The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States
The electrochemical gradients established across cell membranes are paramount for the execution of biological functions. Besides ion channels, other transporters, such as exogenous pore-forming toxins, may present ionic selectivity upon reconstitution in natural and artificial lipid membranes and co...
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MDPI AG
2021
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oai:doaj.org-article:ac5a60af50864157865740aefadd57b82021-11-25T18:20:11ZThe Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States10.3390/membranes111108972077-0375https://doaj.org/article/ac5a60af50864157865740aefadd57b82021-11-01T00:00:00Zhttps://www.mdpi.com/2077-0375/11/11/897https://doaj.org/toc/2077-0375The electrochemical gradients established across cell membranes are paramount for the execution of biological functions. Besides ion channels, other transporters, such as exogenous pore-forming toxins, may present ionic selectivity upon reconstitution in natural and artificial lipid membranes and contribute to the electrochemical gradients. In this context, we utilized electrophysiology approaches to assess the ionic selectivity of the pore-forming toxin lysenin reconstituted in planar bilayer lipid membranes. The membrane voltages were determined from the reversal potentials recorded upon channel exposure to asymmetrical ionic conditions, and the permeability ratios were calculated from the fit with the Goldman–Hodgkin–Katz equation. Our work shows that lysenin channels are ion-selective and the determined permeability coefficients are cation and anion-species dependent. We also exploited the unique property of lysenin channels to transition to a stable sub-conducting state upon exposure to calcium ions and assessed their subsequent change in ionic selectivity. The observed loss of selectivity was implemented in an electrical model describing the dependency of reversal potentials on calcium concentration. In conclusion, our work demonstrates that this pore-forming toxin presents ionic selectivity but this is adjusted by the particular conduction state of the channels.Andrew BogardPangaea W. FinnFulton McKinneyIlinca M. FlacauAviana R. SmithRosey WhitingDaniel FologeaMDPI AGarticlelyseninselectivitymembrane voltagesub-conducting channelsChemical technologyTP1-1185Chemical engineeringTP155-156ENMembranes, Vol 11, Iss 897, p 897 (2021) |
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lysenin selectivity membrane voltage sub-conducting channels Chemical technology TP1-1185 Chemical engineering TP155-156 |
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lysenin selectivity membrane voltage sub-conducting channels Chemical technology TP1-1185 Chemical engineering TP155-156 Andrew Bogard Pangaea W. Finn Fulton McKinney Ilinca M. Flacau Aviana R. Smith Rosey Whiting Daniel Fologea The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
description |
The electrochemical gradients established across cell membranes are paramount for the execution of biological functions. Besides ion channels, other transporters, such as exogenous pore-forming toxins, may present ionic selectivity upon reconstitution in natural and artificial lipid membranes and contribute to the electrochemical gradients. In this context, we utilized electrophysiology approaches to assess the ionic selectivity of the pore-forming toxin lysenin reconstituted in planar bilayer lipid membranes. The membrane voltages were determined from the reversal potentials recorded upon channel exposure to asymmetrical ionic conditions, and the permeability ratios were calculated from the fit with the Goldman–Hodgkin–Katz equation. Our work shows that lysenin channels are ion-selective and the determined permeability coefficients are cation and anion-species dependent. We also exploited the unique property of lysenin channels to transition to a stable sub-conducting state upon exposure to calcium ions and assessed their subsequent change in ionic selectivity. The observed loss of selectivity was implemented in an electrical model describing the dependency of reversal potentials on calcium concentration. In conclusion, our work demonstrates that this pore-forming toxin presents ionic selectivity but this is adjusted by the particular conduction state of the channels. |
format |
article |
author |
Andrew Bogard Pangaea W. Finn Fulton McKinney Ilinca M. Flacau Aviana R. Smith Rosey Whiting Daniel Fologea |
author_facet |
Andrew Bogard Pangaea W. Finn Fulton McKinney Ilinca M. Flacau Aviana R. Smith Rosey Whiting Daniel Fologea |
author_sort |
Andrew Bogard |
title |
The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
title_short |
The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
title_full |
The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
title_fullStr |
The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
title_full_unstemmed |
The Ionic Selectivity of Lysenin Channels in Open and Sub-Conducting States |
title_sort |
ionic selectivity of lysenin channels in open and sub-conducting states |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/ac5a60af50864157865740aefadd57b8 |
work_keys_str_mv |
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