The differentiation of two distinct serological varieties of streptolysin, streptolysin O and streptolysin S

Todd, E. W.

doi:10.1002/path.1700470307

Cited by 92 publications

(47 citation statements)

References 8 publications

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“…Although it appears from Todd's experiments (9) that some rabbits may show a high degree of streptolysin S inhibition following intensive "immunization" with live cultures of beta hemolytic streptococci, specific antibodies do not appear to play a significant role in the neutralization of streptolysin S in streptococcal disease ( 1 ).…”

Section: Discussionmentioning

confidence: 99%

The Association of Lipoproteins With the Inhibition of Streptolysin S by Serum 1

Stollerman¹,

Bernheimer²,

MacLeod³

1950

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

The Association of Lipoproteins With the Inhibition of Streptolysin S by Serum 1

Stollerman¹,

Bernheimer²,

MacLeod³

1950

J. Clin. Invest.

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“…The properties of these hemolysins are described in the papers of Todd (10) and Herbert and Todd (11,12).…”

Section: Probable Identity Of Nucleic Acid-induced Streptolysin With mentioning

confidence: 99%

The Effect of Nucleic Acids and of Carbohydrates on the Formation of Streptolysin

Bernheimer

Rodbart

1948

Journal of Experimental Medicine

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Yeast nucleic acid has been shown by Okamoto (1) to induce the formation of a potent hemolysin in cultures of Streptococcus pyogenes. As reported b y Okamoto, and confirmed in the present paper, the effect of nucleic acid is readily demonstrable since the hemolytic activity of filtrates or supernates of nucleic acid-broth cultures is at least 20 to 100 times greater than the activity of cultures prepared in broth to which no nucleic acid has been added. On blood agar containing yeast nucleic acid, the effect is manifest by the appearance of very large zones of beta hemolysis around the colonies.The nucleic acid effect has been investigated further in order to define the conditions necessary for producing the hemolysin on a large scale and in a manner which will facilitate its purification. In addition, although some of the properties of the nucleic acid-induced hemolysin have been described b y It6 (2), the relationship of this hemolysin to the better characterized streptococcal hemolysins, streptolysin O and streptolysin S, requires clarification. Finally, an opportunity is afforded of studying an almost unknown biological effect of nucleic acid. Methods, Materials, and TerminologyPreparation of Peptone-Infusion Broth.--Fresh beef hearts, freed of gross fat, were ground and then mixed well with tap water, 1 liter of water for each pound of ground heart. Mter being brought to 85°C. and infused at that temperature for 45 minutes, the mixture was filtered while hot, through paper. To each liter of infusion was added 10 gin. peptone (neopeptone Difco) and 5 gin. reagent sodium chloride. After the ingredients were completely dissolved by bringing to a boil, the pI-I was brought to 7.9, the medium was boiled 1 to 2 minutes, and then filtered immediately through paper. The medium was sterilized in the autoclave at 121°C. for 15 to 30 minutes. Immediately before inoculating, a freshly prepared solution of sodium thioglycollate was added to give a final concentration of 0.01 per cent.Culture Technique.--A 6 to 8 hour peptone-infusion broth culture of Streptococcus pyogenes, strain C203S, was distributed in 0.5 ce. amounts among a large number of sterile tubes, and then rapidly frozen solid in an alcohol-carbon dioxide freezing mixture. The tubes were stored in a dry-ice chest until needed. When required, a tube was thawed at room temperature, the contents diluted 10 times in sterile saline, and 0.1 cc. inoculated into each 10 cc. of

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“…These modifications have been shown to be critical for the cytolytic activity of SLS-like peptide toxins (7,8). The cytolytic activity of SLS has historically been attributed to its ability to induce osmotic deregulation and subsequent lysis through an unknown mechanism, and the toxin has been reported to cause membrane rupture in a variety of eukaryotic cell types and subcellular structures (6,(9)(10)(11)(12)(13)(14)(15)(16)(17). The lytic activity of SLS is often measured via red blood cell (RBC) lysis because it is the GAS toxin primarily responsible for the characteristic hemolytic zone that surrounds bacterial colonies on blood agar (18).…”

mentioning

confidence: 99%

Streptolysin S Promotes Programmed Cell Death and Enhances Inflammatory Signaling in Epithelial Keratinocytes during Group A Streptococcus Infection

et al. 2015

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Streptococcus pyogenes, or group A Streptococcus (GAS), is a pathogen that causes a multitude of human diseases from pharyngitis to severe infections such as toxic shock syndrome and necrotizing fasciitis. One of the primary virulence factors produced by GAS is the peptide toxin streptolysin S (SLS). In addition to its well-recognized role as a cytolysin, recent evidence has indicated that SLS may influence host cell signaling pathways at sublytic concentrations during infection. We employed an antibody arraybased approach to comprehensively identify global host cell changes in human epithelial keratinocytes in response to the SLS toxin. We identified key SLS-dependent host responses, including the initiation of specific programmed cell death and inflammatory cascades with concomitant downregulation of Akt-mediated cytoprotection. Significant signaling responses identified by our array analysis were confirmed using biochemical and protein identification methods. To further demonstrate that the observed SLS-dependent host signaling changes were mediated primarily by the secreted toxin, we designed a Transwell infection system in which direct bacterial attachment to host cells was prevented, while secreted factors were allowed access to host cells. The results using this approach were consistent with our direct infection studies and reveal that SLS is a bacterial toxin that does not require bacterial attachment to host cells for activity. In light of these findings, we propose that the production of SLS by GAS during skin infection promotes invasive outcomes by triggering programmed cell death and inflammatory cascades in host cells to breach the keratinocyte barrier for dissemination into deeper tissues. Streptococcus pyogenes, also known as group A Streptococcus (GAS), is a common colonizer of the skin and mucosal surfaces of humans (1-3). GAS is typically innocuous in these locations or else leads to fairly minor and generally self-limiting infections of the skin or respiratory tract, such as impetigo or pharyngitis (1-3). In cases where an initial infection is left untreated, GAS may cause one of several severe postinfection (p.i.) sequelae, including rheumatic fever or glomerulonephritis (1-3). Furthermore, in rare cases, this exclusively human pathogen breaches the epithelial barrier and invades deeper tissues and blood, resulting in outcomes such as necrotizing fasciitis and Streptococcus toxic shock (1-3). The World Health Organization (WHO) estimates that GAS is responsible for about 18 million cases of severe postinfection sequelae and 700,000 cases of invasive disease each year (2, 4). Combined, GAS infections lead to approximately 500,000 deaths annually (2, 4).The success of GAS in causing both mild and severe infections is due largely to the myriad of secreted and surface-bound virulence factors expressed by this pathogen. One of the most potent virulence factors produced by GAS is streptolysin S (SLS), a small, ribosomally produced peptide whose mature product is predicted to be 2.7 kDa in size (5-8...

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The differentiation of two distinct serological varieties of streptolysin, streptolysin O and streptolysin S

Cited by 92 publications

References 8 publications

The Association of Lipoproteins With the Inhibition of Streptolysin S by Serum 1

The Association of Lipoproteins With the Inhibition of Streptolysin S by Serum 1

The Effect of Nucleic Acids and of Carbohydrates on the Formation of Streptolysin

Streptolysin S Promotes Programmed Cell Death and Enhances Inflammatory Signaling in Epithelial Keratinocytes during Group A Streptococcus Infection

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