Interaction between sphingomyelin and a cytolysin from the sea anemone Stoichactis helianthus

Linder, Regina; Bernheimer, Alan W.; Kim, Kwang-Shin

doi:10.1016/0005-2736(77)90306-6

Cited by 45 publications

(16 citation statements)

References 12 publications

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“…Previous work has suggested that S. helianthus toxin specifically requires sphingomyelin for its action on lipid vesicles or mammalian cells (Bernheimer & Avigad, 1976;Linder et al, 1977). Our result with planar lipid bilayer membranes (Table 1) show that although the toxin's ability to increase membrane conductance is enhanced by the presence of sphingomyelin in the membrane, the toxin is still very active on membranes containing no sphingomyelin.…”

Section: A Lipid Dependence Of Stoichastis Helianthus Toxincontrasting

confidence: 45%

“…Departmento de Fisologia e Farmacologia, Instituto de Ci6ncias Biom6dicas, CP 4365 01000 Silo Paulo, Brasil ~16,000) which acts as a cytolytic toxin (Devlin, 1974;Bernheimer & Avigad, 1976). From studies of the hemolytic effect of the toxin on red cells and of the release of trapped marker from toxin-treated liposomes, Bernheimer and his colleagues concluded that the toxin acts directly on the plasma membrane and that sphingomyelin is a necessary component in the membrane for its action (Bernheimer & Avigad, 1976;Linder, Bernheimer & Kim, 1977).…”

mentioning

confidence: 97%

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Ion and nonelectrolyte permeability properties of channels formed in planar lipid bilayer membranes by the cytolytic toxin from the sea anemone,Stoichactis helianthus

Varanda

Finkelstein

1980

J. Membrain Biol.

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Summary. When present at nanomolar concentrations on one side of a lipid bilayer membrane, helianthus toxin (a protein of mol wt~ 16,000) increases enormously membrane permeability to ions and nonelectrolytes by forming channels in the membrane. Membranes containing sphingomyelin are especially sensitive to toxin, but sphingomyelin is not required for toxin action. Conductance is proportional to about the 4th power of toxin concentration. Single channel conductances are approximately 2• -l~ mho in 0.1M KC1. Toxin-treated membranes are more permeable to K + and Na + than to C1-and SO2, but the degree of selectivity is pH dependent. Above pH 7 membranes are almost ideally selective for K + with respect to SO2, whereas below pH 4 they are poorly selective. The channels show classical molecular sieving for urea, glycerol, glucose, and sucrose -implying a channel radius > 5 A_. In symmetrical salt solutions above pH 7, the I-V characteristic of the channel shows significant rectification; below pH 5 there is very little rectfication. Because of the effects of pH on ion selectivity and channel conductance, and also because of the rectification in symmetrical salt solutions and the effect of pH on this, we conclude that there are titratable negative charge groups in the channel modulating ion permeability and selectivity. Since pH changes on the side containing the toxin are effective whereas pH changes on the opposite side are not, we place these negative charges near the mouth of the channel facing the solution to which toxin was added.The sea anemone Stoichactis helianthus produces a basic protein (isoelectric point pH9.8; tool wt * Present address."

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Section: A Lipid Dependence Of Stoichastis Helianthus Toxincontrasting

confidence: 45%

mentioning

confidence: 97%

Ion and nonelectrolyte permeability properties of channels formed in planar lipid bilayer membranes by the cytolytic toxin from the sea anemone,Stoichactis helianthus

Varanda

Finkelstein

1980

J. Membrain Biol.

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“…The haemolytic activity of a cytolysin from Stoichactis (now Stichodactyla) helianthus was inhibited by pre-incubation with SM, and treatment of erythrocyte membranes with sphingomyelinase rendered them resistant to lysis. 20,21 The haemolytic activity of the actinoporin equinatoxin II (EqTII) was also inhibited by preincubation with SM. 22 More recent studies with sticholysins I 14 and II 15 on model membranes confirmed that SM enhances lytic activity and suggested that cholesterol may have a minor role.…”

Section: Introductionmentioning

confidence: 98%

Interaction of the Eukaryotic Pore-forming Cytolysin Equinatoxin II with Model Membranes: 19F NMR Studies

Anderluh

Razpotnik

Podlesek

et al. 2005

Journal of Molecular Biology

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“…Bernheimer and Avigad [21] first reported the interaction of a sea anemone toxin from Stoichactis helianthus with membrane lipids and cell membranes [23,24]. Sphingomyelin had been declared to be the specific receptor molecule.…”

Section: Structure Of Toxins; Interac-tions With Lipidsmentioning

confidence: 99%

Polypeptide cytolytic toxins from sea anemones (Actiniaria)

Maček

1992

FEMS Microbiology Letters

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Interaction between sphingomyelin and a cytolysin from the sea anemone Stoichactis helianthus

Cited by 45 publications

References 12 publications

Ion and nonelectrolyte permeability properties of channels formed in planar lipid bilayer membranes by the cytolytic toxin from the sea anemone,Stoichactis helianthus

Ion and nonelectrolyte permeability properties of channels formed in planar lipid bilayer membranes by the cytolytic toxin from the sea anemone,Stoichactis helianthus

Interaction of the Eukaryotic Pore-forming Cytolysin Equinatoxin II with Model Membranes: 19F NMR Studies

Polypeptide cytolytic toxins from sea anemones (Actiniaria)

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