Characteristics of Streptolysin O Action

Oberley, Terry D.; Duncan, James L.

doi:10.1128/iai.4.6.683-687.1971

Cited by 44 publications

(22 citation statements)

References 11 publications

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“…On the other hand our results suggest that this cysteine residue (and the encompassing region) is not essential for binding to cholesterol, as is currently believed [2][3][4]8,9,12,13], rather it seems to be essential specifically for cytolysis, perhaps by contributing to the conformation of the previously described transmembrane circular or semicircular oligomeric forms of the toxin [2,3], in which cholesterol seems not to take part [22]. These observations are consistent with several reported results suggesting that the thiol groups of SH-cytolysins are not involved in the interaction with membrane cholesterol [2,21,23]. The cholesterol binding sites, therefore, appear to be located in a region other than that of the essential cysteine.…”

Section: Llosupporting

confidence: 90%

Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin

Vázquez‐Boland

1989

FEMS Microbiology Letters

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The inactive truncated 52 Kilodaltons (kDa) Listeriolysin O (LLO) produced by a transposon Tn1545-induced Listeria monocytogenes non-hemolytic/avirulent mutant previously described (Gaillard et al. (1986) Infect. Immun. 52, 50-55), that lacks a 48 aminoacid fragment at the C-terminal end including the single cysteine residue essential for activity (Mengaud et al. (1988) Infect. Immun. 56, 766-772), bound to the SH-cytolysin membrane receptor cholesterol, as did the active 60 kDa toxin. These results indicate that the missing fragment is a functionally important region needed in the 60 kDa LLO to cause membrane-disruption but not to bind to cholesterol, which strongly suggests that in LLO (and presumably in the other SH-cytolysins, in accordance with their structural and functional homologies) different domains are involved in cytolytic activity and cholesterol binding. The cysteine residue contained in the missing fragment, therefore, would not be essential for cholesterol binding, as is currently thought, rather it seems to be essential specifically for cell lysis.

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Section: Llosupporting

confidence: 90%

Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin

Vázquez‐Boland

1989

FEMS Microbiology Letters

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“…It is possible that the configurational changes produced in this lysin when disulphide bonds are reduced are necessary for the lysis of erythrocytes. It may be that attachment to the erythrocyte membrane is achieved through free SK-groups, although this hypothesis is not supported by investigators who have studied other thiol-activated haemolysins (Oberley & Duncan 1971).…”

Section: Inks Albesamentioning

confidence: 96%

Klebsiella pneumoniae haemolysin adsorption to red blood cells

Albesa

1989

Journal of Applied Bacteriology

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It was necessary to incubate the Klebsiella pneumoniae haemolysin with erythrocytes at 37 degrees C to produce the whole lytic action. The amount of attached klebolysin at 4 degrees C increased as its concentration in the medium increased, until the erythrocyte surface was saturated. Treatment with 2-mercaptoethanol was necessary to permit the adsorption; it was inhibited by low concentrations of cholesterol. Klebsolysin was immunogenic and its antiserum neutralized its own haemolytic effect and streptolysin O. Anti-streptolysin serum also neutralized klebsolysin. Streptolysin O attachment to erythrocytes impeded the posterior klebolysin adsorption in the same way that klebsolysin adsorption interfered with streptolysin O attachment.

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“…SLO will adsorb to erythrocytes at 0-4~ but hemolysis does not occur at those low temperatures (1,18). To determine whether the adsorption of toxin to the cell membrane was sufficient to produce the ringlike structures, red cells and toxin were incubated together at 0~ Glutaraldehyde fixation of the sample preparation was carried out at 0-4~ Upon examination, the membranes were normal with no evidence of ring formation.…”

Section: Effect Of Slo On Erythrocyte Membrane Structurementioning

confidence: 99%

Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction.

Duncan¹,

Schlegel²

1975

The Journal of Cell Biology

134

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The effect of the bacterial cytolytic toxin, streptolysin O (SLO), on rabbit erythrocyte membranes, liposomes, and lipid dispersions was examined. SLO produced no gross alterations in the major erythrocyte membrane proteins or lipids. However, when erythrocytes were treated with SLO and examined by electron microscopy, rings and "C"-shaped structures were observed in the cell membrane. The rings had an electron-dense center, 24 nm in diameter, and the overall diameter of the structure was 38 nm. Ring formation also occurred when erythrocyte membranes were fixed with glutaraldehyde and OsO4 before the addition of toxin. In contrast, rings were not seen when erythrocytes were treated with toxin at 0~indicating that adsorption of SLO to the membrane is not sufficient for ring formation since toxin is known to bind to erythrocytes at that temperature. The ring structures were present on lecithin-cholesterol-dicetylphosphate liposomes after SLO treatment, but there was no release of the trapped, internal markers, K2CrO4 or glucose. The crucial role of cholesterol in the formation of rings and C's was demonstrated by the fact that these structures were present in toxin-treated cholesterol dispersions, but not in lecithin-dicetylphosphate dispersions nor in the SLO preparations alone. The importance of cholesterol was also shown by the finding that no rings were present in membranes or cholesterol dispersions which had been treated with digitonin before SLO was added. Although the rings do not appear to be "holes" in the membrane, a model is proposed which suggests that cholesterol molecules are sequestered during ring and C-structure formation, and that this process plays a role in SLO-induced hemolysis.Streptolysin O (SLO) is a bacterial toxin produced by virtually all strains of Streptococcus pyogenes. The toxin is a protein with a molecular weight of approximately 60,000 daltons, and is characteristic of a group of cytolytic toxins known as the oxygen-labile toxins (3). The toxins in this group are produced by several different gram-positive bacteria, and possess a number of common properties: they are activated by SH compounds: they appear to be antigenically related; and their biological activity is completely inhibited by low concentrations of cholesterol and certain related sterols.Hemolysis occurs within minutes after the addi-160 THE JOURNAL OF CELL BIOLOGY 9 VOLUME 67, 1975 9 pages 160-173 tion of SLO to erythrocytes, and toxic effects of SLO on several types of mammalian cells in culture have been demonstrated (13). The speed with which sensitive cells are affected by the toxin suggests that the cell membrane is the primary site of action. Several lines of indirect evidence suggest that membrane cholesterol is the binding site and/or target of SLO action. Only those cells which contain cholesterol in their membranes are susceptible to the toxin, SLO is "inactivated" only by the membrane lipid fraction which contains cholesterol, and the addition of exogenous cholesterol to SLO inhibits toxin action....

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Characteristics of Streptolysin O Action

Cited by 44 publications

References 11 publications

Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin

Preliminary evidence that different domains are involved in cytolytic activity and receptor (cholesterol) binding in listeriolysin O, the Listeria monocytogenes thiol-activated toxin

Klebsiella pneumoniae haemolysin adsorption to red blood cells

Effect of streptolysin O on erythrocyte membranes, liposomes, and lipid dispersions. A protein-cholesterol interaction.

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