Interaction of streptolysin O from Streptococcus pyogenes and theta-toxin from Clostridium perfringens with human fibroblasts.
The membrane-damaging properties on human diploid embryonic lung fibroblasts of streptolysin O (from Streptococcus pyogenes) and theta-toxin (from Clostridium perfringens) were compared. The results are consistent with the suggested mechanism for hemolysis by streptolysin O involving one fixation site and one lytic site of this cytolysin. However, the membrane-damaging activity of the two toxins differed with respect to (i) relative cytolytic activity on human diploid lung fibroblasts compared with that on sheep erythrocytes, (ii) binding to the fibroblast membrane, (iii) activity at 0 degrees C, (iv) membrane repair after more than 30 min, and (v) effect on influx of amino acids. It is concluded that the mechanism of membrane damage caused by theta-toxin differs from that of cytoplasmic membrane. These results question the current concept that all thiol-activated, cholesterol-inactivated bacterial toxins are similar both structurally and functionally.
D001665:Binding Sites; D001692:Biological Transport; D002413:Cations, Divalent; D002470:Cell Survival; D003016:Clostridium perfringens; D004306:Dose-Response Relationship, Immunologic; D005347:Fibroblasts / Q000382:microbiology; D006801:Humans; D013297:Streptococcus pyogenes; D013301:Streptolysins; D013696:Temperature; D013997:Time Factors; D014118:Toxins, Biological
D002413:Cations, Divalent; D013301:Streptolysins; D014118:Toxins, Biological