Isolierung und Charakterisierung von erythrogenen Toxinen VIL Untersuchung des von Streptococcus pyogenes gebildeten erythrogenen Toxins Typ C

Ozegowski, Jörg‐Hermann; Knöll, Heide; Gerlach, Dieter

doi:10.1016/s0174-3031(84)80041-4

Cited by 6 publications

(6 citation statements)

References 28 publications

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“…ETC was purified from culture filtrate of S. pyogenes NY-5 as described previously (33). Unless otherwise stated, the monocytes and PBMC were challenged with increasing concentrations of ETA and ETC ranging from 0.2 to 20 ,ug/ml of cell suspension.…”

Section: Methodsmentioning

confidence: 99%

Comparative study of cytokine release by human peripheral blood mononuclear cells stimulated with Streptococcus pyogenes superantigenic erythrogenic toxins, heat-killed streptococci, and lipopolysaccharide

et al. 1994

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The differences between toxic or septic shocks in humans during infections by streptococci and gramnegative bacteria remain to be fully characterized. For this purpose, a quantitative study of the cytokineinducing capacity of Streptococcus pyogenes erythrogenic (pyrogenic) exotoxins (ETs) A and C, heat-killed S. pyogenes bacteria, and Neisseria meningitidis endotoxin (lipopolysaccharide [LPS]) on human peripheral blood mononuclear cells (PBMC) and monocytes has been undertaken. The levels of interleukin-la (IL-la), IL-1p, IL-6, IL-8, tumor necrosis factor alpha (TNF-a), and TNF-, induced by these bacterial products and bacteria were determined by using cell supernatants. The capacity of ETs to elicit the monocyte-derived cytokines IL-la, IL-1j0, IL-6, and TNF-a was found to depend on the presence of T lymphocytes, because of the failure of purified monocytes to produce significant amounts of these cytokines in response to ETs. PBMC elicited large amounts of these cytokines, as well as IL-8 and TNF-j, with an optimal release after 48 to 96 h. The most abundant cytokine produced in response to ETA was IL-8. In contrast to the superantigens ETA and ETC, LPS and heat-killed streptococci stimulated the production of significant amounts of IL-la, IL-1,, IL-6, and TNF-a, with optimal production after 24 to 48 h in monocytes, indicating no significant involvement of T cells in the process. ETs, but neither LPS nor streptococci, were potent inducers of TNF-0 in PBMC. This study outlines the differences in the pathophysiological features of shock evoked by endotoxins and superantigens during infection by gram-negative bacteria and group A streptococci, respectively. The production of TNF-a was a common pathway for LPS, streptococcal cells, and ETs, although cell requirements and kinetics of cytokine release were different.

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Section: Methodsmentioning

confidence: 99%

Comparative study of cytokine release by human peripheral blood mononuclear cells stimulated with Streptococcus pyogenes superantigenic erythrogenic toxins, heat-killed streptococci, and lipopolysaccharide

et al. 1994

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“…An adequate purification scheme for erythrogenic toxin type C (ETC) is described in this paper. It enabled us, contrary to other already published procedures according to Schlievert et al [26] and Ozegowski et al [21], to obtain highly purified ETC practically in one step and diminish the influence of dephosphorylating activities.…”

Section: Discussionmentioning

confidence: 85%

“…Southern blot hybridization revealed that the strains C 203 S and NY 5 have the genes for the erythrogenic toxins type A, B and C and were shown to produce ETA and ETC [6,21], the strain ' Manfredo' carries the gene for ETC but not for ETA.…”

Section: Strainsmentioning

confidence: 99%

Streptococcal erythrogenic toxin type C is not a phosphorylated protein. Description of two different purification procedures and investigation of its phosphorylation state

Ozegowski¹,

Wollweber

Schmidt³

et al. 1994

FEMS Immunol Med Microbiol

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Erythrogenic toxin type C (ETC) from different streptococcal group A strains was successively purified by absorption on phenylsepharose, acidic dialysis of the eluate at 40% saturated ammonium sulphate solution, CM-Sepharose chromatography, finally by immunoaffinity chromatography on monoclonal antibodies. Second, after growing of bacteria in the presence of [32P]orthophosphate to phosphorylate ETC, the ETC was purified with phenylsepharose following immunoaffinity chromatography. The occurrence of phosphoamino acids in the purified ETC was investigated by an immunoassay. No phosphoamino acids could be detected in the ETC molecule. Also after radiolabelling with 32P it was not possible to demonstrate a radioactive signal. The treatment with alkaline phosphatase has no influence on the mitogenicity or position of ETC in isoelectric focusing. The results obtained led to the conclusion that in contrast to the literature, ETC is not a phosphorylated protein.

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“…Biological active fractions was collected and concentrated by sucrose the protein concentration was determined by [12] ( Table-1). Purification with Sephadex G-100 was used by [16,17,18] they found their was no effect of this treatment on superantigen activity. Determination of molecular weight by SDS electrophoresis apparent that (Spe C) have 24.000 Da while [11] refer it have 21.000 Da by using high speed sedimention equilibrium menisens depletion method and [16] estimate it 24.324 Da depending on calculation of amino acid which formed it [18] refer that (SPe C) have 24 Da with SDS polyacryl amid electrophorysis (Fig.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of Streptococcus pyogenes superantigen (Spe-C)

Al-Mudhafter¹,

Hassan²,

Saleem³

et al. 2011

Baghdad Sci.J

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From 144 specimens of tonsillitis which were collected from patient, (children of 3 -12 year olds) there were 70 isolates beta hemolytic and 28 isolates were identified as S. pyogenes. Sensitivity of S. pyogenes isolates to antibiotics was tested, all isolates were sensitive to amoxicillin and cephaloxia while higher resistant were to erythromycin. One isolate whiche was 100 A had a stable characteristics and produce pyrogenic toxin was chosen for study and it was purified and characterized from the cell free supernatant of S. pyrogenes strain.

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Isolierung und Charakterisierung von erythrogenen Toxinen VIL Untersuchung des von Streptococcus pyogenes gebildeten erythrogenen Toxins Typ C

Cited by 6 publications

References 28 publications

Comparative study of cytokine release by human peripheral blood mononuclear cells stimulated with Streptococcus pyogenes superantigenic erythrogenic toxins, heat-killed streptococci, and lipopolysaccharide

Comparative study of cytokine release by human peripheral blood mononuclear cells stimulated with Streptococcus pyogenes superantigenic erythrogenic toxins, heat-killed streptococci, and lipopolysaccharide

Streptococcal erythrogenic toxin type C is not a phosphorylated protein. Description of two different purification procedures and investigation of its phosphorylation state

Purification and characterization of Streptococcus pyogenes superantigen (Spe-C)

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