Abstract
Time-resolved atomic force microscopy (AFM) offers countless new modes by which to study bacterial cell physiology on relevant time scales, from mere milliseconds to hours and days on end. In addition, time-lapse AFM acts as a complementary tool to optical fluorescence microscopy (OFM), for which the combination offers a correlative link between the physical manifestation of bacterial phenotypes and molecular mechanisms obeying those principles. Herein we describe the essential materials and methods necessary for conducting time-resolved AFM and dual AFM/OFM experiments on bacteria.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Ando T, Uchihashi T, Scheuring S (2014) Filming biomolecular processes by high-speed atomic force microscopy. Chem Rev 114(6):3120–3188. https://doi.org/10.1021/cr4003837
Eskandarian HA et al (2017) Division site selection linked to inherited cell surface wave troughs in mycobacteria. Nat Microbiol 2(9):17094. https://doi.org/10.1038/Nmicrobiol.2017.94
Fantner GE et al (2010) Kinetics of antimicrobial peptide activity measured on individual bacterial cells using high-speed atomic force microscopy. Nat Nanotechnol 5(4):280–285. https://doi.org/10.1038/nnano.2010.29
Watanabe H et al (2013) Wide-area scanner for high-speed atomic force microscopy. Rev Sci Instrum 84(5):053702. https://doi.org/10.1063/1.4803449
Yamashita H et al (2012) Single-molecule imaging on living bacterial cell surface by high-speed AFM. J Mol Biol 422(2):300–309. https://doi.org/10.1016/j.jmb.2012.05.018
Suo Z et al (2009) Antibody selection for immobilizing living bacteria. Anal Chem 81(18):7571–7578. https://doi.org/10.1021/ac9014484
Meyer RL et al (2010) Immobilisation of living bacteria for AFM imaging under physiological conditions. Ultramicroscopy 110(11):1349–1357. https://doi.org/10.1016/j.ultramic.2010.06.010
Dufrene YF (2008) Atomic force microscopy and chemical force microscopy of microbial cells. Nat Protoc 3(7):1132–1138. https://doi.org/10.1038/nprot.2008.101
Butt HJ, Downing KH, Hansma PK (1990) Imaging the membrane protein bacteriorhodopsin with the atomic force microscope. Biophys J 58(6):1473–1480. https://doi.org/10.1016/S0006-3495(90)82492-9
Camesano TA, Natan MJ, Logan BE (2000) Observation of changes in bacterial cell morphology using tapping mode atomic force microscopy. Langmuir 16(10):4563–4572. https://doi.org/10.1021/La990805o
Hoh JH et al (1993) Structure of the extracellular surface of the gap junction by atomic force microscopy. Biophys J 65(1):149–163. https://doi.org/10.1016/S0006-3495(93)81074-9
Velegol SB, Logan BE (2002) Contributions of bacterial surface polymers, electrostatics, and cell elasticity to the shape of AFM force curves. Langmuir 18(13):5256–5262. https://doi.org/10.1021/La011818g
Colville K et al (2010) Effects of poly(L-lysine) substrates on attached Escherichia coli bacteria. Langmuir 26(4):2639–2644. https://doi.org/10.1021/la902826n
Liu Y, Strauss J, Camesano TA (2008) Adhesion forces between Staphylococcus epidermidis and surfaces bearing self-assembled monolayers in the presence of model proteins. Biomaterials 29(33):4374–4382. https://doi.org/10.1016/j.biomaterials.2008.07.044
Micic M et al (2004) Correlated atomic force microscopy and fluorescence lifetime imaging of live bacterial cells. Colloids Surf B Biointerfaces 34(4):205–212. https://doi.org/10.1016/j.colsurfb.2003.10.020
Hett EC, Rubin EJ (2008) Bacterial growth and cell division: a mycobacterial perspective. Microbiol Mol Biol Rev 72(1):126–156, table of contents. https://doi.org/10.1128/MMBR.00028-07
Wakamoto Y et al (2013) Dynamic persistence of antibiotic-stressed mycobacteria. Science 339(6115):91–95. https://doi.org/10.1126/science.1229858
Mendez-Vilas A, Gallardo-Moreno AM, Gonzalez-Martin ML (2007) Atomic force microscopy of mechanically trapped bacterial cells. Microsc Microanal 13(1):55–64. https://doi.org/10.1017/S1431927607070043
Mendez-Vilas A et al (2008) AFM probing in aqueous environment of Staphylococcus epidermidis cells naturally immobilised on glass: physico-chemistry behind the successful immobilisation. Colloids Surf B Biointerfaces 63(1):101–109. https://doi.org/10.1016/j.colsurfb.2007.11.011
Fritz M et al (1994) Visualization and identification of intracellular structures by force modulation microscopy and drug-induced degradation. J Vac Sci Technol B 12(3):1526–1529. https://doi.org/10.1116/1.587278
Ando T et al (2001) A high-speed atomic force microscope for studying biological macromolecules. Proc Natl Acad Sci U S A 98(22):12468–12472. https://doi.org/10.1073/pnas.211400898
