Probing Bacterial Adhesion at the Single-Molecule and Single-Cell Levels by AFM-Based Force Spectroscopy

2018 ◽  
pp. 403-414 ◽  
Author(s):  
Sofiane El-Kirat-Chatel ◽  
Audrey Beaussart
Keyword(s):  
Single Cell ◽  
Single Molecule ◽  
Bacterial Adhesion ◽  
Force Spectroscopy

Quantifying bacterial adhesion on antifouling polymer brushes via single-cell force spectroscopy

2015 ◽  
Vol 6 (31) ◽  
pp. 5740-5751 ◽  
Author(s):  
Cesar Rodriguez-Emmenegger ◽  
Sébastien Janel ◽  
Andres de los Santos Pereira ◽  
Michael Bruns ◽  
Frank Lafont
Keyword(s):  
Atomic Force Microscope ◽  
Single Cell ◽  
Bacterial Adhesion ◽  
Bacterial Cell ◽  
Polymer Brushes ◽  
Force Spectroscopy ◽  
Adhesion Forces ◽  
Atomic Force ◽  
Cell Force

The adhesion forces between a single bacterial cell and different polymer brushes were measured directly with an atomic force microscope and correlated with their resistance to fouling.

scholarly journals Effect of Graphene Oxide Packing on Bacterial Adhesion using Single Cell Force Spectroscopy

2018 ◽  
Vol 114 (3) ◽  
pp. 352a-353a
Author(s):  
Elise Linna ◽  
Sara BinAhmed ◽  
Benjamin L. Stottrup ◽  
Santiago Romero-Vargas Castrill¢n
Keyword(s):  
Graphene Oxide ◽  
Single Cell ◽  
Bacterial Adhesion ◽  
Force Spectroscopy ◽  
Cell Force

Bacterial adhesion force quantification by fluidic force microscopy

Nanoscale ◽  
2015 ◽  
Vol 7 (9) ◽  
pp. 4070-4079 ◽  
Author(s):  
Eva Potthoff ◽  
Dario Ossola ◽  
Tomaso Zambelli ◽  
Julia A. Vorholt
Keyword(s):  
Single Cell ◽  
Bacterial Adhesion ◽  
Adhesion Force ◽  
State Of The Art ◽  
Force Spectroscopy ◽  
Force Microscopy ◽  
Cell Force ◽  
Serial Measurements ◽  
Cell Fixation

Fluidic force microscopy demonstrates the potential to quantify bacterial adhesion by single-cell force spectroscopy, achieving higher immobilization forces than state-of-the-art cell-cantilever interactions. Reversible cell fixation on the tip allows for serial measurements of many cells in the nN range using a single cantilever.

scholarly journals Increasing throughput of AFM-based single cell adhesion measurements through multisubstrate surfaces

2015 ◽  
Vol 6 ◽  
pp. 157-166 ◽  
Author(s):  
Miao Yu ◽  
Nico Strohmeyer ◽  
Jinghe Wang ◽  
Daniel J Müller ◽  
Jonne Helenius
Keyword(s):  
Cell Adhesion ◽  
Single Cell ◽  
Adhesion Molecules ◽  
Cell Lines ◽  
Single Molecule ◽  
Cell Adhesion Molecules ◽  
Mammalian Cells ◽  
Force Spectroscopy ◽  
Matrix Proteins ◽  
Cell Force

Mammalian cells regulate adhesion by expressing and regulating a diverse array of cell adhesion molecules on their cell surfaces. Since different cell types express distinct sets of cell adhesion molecules, substrate-specific adhesion is cell type- and condition-dependent. Single-cell force spectroscopy is used to quantify the contribution of cell adhesion molecules to adhesion of cells to specific substrates at both the cell and single molecule level. However, the low throughput of single-cell adhesion experiments greatly limits the number of substrates that can be examined. In order to overcome this limitation, segmented polydimethylsiloxane (PDMS) masks were developed, allowing the measurement of cell adhesion to multiple substrates. To verify the utility of the masks, the adhesion of four different cell lines, HeLa (Kyoto), prostate cancer (PC), mouse kidney fibroblast and MDCK, to three extracellular matrix proteins, fibronectin, collagen I and laminin 332, was examined. The adhesion of each cell line to different matrix proteins was found to be distinct; no two cell lines adhered equally to each of the proteins. The PDMS masks improved the throughput limitation of single-cell force spectroscopy and allowed for experiments that previously were not feasible. Since the masks are economical and versatile, they can aid in the improvement of various assays.

Optical tweezers for single molecule force spectroscopy on bacterial adhesion organelles

2006 ◽  
Author(s):  
Magnus Andersson ◽  
Ove Axner ◽  
Bernt Eric Uhlin ◽  
Erik Fällman
Keyword(s):  
Optical Tweezers ◽  
Single Molecule ◽  
Bacterial Adhesion ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy

scholarly journals Homophilic and heterophilic cadherin bond rupture forces in homo- or hetero-cellular systems measured by AFM-based single-cell force spectroscopy

2021 ◽  
Author(s):  
Prem Kumar Viji Babu ◽  
Ursula Mirastschijski ◽  
Ganzanfer Belge ◽  
Manfred Radmacher
Keyword(s):  
Single Cell ◽  
Single Molecule ◽  
Actin Filaments ◽  
Adherens Junctions ◽  
Bond Formation ◽  
Force Spectroscopy ◽  
Cellular Systems ◽  
Bond Rupture ◽  
Extracellular Region ◽  
Cell Force

AbstractCadherins enable intercellular adherens junctions to withstand tensile forces in tissues, e.g. generated by intracellular actomyosin contraction. In-vitro single molecule force spectroscopy experiments can reveal cadherin–cadherin extracellular region binding dynamics such as bond formation and strength. However, characterization of cadherin-presenting cell homophilic and heterophilic binding in the proteins’ native conformational and functional states in living cells has rarely been done. Here, we used atomic force microscopy (AFM) based single-cell force spectroscopy (SCFS) to measure rupture forces of homophilic and heterophilic bond formation of N- (neural), OB- (osteoblast) and E- (epithelial) cadherins in living fibroblast and epithelial cells in homo- and hetero-cellular arrangements, i.e., between cells and cadherins of the same and different types. In addition, we used indirect immunofluorescence labelling to study and correlate the expression of these cadherins in intercellular adherens junctions. We showed that N/N and E/E-cadherin homophilic binding events are stronger than N/OB heterophilic binding events. Disassembly of intracellular actin filaments affects the cadherin bond rupture forces suggesting a contribution of actin filaments in cadherin extracellular binding. Inactivation of myosin did not affect the cadherin rupture force in both homo- and hetero-cellular arrangements, but particularly strengthened the N/OB heterophilic bond and reinforced the other cadherins’ homophilic bonds.

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