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Updated: Aug 18, 2026

Invasion of Human Cells by a Bacterial Pathogen
Published on: March 21, 2011
Interaction of streptolysin O from Streptococcus pyogenes and theta-toxin from Clostridium perfringens with human
Abstract:
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.
Insights
This study compared membrane damage from streptolysin O and theta-toxin. Results show theta-toxin
Area of Science:
- Microbiology
- Toxicology
- Cell Biology
Background:
- Streptolysin O (from Streptococcus pyogenes) and theta-toxin (from Clostridium perfringens) are bacterial toxins.
- Both toxins are known to damage cell membranes.
- Thiol-activated, cholesterol-inactivated bacterial toxins are often considered functionally similar.
Purpose of the Study:
- To compare the membrane-damaging properties of streptolysin O and theta-toxin on human diploid embryonic lung fibroblasts.
- To investigate potential differences in the mechanisms of action between these two toxins.
- To challenge the prevailing concept of functional similarity among thiol-activated bacterial toxins.
Main Methods:
- Comparison of cytolytic activity on human diploid lung fibroblasts and sheep erythrocytes.
- Assessment of toxin binding to fibroblast membranes.
- Evaluation of toxin activity at low temperatures (0°C) and effects on membrane repair and amino acid influx.
Main Results:
- Streptolysin O's activity aligns with a mechanism involving one fixation and one lytic site.
- Significant differences were observed in cytolytic activity, membrane binding, low-temperature activity, membrane repair, and amino acid influx between the two toxins.
- Theta-toxin's membrane-damaging activity was found to differ from that of streptolysin O.
Conclusions:
- The mechanism of membrane damage induced by theta-toxin is distinct from that of streptolysin O.
- These findings question the established notion that all thiol-activated, cholesterol-inactivated bacterial toxins share similar structural and functional characteristics.
- Highlights the need for nuanced understanding of toxin-host interactions.
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