Literature DB >> 9228742

Function and modulation of bacterial porins: insights from electrophysiology.

A H Delcour1.   

Abstract

Electrophysiological techniques provide a wealth of information regarding the molecular mechanisms that underlie the function and modulation of ion channels. They have revealed that bacterial porins do not behave as static, permanently open pores but display a much more complex and dynamic behavior than anticipated from non-electrophysiological studies. The channels switch between short-lived open and closed conformations (gating activity), and can also remain in an inactivated, non-ion conducting state for prolonged periods of time. Thus the role of porins is not limited to that of a molecular filter, but is extended to the control of outer membrane permeability through the regulation of their activity. Electrophysiological studies have indeed demonstrated that both gating and inactivation are modulated by a variety of physical and chemical parameters and are highly cooperative phenomena, often involving numerous channels working in concert. Cooperativity acts as an amplification mechanism that grants a large population of porins, such as found in the outer membrane, with sensitivity to modulation by external or internal factors. By conferring permeability properties to the outer membrane, porins play a crucial role in the bacterium's antibiotic susceptibility and survival in various environmental conditions. The detailed information that electrophysiology only can provide on porin function and modulation promises to yield a more accurate description of how porin properties can be used by cells to adapt to a changing environment, and to offer mechanisms that might optimize the drug sensitivity of the microorganism.

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Year:  1997        PMID: 9228742     DOI: 10.1111/j.1574-6968.1997.tb12558.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  22 in total

1.  Alteration of pore properties of Escherichia coli OmpF induced by mutation of key residues in anti-loop 3 region.

Authors:  Jérôme Bredin; Nathalie Saint; Monique Malléa; Emmanuelle Dé; Gérard Molle; Jean-Marie Pagès; Valérie Simonet
Journal:  Biochem J       Date:  2002-05-01       Impact factor: 3.857

2.  Cadaverine inhibition of porin plays a role in cell survival at acidic pH.

Authors:  Hrissi Samartzidou; Mahsa Mehrazin; Zhaohui Xu; Michael J Benedik; Anne H Delcour
Journal:  J Bacteriol       Date:  2003-01       Impact factor: 3.490

Review 3.  Molecular basis of bacterial outer membrane permeability revisited.

Authors:  Hiroshi Nikaido
Journal:  Microbiol Mol Biol Rev       Date:  2003-12       Impact factor: 11.056

4.  A fast in silico simulation of ion flux through the large-pore channel proteins.

Authors:  Sharron Bransburg-Zabary; Esther Nachliel; Menachem Gutman
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

5.  The influence of amino acid protonation states on molecular dynamics simulations of the bacterial porin OmpF.

Authors:  Sameer Varma; See-Wing Chiu; Eric Jakobsson
Journal:  Biophys J       Date:  2005-09-23       Impact factor: 4.033

6.  Channel activity of OmpF monitored in nano-BLMs.

Authors:  Eva K Schmitt; Maarten Vrouenraets; Claudia Steinem
Journal:  Biophys J       Date:  2006-06-16       Impact factor: 4.033

7.  Prediction of antigenically active regions in the OmpF-like porin of Yersinia pseudotuberculosis.

Authors:  D V Antonets; A Y Bakulina; O Y Portnyagina; O V Sidorova; O D Novikova; A Z Maksyutov
Journal:  Dokl Biochem Biophys       Date:  2007 May-Jun       Impact factor: 0.788

Review 8.  Microdermatology: cell surface in the interaction of microbes with the external world.

Authors:  H Nikaido
Journal:  J Bacteriol       Date:  1999-01       Impact factor: 3.490

9.  Single-channel measurements of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli.

Authors:  Janhavi Giri; John M Tang; Christophe Wirth; Caroline M Peneff; Bob Eisenberg
Journal:  Eur Biophys J       Date:  2012-01-13       Impact factor: 1.733

10.  Structures formed by a cell membrane-associated arabinogalactan-protein on graphite or mica alone and with Yariv phenylglycosides.

Authors:  Li Hong Zhou; Renate A Weizbauer; Srikanth Singamaneni; Feng Xu; Guy M Genin; Barbara G Pickard
Journal:  Ann Bot       Date:  2014-08-27       Impact factor: 4.357

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