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Updated: Aug 16, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
The toxin-antitoxin system of the streptococcal plasmid pSM19035
Urszula Zielenkiewicz1, Piotr Ceglowski
1Department of Microbial Biochemistry, Institute of Biochemistry and Biophysics of the Polish Academy of Sciences, 02-106 Warsaw, Poland. ulazet@ibb.waw.pl
Abstract:
pSM19035 of the pathogenic bacterium Streptococcus pyogenes is a low-copy-number plasmid carrying erythromycin resistance, stably maintained in a broad range of gram-positive bacteria. We show here that the omega-epsilon-zeta operon of this plasmid constitutes a novel proteic plasmid addiction system in which the epsilon and zeta genes encode an antitoxin and toxin, respectively, while omega plays an autoregulatory function. Expression of toxin Zeta is bactericidal for the gram-positive Bacillus subtilis and bacteriostatic for the gram-negative Escherichia coli. The toxic effects of zeta gene expression in both bacterial species are counteracted by proper expression of epsilon. The epsilon-zeta toxin-antitoxin cassette stabilizes plasmids in E. coli less efficiently than in B. subtilis.
Insights
Streptococcus pyogenes plasmid pSM19035 utilizes a novel omega-epsilon-zeta operon for stable maintenance. This system features an antitoxin (epsilon) and toxin (zeta), providing plasmid addiction and stability in various bacteria.
Area of Science:
- Microbiology
- Bacterial Genetics
- Molecular Biology
Background:
- Streptococcus pyogenes harbors the pSM19035 plasmid, a low-copy-number element conferring erythromycin resistance.
- Plasmid stability is crucial for bacterial genetics and antibiotic resistance dissemination.
- Novel plasmid maintenance systems are essential for understanding bacterial evolution and control.
Purpose of the Study:
- To elucidate the function of the omega-epsilon-zeta operon in the pSM19035 plasmid.
- To characterize the novel proteic plasmid addiction system.
- To investigate the differential effects of the toxin-antitoxin system in various bacterial species.
Main Methods:
- Genetic analysis of the omega-epsilon-zeta operon.
- Expression studies of epsilon (antitoxin) and zeta (toxin) genes.
- Bactericidal and bacteriostatic assays in Bacillus subtilis and Escherichia coli.
Main Results:
- The omega-epsilon-zeta operon functions as a proteic plasmid addiction system.
- Epsilon acts as an antitoxin, neutralizing the bactericidal/bacteriostatic effects of toxin Zeta.
- The epsilon-zeta cassette demonstrated differential plasmid stabilization efficiency between B. subtilis and E. coli.
Conclusions:
- The omega-epsilon-zeta operon represents a novel toxin-antitoxin system for plasmid stabilization.
- This system contributes to the stable maintenance of pSM19035 in diverse bacterial hosts.
- Understanding such systems offers insights into plasmid biology and potential antimicrobial strategies.
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