Disruption of Wall-less Bacteria by Streptococcal and Staphylococcal Toxins

Bernheimer, Alan W.

doi:10.1128/jb.91.5.1677-1680.1966

Cited by 29 publications

(11 citation statements)

References 10 publications

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“…remain undefined. Preparations of stabilized SLS are lytic to bacterial protoplasts and spheroplasts (Bernheimer, 1966), but to date no definitive bacteriocidal activities against cell-wall competent bacteria have been defined in co-culture experiments comparing wild type and SLSnegative mutant GAS (Nizet et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection

Datta

Myskowski

Kwinn

et al. 2005

Molecular Microbiology

158

220

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SummaryThe pathogen group A Streptococcus (GAS) produces a wide spectrum of infections including necrotizing fasciitis (NF). Streptolysin S (SLS) produces the hallmark b b b b -haemolytic phenotype produced by GAS. The nine-gene GAS locus ( sag A-sag I) resembling a bacteriocin biosynthetic operon is necessary and sufficient for SLS production. Using precise, inframe allelic exchange mutagenesis and single-gene complementation, we show sag A, sag B, sag C, sag D, sag E, sag F and sag G are each individually required for SLS production, and that sag E may further serve an immunity function. Limited site-directed mutagenesis of specific amino acids in the SagA prepropeptide supports the designation of SLS as a bacteriocin-like toxin. No significant pleotrophic effects of sag A deletion were observed on M protein, capsule or cysteine protease production. In a murine model of NF, the SLS-negative M1T1 GAS mutant was markedly diminished in its ability to produce necrotic skin ulcers and spread to the systemic circulation. The SLS toxin impaired phagocytic clearance and promoted epithelial cell cytotoxicity, the latter phenotype being enhanced by the effects of M protein and streptolysin O. We conclude that all genetic components of the sag operon are required for expression of functional SLS, an important virulence factor in the pathogenesis of invasive M1T1 GAS infection.

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Section: Discussionmentioning

confidence: 99%

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection

Datta

Myskowski

Kwinn

et al. 2005

Molecular Microbiology

158

220

View full text Add to dashboard Cite

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“…It has been suggested that cholesterol is involved in the lytic action (2,3). Such a sterol could serve as the receptor site (or substrate) for the toxin (1). Although these toxins may be similar in many ways, the same mechanism of action may not necessarily be found for each member of this group of toxins.…”

Section: Fig 2 (A)mentioning

confidence: 99%

Effect of Tetanolysin on Platelets and Lysosomes

1974

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Tetanolysin, partially purified, caused the lysis of human and rabbit platelets, as determined by a decrease in the optical density of platelet suspensions and the release of serotonin, enzymes, and protein. This lytic activity was neutralized by antitoxin. In addition, a suspension of the lysosome-containing large granule fraction of rabbit liver released hydrolytic enzymes when exposed to tetanolysin. Thus, tetanolysin can be added to the list of bacterial toxins that are lytic for a variety of cellular or subcellular membranes. These findings provide additional data that suggest that tetanolysin may contribute to the pathogenesis of some of the unusual manifestations observed in clinical tetanus.

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“…Protoplasts of Streptococcus faecalis (ATCC 9790) were prepared by the method of Shockman and Slade (61) by use of 1 mg of lysozyme per ml for 16 hr at 37 C. The protoplasts were sedimented by centrifugation and were suspended in 0.5 M sucrose in 0.05 M phosphate buffer (pH 6.6) containing 0.01 M Mga+. Micrococcus lysodeikticus protoplasts were prepared with lysozyme as reported by Bernheimer (5). Protoplasts of Bacillus megaterium KM and Sarcina lutea and spheroplasts of Escherichia coli W [prepared with lysozyme and ethylenediaminetetraacetic acid (EDTA)J and Vibrio metschnikovii were obtained as previously described (10).…”

Section: Gel Filtration Chromatography Gel Ifitration Was Performed mentioning

confidence: 99%

Purification and Properties of Staphylococcal Delta Hemolysin

et al. 1971

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Large amounts (200 mg per liter of culture supernatant fluid) of highly purified staphylococcal soluble delta hemolysin were obtained by adsorption to and selective elution from hydroxyapatite followed by exhaustive dialysis against water, concentration by polyvinylpyrrolidone or polyethylene glycol 20,000 dialysis, and a final water dialysis. No carbohydrate, phosphorus, or inactive 280-nm absorbing material was detected in the preparation; however, analysis by density gradient centrifugation, gel filtration, analytical ultracentrifugation, carboxymethyl cellulose chromatography, polyacrylamide disc gel electrophoresis, isoelectric focusing, and electron microscopy revealed that the lysin was molecularly heterogeneous. The preparation contained an acidic fibrous lysin (S20, of 11.9) and a basic lysin component composed of a population of granular aggregates of various sizes, with a maximum Sm,, of approximately 4.9. No other staphylococcal products were detected in the preparation. The lysin was active against erythrocytes from many animal species and acted synergistically with staphylococcal beta hemolysin against sheep erythrocytes. It was soluble in chloroform-methanol (2: 1), was inactivated by various phospholipids, normal sera, and proteolytic enzymes, but was partially resistant to heat inactivation. Activity was not affected by Ca2+, Mg2+, citrate, ethylenediaminetetraacetic acid, or cysteine. The lysin preparation also disrupted bacterial protoplasts and spheroplasts, erythrocyte membranes, lysosomes, and lipid spherules, was growth-inhibitory for certain bacteria, and clarified egg yolk-agar. Large amounts produced dermonecrosis in rabbits and guinea pigs. The minimum lethal intravenous dose for mice and guinea pigs was approximately 110 and 30 mg/kg, respectively. (vii) clear egg yolk-agar (41); and (viii) possess phospholipase C activity with phosphatidylinositol and phosphatidylserine as substrates (67). Rigorous proof for the belief that all of these effects are caused by delta hemolysin is lacking. Delta hemolysin has been partially purified and characterized by Marks and Vaughan (51),

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Disruption of Wall-less Bacteria by Streptococcal and Staphylococcal Toxins

Cited by 29 publications

References 10 publications

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection

Effect of Tetanolysin on Platelets and Lysosomes

Purification and Properties of Staphylococcal Delta Hemolysin

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