scholarly journals Bacterial Immunotherapy-Antitumoral Potential of the Streptococcal Toxin Streptolysin S-

10.5772/28730 ◽  
2012 ◽  
Author(s):  
Claudia Maletzki ◽  
Bernd Kreikemeyer ◽  
Peggy Bodammer ◽  
Joerg Emmrich ◽  
Michael Linnebacher
Keyword(s):  
Streptolysin S

scholarly journals ON THE FORMATION OF STREPTOLYSIN S BY HEMOLYTIC STREPTOCOCCI ACTING ON TUMOR CELLS

1958 ◽  
Vol 2 (1) ◽  
pp. 23-28 ◽  
Author(s):  
Saburo Koshimura ◽  
Ryusaku Shimizu ◽  
Tetsuo Masusaki ◽  
Takanari Ohta ◽  
Gengo Kishi
Keyword(s):  
Tumor Cells ◽  
Streptolysin S

Influence of streptolysin S from Streptococcus pyogenes on some functions of lymphocyte membrane

Toxicon ◽  
1981 ◽  
Vol 19 (1) ◽  
pp. 33-39 ◽  
Author(s):  
W. Hryniewicz ◽  
W. Roszkowski ◽  
S. Lipski ◽  
J. Jeljaszewicz
Keyword(s):  
Streptococcus Pyogenes ◽  
Lymphocyte Membrane ◽  
Streptolysin S

scholarly journals Discovery of genes encoding a Streptolysin S-like toxin biosynthetic cluster in a select highly pathogenic methicillin resistant Staphylococcus aureus JKD6159 strain

2019 ◽  
Author(s):  
Trevor Kane ◽  
Katelyn E. Carothers ◽  
Yunjuan Bao ◽  
Won-Sik Yeo ◽  
Taeok Bae ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Gene Cluster ◽  
Virulence Factor ◽  
Gene Organization ◽  
Biosynthetic Gene ◽  
Bacterial Gene ◽  
Methicillin Resistant ◽  
Streptolysin S

AbstractBackgroundStaphylococcus aureus (S. aureus) is a major human pathogen owing to its arsenal of virulence factors, as well as its acquisition of multi-antibiotic resistance. Here we report the identification of a Streptolysin S (SLS) like biosynthetic gene cluster in a highly virulent community-acquired methicillin resistant S. aureus (MRSA) isolate, JKD6159. Examination of the SLS-like gene cluster in JKD6159 shows significant homology and gene organization to the SLS-associated biosynthetic gene (sag) cluster responsible for the production of the major hemolysin SLS in Group A Streptococcus.ResultsWe took a comprehensive approach to elucidating the putative role of the sag gene cluster in JKD6159 by constructing a mutant in which one of the biosynthesis genes (sagB homologue) was deleted in the parent JKD6159 strain. Assays to evaluate bacterial gene regulation, biofilm formation, antimicrobial activity, as well as complete host cell response profile and comparative in vivo infections in Balb/Cj mice were conducted.ConclusionsAlthough no significant phenotypic changes were observed in our assays, we postulate that the SLS-like toxin produced by this strain of S. aureus may be a highly specialized virulence factor utilized in specific environments for selective advantage; studies to better understand the role of this newly discovered virulence factor in S. aureus warrant further investigation.

scholarly journals Streptolysin S Formation by Streptococcal Ghosts

1960 ◽  
Vol 36 (3) ◽  
pp. 141-144
Author(s):  
Sadako SUGAI ◽  
Fujio EGAMI
Keyword(s):  
Streptolysin S

BIOCHEMICAL STUDIES ON STREPTOLYSIN S.

1956 ◽  
Vol 43 (6) ◽  
pp. 827-832 ◽  
Author(s):  
KENTARO TANAKA ◽  
SHIZUE MAEKAWA ◽  
TAKAYOSHI HAYASHI ◽  
YOSHIRO KUROIWA
Keyword(s):  
Streptolysin S ◽  
Biochemical Studies

scholarly journals OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI

1965 ◽  
Vol 121 (4) ◽  
pp. 633-645 ◽  
Author(s):  
Isaac Ginsburg ◽  
Zvi Bentwich ◽  
T. N. Harris
Keyword(s):  
Trypan Blue ◽  
Animal Species ◽  
Ph Dependence ◽  
Optimal Production ◽  
Streptolysin S ◽  
Hemolytic Effect ◽  
Group A ◽  
Relationship Of ◽  
The Relationship ◽  
Maximal Production

The relationship of the streptococcal hemolysin which is recognized on incubation of RBC with streptococcal cells (cell-bound hemolysin, CBH), to RNA hemolysin, a representative of oxygen-stable hemolysin (streptolysin S) has been studied. A number of similarities have been found in the conditions for optimal production of each of these hemolysins, a requirement for cysteine, Mg++, and glucose; maximal production by streptococci in the stationary phase; similar curves of pH-dependence. In both systems, the production of hemolysin was inhibited by certain antibiotics, by ultraviolet irradiation, and by sonic disruption and was absent in the same streptococcal mutant strain. The hemolytic activity of both systems was inhibited by lecithin, trypan blue, and papain. Similarities were also found in relative susceptibilities to the two hemolytic systems of erythrocytes of a number of animal species. These data support a suggestion advanced in an earlier study that a streptococcal hemolytic moiety, which can be induced by, and carried on, a number of diverse agents to comprise the group of oxygen-stable hemolysins, serves, in its original attachment to a component of the streptococcal cell, to produce the hemolytic effect recognized as the cell-bound hemolysin.

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