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Analysis of Antimicrobial-Triggered Membrane Depolarization Using Voltage Sensitive Dyes
Open accessAbstract
The bacterial cytoplasmic membrane is a major inhibitory target for antimicrobial compounds. Commonly, although not exclusively, these compounds unfold their antimicrobial activity by disrupting the essential barrier function of the cell membrane. As a consequence, membrane permeability assays are central for mode of action studies analysing membrane-targeting antimicrobial compounds. The most frequently used in vivo methods detect changes in membrane permeability by following internalization of normally membrane impermeable and relatively large fluorescent dyes. Unfortunately, these assays are not sensitive to changes in membrane ion permeability which are sufficient to inhibit and kill bacteria by membrane depolarization. In this manuscript, we provide experimental advice how membrane potential, and its changes triggered by membrane-targeting antimicrobials can be accurately assessed in vivo. Optimized protocols are provided for both qualitative and quantitative kinetic measurements of membrane potential. At last, single cell analyses using voltage-sensitive dyes in combination with fluorescence microscopy are introduced and discussed.
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Cites
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704
Mechanisms of Antimicrobial Peptide Action and Resistance
Yeaman, M. R., & Yount, N. Y. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.2 · Cited by 3,001
Bacterial competition: surviving and thriving in the microbial jungle
Hibbing, M. E., Fuqua, C., Parsek, M. R., & Peterson, S. B. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2259 · Cited by 2,689
The toxic shock syndrome exotoxin structural gene is not detectably transmitted by a prophage
Kreiswirth, B. N., Löfdahl, S., Betley, M. J., O'Reilly, M., Schlievert, P. M., Bergdoll, M. S., & Novick, R. P. (1983) · Nature · doi:10.1038/305709a0 · Cited by 1,326
Oxidative Phosphorylation at the fin de siècle
Saraste, M. (1999) · Science · doi:10.1126/science.283.5407.1488 · Cited by 1,313
Ion channels enable electrical communication in bacterial communities
Prindle, A., Liu, J., Asally, M., Ly, S., Garcia-Ojalvo, J., & Süel, G. M. (2015) · Nature · doi:10.1038/nature15709 · Cited by 790
Stiefel, P., Schmidt-Emrich, S., Maniura-Weber, K., & Ren, Q. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0376-x · Cited by 710
Correlation of Daptomycin Bactericidal Activity and Membrane Depolarization in Staphylococcus aureus
Silverman, J. A., Perlmutter, N. G., & Shapiro, H. M. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.8.2538-2544.2003 · Cited by 656
Antimicrobial peptides: an overview of a promising class of therapeutics
Giuliani, A., Pirri, G., & Nicoletto, S. (2007) · Open Life Sciences · doi:10.2478/s11535-007-0010-5 · Cited by 606
Bacterial viability and antibiotic susceptibility testing with SYTOX green nucleic acid stain
Roth, B. L., Poot, M., Yue, S. T., & Millard, P. J. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.6.2421-2431.1997 · Cited by 579
Dye Indicators of Membrane Potential
Waggoner, A. S. (1979) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.08.060179.000403 · Cited by 564
Membrane potential is important for bacterial cell division
Strahl, H., & Hamoen, L. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005485107 · Cited by 553
Self-citationAntimicrobial peptides: General overview and clinical implications in human health and disease
Guaní-Guerra, E., Santos-Mendoza, T., Lugo-Reyes, S. O., & Terán, L. M. (2010) · Clinical Immunology · doi:10.1016/j.clim.2009.12.004 · Cited by 549
Ehrenberg, B., Montana, V., Wei, M. D., Wuskell, J. P., & Loew, L. M. (1988) · Biophysical Journal · doi:10.1016/s0006-3495(88)83158-8 · Cited by 524
Antimicrobial Peptides: Successes, Challenges and Unanswered Questions
Wimley, W. C., & Hristova, K. (2011) · The Journal of Membrane Biology · doi:10.1007/s00232-011-9343-0 · Cited by 495
Riedl, S., Zweytick, D., & Lohner, K. (2011) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2011.09.004 · Cited by 405
Barbe, V., Cruveiller, S., Kunst, F., Lenoble, P., Meurice, G., Sekowska, A., Vallenet, D., Wang, T., Moszer, I., Médigue, C., et al. (2009) · Microbiology · doi:10.1099/mic.0.027839-0 · Cited by 381
The gramicidin ion channel: A model membrane protein
Kelkar, D. A., & Chattopadhyay, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.011 · Cited by 380
Marston, A. L., Thomaides, H. B., Edwards, D. H., Sharpe, M. E., & Errington, J. (1998) · Genes & Development · doi:10.1101/gad.12.21.3419 · Cited by 377
Optical probes of membrane potential
Waggoner, A. (1976) · The Journal of Membrane Biology · doi:10.1007/bf01869143 · Cited by 358
Nonejuie, P., Burkart, M., Pogliano, K., & Pogliano, J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311066110 · Cited by 341
Spatial control of bacterial division-site placement
Rothfield, L., Taghbalout, A., & Shih, Y.-L. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1290 · Cited by 305
The effects of osmotic upshock on the intracellular solute pools of Bacillus subtilis
Whatmore, A. M., Chudek, J. A., & Reed, R. H. (1990) · Journal of General Microbiology · doi:10.1099/00221287-136-12-2527 · Cited by 284
Real-time attack on single Escherichia coli cells by the human antimicrobial peptide LL-37
