IgGs are made for walking on bacterial and viral surfaces

Preiner, Johannes; Kodera, Noriyuki; Tang, Jilin; Ebner, Andreas; Brameshuber, Mario; Blaas, Dieter; Gelbmann, Nicola; Gruber, Hermann J.; Ando, Toshio; Hinterdorfer, Peter

doi:10.1038/ncomms5394

Cited by 105 publications

(112 citation statements)

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“…Note that R max depends on the sample fragility and spatial frequency of the surface corrugation to be detected, 1/λ, in the sample. As demonstrated in the studies of GroEL-GroES and immunoglobulin G (IgG)-antibody (Preiner et al 2014) interactions, the kinetics or strength of protein-protein interaction can be estimated from successive AFM images. Here, I briefly estimate how strong or weak protein-protein interactions can be measured by HS-AFM imaging.…”

Section: Imaging Ratementioning

confidence: 99%

“…Thus, the question arises: how, and how strongly, do the two Fabs bind to their epitopes? HS-AFM imaging was performed for monoclonal IgG antibodies placed on twodimensional crystalline protein layers and on a viral capsid (Preiner et al 2014). Monovalent Fab fragments bind to antigens tightly and not to move on the lattice surfaces.…”

Section: Hs-afm Imaging Of Biological Molecules In Actionmentioning

confidence: 99%

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Directly watching biomolecules in action by high-speed atomic force microscopy

Ando

2017

Biophys Rev

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Proteins are dynamic in nature and work at the single molecule level. Therefore, directly watching protein molecules in dynamic action at high spatiotemporal resolution must be the most straightforward approach to understanding how they function. To make this observation possible, highspeed atomic force microscopy (HS-AFM) has been developed. Its current performance allows us to film biological molecules at 10-16 frames/s, without disturbing their function. In fact, dynamic structures and processes of various proteins have been successfully visualized, including bacteriorhodopsin responding to light, myosin V walking on actin filaments, and even intrinsically disordered proteins undergoing order/disorder transitions. The molecular movies have provided insights that could not have been reached in other ways. Moreover, the cantilever tip can be used to manipulate molecules during successive imaging. This capability allows us to observe changes in molecules resulting from dissection or perturbation. This mode of imaging has been successfully applied to myosin V, peroxiredoxin and doublet microtubules, leading to new discoveries. Since HS-AFM can be combined with other techniques, such as super-resolution optical microscopy and optical tweezers, the usefulness of HS-AFM will be further expanded in the near future.

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Section: Imaging Ratementioning

confidence: 99%

Section: Hs-afm Imaging Of Biological Molecules In Actionmentioning

confidence: 99%

Directly watching biomolecules in action by high-speed atomic force microscopy

Ando

2017

Biophys Rev

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“…While the overall protein motion scales roughly with the local density of proteins in the membrane, individual proteins can also diffuse freely or become trapped by protein-protein interactions. In 2014, Preiner et al 147 utilized high-speed AFM to visualize the dynamics of single antibodies on membrane patches. Purple membrane was attached on mica.…”

mentioning

confidence: 99%

“…Antibodies bound to the non-enveloped viruses also moved around on the surface, similar to that of antibodies on bacterial surfaces. These studies [145][146][147] provide a straightforward visual evidence for elucidating how single protein molecules function in diverse surfaces, which is of important significance for us to understand nanoscale molecular activities. Besides topography imaging, AFM can also probe the folding processes of single native membrane protein in the cell membrane by mechanically unfolding single native protein.…”

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confidence: 99%

Nanoscale imaging and force probing of biomolecular systems using atomic force microscopy: from single molecules to living cells

Dang

et al. 2017

Nanoscale

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Due to the lack of adequate tools for observation, native molecular behaviors at the nanoscale have been poorly understood. The advent of atomic force microscopy (AFM) provides an exciting instrument for investigating physiological processes on individual living cells with molecular resolution, which attracts the attention of worldwide researchers. In the past few decades, AFM has been widely utilized to investigate molecular activities on diverse biological interfaces, and the performances and functions of AFM have also been continuously improved, greatly improving our understanding of the behaviors of single molecules in action and demonstrating the important role of AFM in addressing biological issues with unprecedented spatiotemporal resolution. In this article, we review the related techniques and recent progress about applying AFM to characterize biomolecular systems in situ from single molecules to living cells. The challenges and future directions are also discussed.

