Interaction of streptolysin O from Streptococcus pyogenes and theta-toxin from Clostridium perfringens with human fibroblasts

Thelestam, Mónica; Möllby, R.

doi:10.1128/iai.29.3.863-872.1980

Cited by 34 publications

(1 citation statement)

References 29 publications

(31 reference statements)

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“…In recent years the toxins were reported to damage the cell membrane of human fibroblasts (Thelestam & Mollby, 1980), Hela cells (Duncan & Buckiftgham, 1980), and myocardial cells (Fisher et al, 1981) in addition to the erythrocyte membrane. However, it is not well understood how they damage the cells after adsorption on the membrane cholesterol.…”

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confidence: 99%

Cold-labile hemolysin produced by limited proteolysis of .theta.-toxin from Clostridium perfringens

Ohno‐Iwashita¹,

Iwamoto²,

Mitsui³

et al. 1986

Biochemistry

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A nicked toxin whose hemolytic activity is temperature dependent was obtained by limited proteolysis of theta-toxin (Mr 54,000) with subtilisin. The nicked toxin (C theta) is a complex of two fragments: the N-terminal fragment (Mr 15,000) with basic isoelectric point and the C-terminal fragment (Mr 39,000) with the single cysteinyl residue of the toxin whose reduced form is essential for the hemolytic activity. C theta hemolyzes erythrocytes only at temperatures above 25 degrees C, whereas the native toxin hemolyzes them even at 10 degrees C. At temperatures below 25 degrees C, C theta does not hemolyze them although it does bind to membrane cholesterol and although no distinct difference was observed between the secondary structure of C theta and that of native toxin. It was found that C theta binds to the cells only in a reversible manner at low temperature, while the native one binds irreversibly to the cells within 10 min, which explains the cold lability of C theta on hemolysis. The structural basis of the cold lability was discussed through comparison of C theta with another nicked derivative of theta-toxin that was also obtained.

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confidence: 99%

Cold-labile hemolysin produced by limited proteolysis of .theta.-toxin from Clostridium perfringens

Ohno‐Iwashita¹,

Iwamoto²,

Mitsui³

et al. 1986

Biochemistry

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PRODUCTION AND CHARACTERIZATION OF ESCHERICHIA COLI ENTEROHEMOLYSIN AND ITS EFFECTS ON THE STRUCTURE OF ERYTHROCYTE MEMBRANES

Jürgens

Özel

Takaisi-Kikuni

2002

Cell Biology International

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Hemolysins are cell-damaging protein toxins produced by pathogenic bacteria, which are usually released into the extracellular medium. Escherichia coli enterohemolysin is an intracellular toxin produced during the log phase of growth, with a maximal intracellular accumulation in the late log phase. In the present study, we have employed electron microscopy and SDS-PAGE to assess the effects of enterohemolysin on erythocyte membranes from different species. The erythrocyte cell damage began immediately after exposure to enterohemolysin with chemically detectable changes in cell membrane permeability, and the formation of surface lesions which increased rapidly in size. This process resulted in complete cell destruction. Ring-shaped structures with a diameter of 10nm were observed by electron microscopy after treatment of horse erythrocyte membranes with enterohemolysin. The ring structures were found clustered and irregularly distributed on the surface of the membranes. Following incubation of the toxin with horse erythrocyte ghosts and detergent-solubilization, the enterohemolysin was isolated from the cytoplasm in its membrane-bound form by sucrose density gradient. SDS-PAGE and silver staining of deoxycholate-solubilized target membranes revealed heterogeneous forms of the toxin. By using SDS-PAGE and gel filtration, the molecular weight of the toxin was estimated to be 35 kDa. With respect to species specificity, horse erythrocytes showed the highest sensitivity to the enterohemolysin, followed by human and guinea pig erythrocytes. The hemolytic sensitivity correlated with the toxin binding capacity of erythrocyte membranes of different animal species. The degree of hemolysis was unaffected by temperature in the range of 4 degrees C-37 degrees C and was optimal at pH 9.0. In contrast to pore-forming cytolysins, the hemolytic activity of enterohemolysin was enhanced continuously in the presence of increasing concentrations of dextran 4 and dextran 8 within the range of 5 to 30 mM. Trypsin sensitivity of membrane-bound enterohemolysin indicates that the cell surface is the most likely target site for this toxin. Additionally, the fact that proteinase and phosphatase inhibitors failed to inhibit lysis suggests that enterohemolysin alters and disrupts cell membranes by a detergent-like mechanism.

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The Potential of Membrane-Acting Toxins for Targeted Cancer Therapy

Drobniewski¹,

Wallace²,

Wawrzynczak

1988

Targeting of Drugs

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Interaction of streptolysin O from Streptococcus pyogenes and theta-toxin from Clostridium perfringens with human fibroblasts

Cited by 34 publications

References 29 publications

Cold-labile hemolysin produced by limited proteolysis of .theta.-toxin from Clostridium perfringens

Cold-labile hemolysin produced by limited proteolysis of .theta.-toxin from Clostridium perfringens

PRODUCTION AND CHARACTERIZATION OF ESCHERICHIA COLI ENTEROHEMOLYSIN AND ITS EFFECTS ON THE STRUCTURE OF ERYTHROCYTE MEMBRANES

The Potential of Membrane-Acting Toxins for Targeted Cancer Therapy

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