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Pseudomonas toxin binds triton X-114 at low pH
1Institute for Cancer Research, Norwegian Radium Hospital, Oslo.
The Biochemical Journal
|August 1, 1987
Summary
Pseudomonas toxin binds Triton X-114 at low pH, indicating a conformational change. This interaction is enhanced by salt, suggesting a mechanism for toxin entry into host cells.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Pseudomonas toxins are critical virulence factors.
- Understanding toxin-host interactions is key to developing therapeutics.
Purpose of the Study:
- To investigate the binding properties of Pseudomonas toxin with Triton X-114.
- To elucidate the role of pH and salt concentration on toxin-membrane interactions.
Main Methods:
- Triton X-114 binding assays were performed.
- Experiments were conducted across a range of pH values.
- The effect of varying salt concentrations (NaCl, KCl, NaNO3) was assessed.
Main Results:
- Pseudomonas toxin exhibited significant binding to Triton X-114 below pH 5.0.
- Binding affinity increased at higher pH values in the presence of 0.14 M salt.
- Low pH appears to induce a conformational change facilitating membrane transport.
Conclusions:
- The study reveals pH-dependent conformational changes in Pseudomonas toxin.
- These changes are modulated by salt concentration, influencing membrane interaction.
- Findings suggest a mechanism for Pseudomonas toxin translocation into the cytosol.