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“…In liquid, viscous damping yields Q ≈ 2-4, enabling extremely high imaging speeds. Using small cantilevers immersed in fluid, Ando and colleagues 5 pioneered close to video-rate AFM imaging and thereby established the field of HS-AFM in liquid on biological samples [1][2][3][12][13][14][15] . Although such cantilevers may also have a relatively low Q in air, their low spring constants make them primarily intended for imaging in fluid.…”

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confidence: 99%

Harnessing the damping properties of materials for high-speed atomic force microscopy

et al. 2015

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The success of high-speed atomic force microscopy in imaging molecular motors 1 , enzymes 2 and microbes 3 in liquid environments suggests that the technique could be of significant value in a variety of areas of nanotechnology. However, the majority of atomic force microscopy experiments are performed in air, and the tapping-mode detection speed of current highspeed cantilevers is an order of magnitude lower in air than in liquids. Traditional approaches to increasing the imaging rate of atomic force microscopy have involved reducing the size of the cantilever 4,5 , but further reductions in size will require a fundamental change in the detection method of the microscope [6][7][8] . Here, we show that high-speed imaging in air can instead be achieved by changing the cantilever material. We use cantilevers fabricated from polymers, which can mimic the high damping environment of liquids. With this approach, SU-8 polymer cantilevers are developed that have an imaging-in-air detection bandwidth that is 19 times faster than those of conventional cantilevers of similar size, resonance frequency and spring constant.A primary research goal in atomic force microscopy (AFM) is to increase the imaging speed, improve its ease of use and expand its potential range of applications 9 . In the most widely used AFM mode (a.c. mode or tapping mode) the detection speed (mechanical bandwidth, BW) of the AFM cantilever fundamentally limits the imaging speed. The bandwidth is a measure of the maximum rate of topography change the cantilever can accurately detect. It is related to the cantilever resonance as BW ∝ f 0 /Q, where the cantilever resonance frequency f 0 is primarily determined by the cantilever mass and elastic modulus, and the quality factor Q is determined by the cantilever damping 10 . When the oscillating cantilever experiences a change in boundary condition (that is, topography), it requires several cycles to reach a new steady-state amplitude (Fig. 1a). A cantilever with higher resonance frequency runs through the required number of cycles more quickly, thereby enabling faster imaging (Fig. 1b). The number of required oscillatory cycles is determined by the damping of the cantilever, characterized by Q. A cantilever with low resonance frequency and low Q can therefore be equally as fast as a cantilever with high resonance frequency and high Q (compare Fig. 1b and c). From a detection bandwidth perspective, the ideal combination is a high resonance frequency and low quality factor (Fig. 1d).The development of current high-speed AFM (HS-AFM) technology was enabled by the miniaturization of silicon and silicon nitride (SiN) cantilevers to x-y dimensions below 10 µm (the approach taken in Fig. 1b), resulting in cantilevers with megahertz resonance frequencies 4,5 . Modelling and an improved understanding of cantilever behaviour in fluids has greatly benefited this geometric optimization. For nearly all cantilevers, viscous damping in the surrounding medium determines Q (ref. 11). In liquid, viscous damping yields Q ≈ 2...

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IgGs are made for walking on bacterial and viral surfaces

Cited by 105 publications

References 47 publications

Directly watching biomolecules in action by high-speed atomic force microscopy

Directly watching biomolecules in action by high-speed atomic force microscopy

Nanoscale imaging and force probing of biomolecular systems using atomic force microscopy: from single molecules to living cells

Harnessing the damping properties of materials for high-speed atomic force microscopy

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