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Modulation of Vibrio cholerae porin function by acidic pH
Guillaume Duret1, Valérie Simonet, Anne H Delcour
1Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5001, USA.
Channels (Austin, Tex.)
|August 12, 2008
Summary
Acidic conditions trigger pH-dependent closures in Vibrio cholerae OmpU porins, decreasing channel activity. OmpT porins remain unaffected, suggesting distinct roles in bacterial adaptation to host environments.
Area of Science:
- Microbiology
- Biophysics
- Structural Biology
Background:
- Gram-negative bacteria outer membranes utilize porins for nutrient transport.
- Vibrio cholerae, the cholera pathogen, faces environmental challenges like low pH during infection.
- OmpU and OmpT porins are implicated in V. cholerae's adaptation to host conditions.
Purpose of the Study:
- To investigate the impact of pH on the channel properties of OmpU and OmpT porins from Vibrio cholerae.
- To elucidate the role of these porins in bacterial adaptation to acidic environments.
Main Methods:
- Patch clamp electrophysiology.
- Planar lipid bilayer reconstitution assays.
- Analysis of porin channel gating and conductance at varying pH levels.
Main Results:
- OmpT activity remained stable across a pH range of 4 to 7.2.
- Acidic pH induced single-step closures in OmpU, increasing in duration and frequency as pH decreased.
- OmpU closures showed increased current size but unchanged overall trimeric conductance, suggesting coordinated gating.
Conclusions:
- OmpU exhibits pH-sensitive gating, contributing to V. cholerae's adaptation to acidic environments.
- The observed coordinated gating in OmpU suggests complex regulatory mechanisms within the porin trimer.
- Distinct pH-dependent behaviors of OmpU and OmpT highlight their specialized roles in V. cholerae pathogenesis.
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