Casuso I et al (2012) Characterization of the motion of membrane proteins using high-speed atomic force microscopy. Nat Nanotechnol 7(8):525–529. https://doi.org/10.1038/nnano.2012.109
Kindt JH et al (2002) Atomic force microscope detector drift compensation by correlation of similar traces acquired at different setpoints. Rev Sci Instrum 73(6):2305–2307. https://doi.org/10.1063/1.1475352
Fantner GE et al (2005) Data acquisition system for high speed atomic force microscopy. Rev Sci Instrum 76(2):026118. https://doi.org/10.1063/1.1850651
Fantner GE et al (2006) Components for high speed atomic force microscopy. Ultramicroscopy 106(8–9):881–887. https://doi.org/10.1016/j.ultramic.2006.01.015
Nievergelt AP, et al. (2017) Components for high-speed atomic force microscopy optimized for low phase-lag. 2017 I.E. International Conference on Advanced Intelligent Mechatronics (AIM). p 731–736. doi:https://doi.org/10.1109/AIM.2017.8014104
Hu DH et al (2003) Correlated topographic and spectroscopic imaging beyond diffraction limit by atomic force microscopy metallic tip-enhanced near-field fluorescence lifetime microscopy. Rev Sci Instrum 74(7):3347–3355. https://doi.org/10.1063/1.1581359
Adams JD et al (2014) High-speed imaging upgrade for a standard sample scanning atomic force microscope using small cantilevers. Rev Sci Instrum 85(9):093702. https://doi.org/10.1063/1.4895460
Nievergelt AP et al (2014) High-frequency multimodal atomic force microscopy. Beilstein J Nanotechnol 5:2459–2467. https://doi.org/10.3762/bjnano.5.255
Burns DJ, Youcef-Toumi K, Fantner GE (2011) Indirect identification and compensation of lateral scanner resonances in atomic force microscopes. Nanotechnology 22(31):315701. https://doi.org/10.1088/0957-4484/22/31/315701
Kammer CM, et al. Data-driven controller design for atomic-force microscopy In: 20th World Congress of IFAC2017: Toulouse, France
Nievergelt AP et al (2015) Studying biological membranes with extended range high-speed atomic force microscopy. Sci Rep 5:11987. https://doi.org/10.1038/srep11987
Lonergan NE, Britt LD, Sullivan CJ (2014) Immobilizing live Escherichia coli for AFM studies of surface dynamics. Ultramicroscopy 137:30–39. https://doi.org/10.1016/j.ultramic.2013.10.017
Johansson J et al (2002) An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes. Cell 110(5):551–561
Deng Y, Sun M, Shaevitz JW (2011) Direct measurement of cell wall stress stiffening and turgor pressure in live bacterial cells. Phys Rev Lett 107(15):158101. https://doi.org/10.1103/PhysRevLett.107.158101
Polyakov P et al (2011) Automated force volume image processing for biological samples. PLoS One 6(4):e18887. https://doi.org/10.1371/journal.pone.0018887
Raman A et al (2011) Mapping nanomechanical properties of live cells using multi-harmonic atomic force microscopy. Nat Nanotechnol 6(12):809–814. https://doi.org/10.1038/nnano.2011.186
Velegol SB et al (2003) AFM imaging artifacts due to bacterial cell height and AFM tip geometry. Langmuir 19(3):851–857. https://doi.org/10.1021/la026440g
Kindt JH et al (2004) Automated wafer-scale fabrication of electron beam deposited tips for atomic force microscopes using pattern recognition. Nanotechnology 15(9):1131–1134. https://doi.org/10.1088/0957-4484/15/9/005
Erickson BW et al (2012) Large-scale analysis of high-speed atomic force microscopy data sets using adaptive image processing. Beilstein J Nanotechnol 3:747–758. https://doi.org/10.3762/bjnano.3.84
Eaton PJ, West P (2010) Atomic force microscopy, vol viii. Oxford University Press, Oxford; New York, p 248
Odermatt PD et al (2015) High-resolution correlative microscopy: bridging the gap between single molecule localization microscopy and atomic force microscopy. Nano Lett 15(8):4896–4904. https://doi.org/10.1021/acs.nanolett.5b00572
Acknowledgments
This work was supported by the Swiss National Science Foundation under grant agreement numbers 205321_134786 and 205320_152675. H.A. Eskandarian acknowledges the support of an EMBO advanced long-term fellowship (LTF 191-2014 & ALTF 750-2016).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Eskandarian, H.A., Nievergelt, A.P., Fantner, G.E. (2018). Time-Resolved Imaging of Bacterial Surfaces Using Atomic Force Microscopy. In: Lyubchenko, Y. (eds) Nanoscale Imaging. Methods in Molecular Biology, vol 1814. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8591-3_23
Download citation
DOI: https://doi.org/10.1007/978-1-4939-8591-3_23
Published:
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-8590-6
Online ISBN: 978-1-4939-8591-3
eBook Packages: Springer Protocols