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TitleRefined Mechanism of Mycoplasma mobile Gliding Based on Structure, ATPase Activity, and Sialic Acid Binding of Machinery.
Journal, issue, pagesmBio, Vol. 10, Issue 6, Year 2019
Publish dateDec 24, 2019
AuthorsMiyuki S Nishikawa / Daisuke Nakane / Takuma Toyonaga / Akihiro Kawamoto / Takayuki Kato / Keiichi Namba / Makoto Miyata /
PubMed Abstract, a fish pathogen, glides on solid surfaces by repeated catch, pull, and release of sialylated oligosaccharides by a unique mechanism based on ATP energy. The gliding machinery is composed of huge ..., a fish pathogen, glides on solid surfaces by repeated catch, pull, and release of sialylated oligosaccharides by a unique mechanism based on ATP energy. The gliding machinery is composed of huge surface proteins and an internal "jellyfish"-like structure. Here, we elucidated the detailed three-dimensional structures of the machinery by electron cryotomography. The internal "tentacle"-like structure hydrolyzed ATP, which was consistent with the fact that the paralogs of the α- and β-subunits of F-ATPase are at the tentacle structure. The electron microscopy suggested conformational changes of the tentacle structure depending on the presence of ATP analogs. The gliding machinery was isolated and showed that the binding activity to sialylated oligosaccharide was higher in the presence of ADP than in the presence of ATP. Based on these results, we proposed a model to explain the mechanism of gliding. The genus is made up of the smallest parasitic and sometimes commensal bacteria; , which causes human "walking pneumonia," is representative. More than ten species glide on host tissues by novel mechanisms, always in the direction of the distal side of the machinery. , the fastest species in the genus, catches, pulls, and releases sialylated oligosaccharides (SOs), the carbohydrate molecules also targeted by influenza viruses, by means of a specific receptor and using ATP hydrolysis for energy. Here, the architecture of the gliding machinery was visualized three dimensionally by electron cryotomography (ECT), and changes in the structure and binding activity coupled to ATP hydrolysis were discovered. Based on the results, a refined mechanism was proposed for this unique motility.
External linksmBio / PubMed:31874918 / PubMed Central
MethodsEM (tomography)
Structure data

EMDB-0893:
Detailed structures of the gliding machinery observed by ECT
Method: EM (tomography)

Source
  • Mycoplasma mobile (bacteria)

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