ArticleFEMS microbiology letters2019
Identification of novel protein domain for sialyloligosaccharide binding essential to Mycoplasma mobile gliding.
Article in FEMS microbiology letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 28 citations in OpenAlex.
- Dimeric assembly of FScience advances · 2025Article
- Nano-Scale Video Imaging of Motility Machinery by High-Speed Atomic Force Microscopy.Biomolecules · 2025Review
- Internal structure ofBiophysics and physicobiology · 2024Article
- 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
- Purification and Structural Analysis of the Gliding Motility Machinery in Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cell shape controls rheotaxis in small parasitic bacteria.PLoS pathogens · 2022Article
- Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae.BMC microbiology · 2022Article
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- Chained Structure of Dimeric FmBio · 2021Article
- Movements of Mycoplasma mobile Gliding Machinery Detected by High-Speed Atomic Force Microscopy.mBio · 2021Article
- Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile.Scientific reports · 2020Article
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4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialic acids, terminal structures of sialylated glycoconjugates, are widely distributed in animal tissues and are often involved in intercellular recognitions, including some bacteria and viruses. Mycoplasma mobile, a fish pathogenic bacterium, binds to sialyloligosaccharide (SO) through adhesin Gli349 and glides on host cell surfaces. The amino acid sequence of Gli349 shows no similarity to known SO-binding proteins. In the present study, we predicted the binding part of Gli349, produced it in Escherichia coli and proved its binding activity to SOs of fetuin using atomic force microscopy. Binding was detected with a frequency of 10.3% under retraction speed of 400 nm/s and was shown to be specific for SO, as binding events were competitively inhibited by the addition of free 3'-sialyllactose. The histogram of the unbinding forces showed 24 pN and additional peaks. These results suggested that the distal end of Gli349 constitutes a novel sialoadhesin domain and is directly involved in the gliding mechanism of M. mobile.
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