Sochacki, K. A., Barns, K. J., Bucki, R., & Weisshaar, J. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101130108 · Cited by 267
The actin homologue MreB organizes the bacterial cell membrane
Strahl, H., Bürmann, F., & Hamoen, L. W. (2014) · Nature Communications · doi:10.1038/ncomms4442 · Cited by 238
Self-citationThe mode of antifungal action of plant, insect and human defensins
Aerts, A. M., François, I. E. J. A., Cammue, B. P. A., & Thevissen, K. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8035-0 · Cited by 209
Comparative measurements of membrane potentials with microelectrodes and voltage-sensitive dyes
Bräuner, T., Hülser, D. F., & Strasser, R. J. (1984) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(84)90535-2 · Cited by 203
Epps, D. E., Wolfe, M. L., & Groppi, V. (1994) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(94)90035-3 · Cited by 198
Indole prevents Escherichia coli cell division by modulating membrane potential
Chimerel, C., Field, C. M., Piñero-Fernandez, S., Keyser, U. F., & Summers, D. K. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.02.022 · Cited by 169
Regulation of cell wall morphogenesis in Bacillus subtilis by recruitment of PBP1 to the MreB helix
Kawai, Y., Daniel, R. A., & Errington, J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06601.x · Cited by 146
de Jong, I. G., Beilharz, K., Kuipers, O. P., & Veening, J. (2011) · Journal of Visualized Experiments · doi:10.3791/3145 · Cited by 143
Zhang, W., Yang, F. K., Han, Y., Gaikwad, R. M., Leonenko, Z., & Zhao, B. (2013) · Biomacromolecules · doi:10.1021/bm3015768 · Cited by 120
Vischer, N. O. E., Verheul, J., Postma, M., van Saparoea, H. B. V. D. B., Galli, E., Natale, P., Gerdes, K., Luirink, J., Vollmer, W., Vicente, M., et al. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00586 · Cited by 115
Novel Inhibitors of Bacterial Cytokinesis Identified by a Cell-based Antibiotic Screening Assay
Stokes, N. R., Sievers, J., Barker, S., Bennett, J. M., Brown, D. R., Collins, I., Errington, V. M., Foulger, D., Hall, M. J., Halsey, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506741200 · Cited by 111
Deciphering the Mode of Action of the Synthetic Antimicrobial Peptide Bac8c
Spindler, E. C., Hale, J. D. F., Giddings, T. H., Hancock, R. E. W., & Gill, R. T. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01053-10 · Cited by 105
Wenzel, M., Kohl, B., Münch, D., Raatschen, N., Albada, B., Hamoen, L. W., Metzler‐Nolte, N., Sahl, H., & Bandow, J. E. (2012) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01380-12 · Cited by 101
Self-citationReal-time attack of LL-37 on single Bacillus subtilis cells
Barns, K. J., & Weisshaar, J. C. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.02.011 · Cited by 85
Chapter 4 Cell Membrane Potential Analysis
Shapiro, H. M. (1990) · Methods in cell biology · doi:10.1016/s0091-679x(08)60509-9 · Cited by 83
Transmembrane protein sorting driven by membrane curvature
Strahl, H., Ronneau, S., Gonzalez, B. I., Klütsch, D., Schaffner-Barbero, C., & Hamoen, L. W. (2015) · Nature Communications · doi:10.1038/ncomms9728 · Cited by 72
Self-citationDCAP: A Broad-Spectrum Antibiotic That Targets the Cytoplasmic Membrane of Bacteria
Eun, Y.-J., Foss, M. H., Kiekebusch, D., Pauw, D. A., Westler, W. M., Thanbichler, M. R., & Weibel, D. B. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302542j · Cited by 66
Inhibitors of bacterial tubulin target bacterial membranes in vivo
Foss, M. H., Eun, Y.-J., Grove, C. I., Pauw, D. A., Sorto, N. A., Rensvold, J. W., Pagliarini, D. J., Shaw, J. T., & Weibel, D. B. (2012) · MedChemComm · doi:10.1039/c2md20127e · Cited by 52
Isolation and characterization of topological specificity mutants of minD in Bacillus subtilis
Karoui, M. E., & Errington, J. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02710.x · Cited by 33
Section 8 - Molecular tools to assess microbial activities
Breeuwer, P., & Abee, T. (2008) · Springer eBooks · doi:10.1007/978-1-4020-2177-0_8 · Cited by 16
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Müller, A., Wenzel, M., Strahl, H., Grein, F., Saaki, T. N. V., Kohl, B., Siersma, T., Bandow, J. E., Sahl, H.-G., Schneider, T., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611173113 · Cited by 425
Self-citationMode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms
Benfield, A. H., & Henriques, S. T. (2020) · Frontiers in Medical Technology · doi:10.3389/fmedt.2020.610997 · Cited by 367
Csx28 is a membrane pore that enhances CRISPR-Cas13b–dependent antiphage defense
VanderWal, A. R., Park, J.-U., Polevoda, B., Nicosia, J. K., Molina Vargas, A. M., Kellogg, E. H., & O’Connell, M. R. (2023) · Science · doi:10.1126/science.abm1184 · Cited by 55
A hyperpromiscuous antitoxin protein domain for the neutralization of diverse toxin domains
Kurata, T., Saha, C. K., Buttress, J. A., Mets, T., Brodiazhenko, T., Turnbull, K. J., Awoyomi, O. F., Oliveira, S. R. A., Jimmy, S., Ernits, K., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2102212119 · Cited by 38
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Metadata
- Authors
- te Winkel, J. D., Gray, D. A., Seistrup, K. H., Hamoen, L. W., & Strahl, H.
- Venue
- Frontiers in Cell and Developmental Biology
- Publisher
- Frontiers Media SA
- Published
- 2016-04-13
- Volume
- 4
- Pages
- 29-29
- ISSN
- 2296-634X (ISSN-L)
- OpenAlex
- W2341866225
- Cited by
- 326
- References
- 44
- FWCI
- 7.13
- Type
- journal article
- Language
- en
- Open access
- gold
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