Streptolysin S: Improved purification and characterization

Lai, Chun‐Yen; Wang, M T; Faria, Juarez Braz de; Akao, Teruaki

doi:10.1016/0003-9861(78)90423-x

Cited by 29 publications

(18 citation statements)

References 10 publications

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“…The value of 19 000 is similar to the mol. wt estimates (1 1 000 and 18 000) for streptolysin S (Bernheimer, 1967 ;Calandra and Oginsky, 1975 ;Lai et al, 1978). Hryniewicz et al (1978) reported that the mol.…”

Section: Discussionmentioning

confidence: 99%

Production, purification and molecular weight determination of the haemolysin of Treponema hyodysenteriae

Kent

Lemcke²,

Lysons³

1988

Journal of Medical Microbiology

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Summary. The production of haemolysin from Treponema hyodysenteriae was increased by an improved culture method and by repeated incubation of spirochaetes suspended in a buffer containing RNA-core. Ion exchange chromatography on DEAE cellulose followed by gel filtration on Sephadex GlOO yielded purified haemolysin free from extraneous protein, as judged by silver-stained polyacrylamide gels. The mol. wt of the purified haemolysin, determined by gel filtration was 19 000, a value similar to that of streptolysin S, but much lower than that previously reported.

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Section: Discussionmentioning

confidence: 99%

Production, purification and molecular weight determination of the haemolysin of Treponema hyodysenteriae

Kent

Lemcke²,

Lysons³

1988

Journal of Medical Microbiology

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“…After repeated washing in this cell with 20 mM-potassium phosphate/100 mM-ammonium acetate buffer (pH 7.0), the retentate (fraction F1,4.5 ml) was supplemented with 5 m16 M-guanidine. HCl as described by Lai et al (1978), allowed to stand at room temperature for 15 min, ice-chilled, loaded onto a Sephadex G-100 column (2.6 x 100 cm) equilibrated with 20 mM-potassium phosphate/100 mwammonium acetate buffer (pH 7.0) and eluted (flow rate 15 ml h-I) with this buffer. Eluted fractions (3.5 ml) were monitored as described above.…”

Section: Chemicals and Biochemicalsmentioning

confidence: 99%

Purification of RNA-core Induced Streptolysin S, and Isolation and Haemolytic Characteristics of the Carrier-free Toxin

Loridan¹,

Alouf

1986

Microbiology

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RNA-core (RNAase-resistant fraction of yeast RNA) induced streptolysin S (SLS) was purified (40% recovery) to apparent electrophoretic homogeneity by hydroxylapatite chromatography followed by gel filtration on Sephadex G-100 in the presence of 6 M-guanidine. HCl. The specific activity of the purified toxin was 3 X 10(6) haemolytic units (mg protein)-1. The Mr of the toxin was below 4000 on the basis of SDS-PAGE and 20 000 by gel filtration in guanidine. HCl. High-voltage isoelectric focusing of the purified toxin allowed the isolation of the carrier-free SLS peptide for the first time. This peptide was basic (pI 9.2) as compared to native SLS (pI 3.6). The native toxin and the peptide had similar haemolytic properties except for the high lability of the peptide, which was stabilized by RNA-core. The Mr of the denatured peptide was about 1800, as estimated by gel filtration.

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“…The standard hemolysis assay for thiol-activated cytolysins was described in previous papers (17,27). SLS-induced hemolysis was determined as described previously (15). One HU of each cytolysin was defined as the amount of cytolysin required to cause 50% hemolysis (HD 50 ) of sheep erythrocytes (1.5 ml of 1% suspension) in 30 min at 37 C.…”

Section: Materials Perfringolysin O (Plo) Frommentioning

confidence: 99%

“…SLS was produced essentially from S. pyogenes cell wall extract as reported (15). LPS from Escherichia coli (serotype 026: B6) and brain heart infusion (BHI) were products of Difco Laboratories (Detroit, Mich., U.S.A.).…”

Section: Materials Perfringolysin O (Plo) Frommentioning

confidence: 99%

Chemokine Production by Rat Macrophages Stimulated with Streptolysin O from Streptococcus pyogenes

Mitsui

Takano

Nakatani

et al. 2002

Microbiology and Immunology

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The contribution of streptolysin O (SLO) from Streptococcus pyogenes to neutrophil infiltration in inflammatory lesions was determined by production of cytokine‐induced neutrophil chemoattractant (CINC)−1, −2 and −3, and macrophage inflammatory protein (MIP)‐1α by rat macrophages stimulated with SLO in culture. Active SLO induced the production of CINCs and MIP‐1α in dose‐ and time‐dependent manners. These inductions were ascertained by chemokine mRNA expression in macrophages. Streptolysin S was without effect. The SLO‐cholesterol complex induced the chemokine production in proportion to the residual hemolytic activity of the complex. In addition, the effects of SLO on the chemokine production were confirmed by the injection of active SLO into the preformed air pouch on the back of rats. The infiltration of neutrophils into the pouch fluid (exudate) increased steadily with a lag phase of about 2 hr. The major chemokine found in exudates was MIP‐1α but not CINCs. In this study, it became clear that active SLO, but not the inactive one, contributed to the production of MIP‐1α and CINCs in the conditioned medium and in exudates.

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Streptolysin S: Improved purification and characterization

Cited by 29 publications

References 10 publications

Production, purification and molecular weight determination of the haemolysin of Treponema hyodysenteriae

Production, purification and molecular weight determination of the haemolysin of Treponema hyodysenteriae

Purification of RNA-core Induced Streptolysin S, and Isolation and Haemolytic Characteristics of the Carrier-free Toxin

Chemokine Production by Rat Macrophages Stimulated with Streptolysin O from Streptococcus pyogenes

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