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Identification and sequence analyses of the gliding machinery proteins from Mycoplasma mobile

Isil Tulum1, Kenta Kimura1, Makoto Miyata2

  • 1Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka, 558-8585, Japan.

Scientific Reports
|March 4, 2020
PubMed

Insights

Mycoplasma mobile uses a specialized protein machinery for gliding motility, powered by ATP hydrolysis. Key internal proteins were identified, revealing conserved mechanisms essential for this fish pathogen's movement.

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Mycoplasma mobile is a fish pathogen known for its unique gliding motility.
  • This motility is crucial for host cell interaction and is driven by ATP hydrolysis.
  • The motility machinery involves complex surface and internal protein structures.

Purpose of the Study:

  • To investigate the cellular localization of candidate gliding machinery proteins in Mycoplasma mobile.
  • To determine the role of specific proteins in the gliding motility mechanism.
  • To analyze the sequence conservation of motility proteins across different Mycoplasma species.

Main Methods:

  • Utilized total internal reflection fluorescence microscopy (TIRFm) to visualize protein localization.
  • Engineered M. mobile strains expressing EYFP-tagged candidate proteins (MMOBs 1620, 1640, 1650, 5430).
  • Performed genomic sequence analysis to assess protein conservativity.

Main Results:

  • MMOB1620-EYFP fusion protein expression correlated with reduced cell-binding activity.
  • MMOB1640-EYFP fusion protein expression was linked to increased gliding speed.
  • Internal gliding complex proteins showed higher sequence conservation than surface complex proteins across four species.

Conclusions:

  • MMOB1620 and MMOB1640 are involved in the gliding motility mechanism of Mycoplasma mobile.
  • The internal gliding complex is highly conserved, likely due to its fundamental role in motility.
  • The surface complex appears more adaptable, potentially undergoing host-specific modifications.

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