ArticlemBio2021
Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy.
Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Unraveling the role of distinct cytoskeletal motility structures in Mycoplasma pneumoniae relatives.BMC microbiology · 2025Review
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Dimeric assembly of FScience advances · 2025Article
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Screening the receptors forFrontiers in cellular and infection microbiology · 2025Article
- Holotomography and atomic force microscopy: a powerful combination to enhance cancer, microbiology and nanotoxicology research.Discover nano · 2024Review
- Internal structure ofBiophysics and physicobiology · 2024Article
- Spatiotemporal resolution in high-speed atomic force microscopy for studying biological macromolecules in action.Microscopy (Oxford, England) · 2023Review
- Detection of Steps and Rotation in the Gliding Motility of Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Purification and Structural Analysis of the Gliding Motility Machinery in Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mechanical limitation of bacterial motility mediated by growing cell chains.Biophysical journal · 2022Article
- High-speed Atomic Force Microscopy Observation of Internal Structure Movements in LivingBio-protocol · 2022Article
- A Single Shot of Vesicles.Microbes and environments · 2022Article
- Chained Structure of Dimeric FmBio · 2021Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma mobile, a parasitic bacterium, glides on solid surfaces, such as animal cells and glass, by a special mechanism. This process is driven by the force generated through ATP hydrolysis on an internal structure. However, the spatial and temporal behaviors of the internal structures in living cells are unclear. In this study, we detected the movements of the internal structure by scanning cells immobilized on a glass substrate using high-speed atomic force microscopy (HS-AFM). By scanning the surface of a cell, we succeeded in visualizing particles, 2 nm in height and aligned mostly along the cell axis with a pitch of 31.5 nm, consistent with previously reported features based on electron microscopy. Movements of individual particles were then analyzed by HS-AFM. In the presence of sodium azide, the average speed of particle movements was reduced, suggesting that movement is linked to ATP hydrolysis. Partial inhibition of the reaction by sodium azide enabled us to analyze particle behavior in detail, showing that the particles move 9 nm right, relative to the gliding direction, and 2 nm into the cell interior in 330 ms and then return to their original position, based on ATP hydrolysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.