop vapour-diffusion method at 291,K. Diffraction-quality crystals have unit-cell parameters a = 32.30, b = 119.73, c = 43.42,Å, , = 90.04° and belong to the monoclinic space group P21. Diffraction data to a resolution of 1.71,Å were collected at synchrotron facilities. [source]

Detergent-resistant membranes are platforms for actinoporin pore-forming activity on intact cells

FEBS JOURNAL, Issue 4 2006
Jorge Alegre-Cebollada
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. [source]

Crystallization and preliminary X-ray diffraction studies of the water-soluble state of the pore-forming toxin sticholysin II from the sea anemone Stichodactyla helianthus

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2002
José M. Mancheño
Sticholysin II (StnII) is a potent cytolytic protein produced by the sea anemone Stichodactyla helianthus. StnII belongs to the actinoporin family, a group of proteins which are characterized by their ability to spontaneously interact with biological membranes. The cytolytic character of these proteins is currently explained in terms of a molecular mechanism involving the formation of transmembrane pores. StnII has been crystallized using the hanging-drop vapour-diffusion method at 291,K. Diffraction-quality crystals have unit-cell parameters a = 32.30, b = 119.73, c = 43.42,Å, , = 90.04° and belong to the monoclinic space group P21. Diffraction data to a resolution of 1.71,Å were collected at synchrotron facilities. [source]