ArticleScientific reports2020
Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Distinct motors, shared mechanics: unifying principles of microbial gliding.Journal of bacteriology · 2026Review
- An atypical F-type ATPase is necessary for the function of the antibody cleavage system MIB-MIP in mycoplasmas.PLoS pathogens · 2026Article
- Dimeric assembly of FScience advances · 2025Article
- Gliding direction ofBiophysics and physicobiology · 2025Article
- The gut microbiome of farmed Arctic char (FEMS microbes · 2024Article
- Internal structure ofBiophysics and physicobiology · 2024Article
- Rapid in vitro method to assemble and transfer DNA fragments into the JCVI-syn3B minimal synthetic bacterial genome through Cre/Biophysics and physicobiology · 2024Article
- Hyperactive nanobacteria with host-dependent traits pervade Omnitrophota.Nature microbiology · 2023Article
- Structure and Function of Gli123 Involved in Mycoplasma mobile Gliding.Journal of bacteriology · 2023Article
- Motility Assays of Mycoplasma mobile Under Light Microscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Imaging Minimal Bacteria at the Nanoscale: a Reliable and Versatile Process to Perform Single-Molecule Localization Microscopy in Mycoplasmas.Microbiology spectrum · 2022Article
- Chained Structure of Dimeric FmBio · 2021Article
- Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy.mBio · 2021Article
- The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction.Science advances · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma mobile, a fish pathogen, exhibits its own specialized gliding motility on host cells based on ATP hydrolysis. The special protein machinery enabling this motility is composed of surface and internal protein complexes. Four proteins, MMOBs 1630, 1660, 1670, and 4860 constitute the internal complex, including paralogs of F-type ATPase/synthase α and β subunits. In the present study, the cellular localisation for the candidate gliding machinery proteins, MMOBs 1620, 1640, 1650, and 5430 was investigated by using a total internal reflection fluorescence microscopy system after tagging these proteins with the enhanced yellow fluorescent protein (EYFP). The M. mobile strain expressing a fusion protein MMOB1620-EYFP exhibited reduced cell-binding activity and a strain expressing MMOB1640 fused with EYFP exhibited increased gliding speed, showing the involvement of these proteins in the gliding mechanism. Based on the genomic sequences, we analysed the sequence conservativity in the proteins of the internal and the surface complexes from four gliding mycoplasma species. The proteins in the internal complex were more conserved compared to the surface complex, suggesting that the surface complex undergoes modifications depending on the host. The analyses suggested that the internal gliding complex was highly conserved probably due to its role in the motility mechanism.
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