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Published on: February 17, 2014
WLIP and tolaasin I, lipodepsipeptides from Pseudomonas reactans and Pseudomonas tolaasii, permeabilise model
M Coraiola1, P Lo Cantore, S Lazzaroni
1ITC-CNR Istituto di Biofisica, via Sommarive 18, I-38050 Povo (Trento), Italy. manucora@itc.it
Abstract:
The activity of the White Line Inducing Principle (WLIP) and tolaasin I, produced by virulent strains of Pseudomonas reactans and Pseudomonas tolaasii, respectively, was comparatively evaluated on lipid membranes. Both lipodepsipeptides were able to induce the release of calcein from large unilamellar vesicles. Their activity was dependent on the toxin concentration and liposome composition and in particular it increased with the sphingomyelin content of the membrane. Studies of dynamic light scattering suggested a detergent-like activity for WLIP at high concentration (> 27 microM). This effect was not detected for tolaasin I at the concentrations tested (< 28 microM). Differences were also observed in lipodepsipeptides secondary structure. In particular, the conformation of the smaller WLIP changed slightly when it passed from the buffer solution to the lipid environment. On the contrary, we observed a valuable increment in the helical content of tolaasin I which was inserted in the membrane core and oriented parallel to the lipid acyl chains.
Insights
White Line Inducing Principle (WLIP) and tolaasin I toxins both disrupt lipid membranes, with activity influenced by sphingomyelin content. WLIP exhibits detergent-like effects at high concentrations, unlike tolaasin I.
Area of Science:
- Biochemistry
- Membrane Biophysics
- Microbial Toxinology
Background:
- Pseudomonas reactans and Pseudomonas tolaasii produce virulent lipodepsipeptides.
- White Line Inducing Principle (WLIP) and tolaasin I are key toxins studied for their membrane interactions.
Purpose of the Study:
- To comparatively evaluate the activity of WLIP and tolaasin I on lipid membranes.
- To investigate the influence of liposome composition and toxin concentration on membrane disruption.
Main Methods:
- Large unilamellar vesicles (LUVs) were used to assess calcein release.
- Dynamic light scattering (DLS) was employed to study toxin-induced membrane changes.
- Spectroscopic methods were utilized to analyze secondary structures of the lipodepsipeptides.
Main Results:
- Both WLIP and tolaasin I induced calcein release from LUVs in a concentration-dependent manner.
- Membrane sphingomyelin content significantly enhanced the activity of both toxins.
- WLIP displayed detergent-like activity at >27 microM, while tolaasin I did not at <28 microM.
- Conformational changes were observed for both toxins upon interaction with lipid membranes, with tolaasin I showing increased helical content.
Conclusions:
- WLIP and tolaasin I exhibit distinct mechanisms of membrane interaction and structural responses.
- Lipid membrane composition, particularly sphingomyelin, plays a crucial role in modulating toxin activity.
- Understanding these differences is vital for elucidating bacterial pathogenesis and developing targeted interventions.
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