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Updated: Mar 19, 2026

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Structural Study of MPN387, an Essential Protein for Gliding Motility of a Human-Pathogenic Bacterium, Mycoplasma

Yoshito Kawakita1, Miki Kinoshita2, Yukio Furukawa3

  • 1Graduate School of Science, Osaka City University, Osaka, Japan.

Journal of Bacteriology
|June 22, 2016
PubMed
Abstract

Insights

Mycoplasma pneumoniae uses a unique gliding motility mechanism involving the MPN387 protein. This study reveals MPN387

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biophysics

Background:

  • Mycoplasma pneumoniae causes human pneumonia through a unique gliding motility.
  • This motility involves binding to sialylated oligosaccharides on host cells.
  • The attachment organelle, a protrusion at the cell pole, facilitates this process.

Purpose of the Study:

  • To elucidate the gliding motility mechanism of Mycoplasma pneumoniae.
  • To characterize the structure and function of MPN387, a key protein in the attachment organelle's bowl complex.

Main Methods:

  • Isolation and purification of recombinant MPN387 proteins (with and without EYFP tag).
  • Analysis using gel filtration chromatography, circular dichroism spectroscopy, analytical ultracentrifugation, partial proteolysis, and rotary-shadowing electron microscopy.
  • Superimposition of molecular images onto electron micrographs using fluorescent protein tagging.

Main Results:

  • MPN387 is a dumbbell-shaped homodimer, 42.7 nm in length and 9.1 nm in diameter.
  • It features a central parallel coiled-coil region of 24.5 nm.
  • MPN387 is essential for gliding motility but not for cytadherence.

Conclusions:

  • MPN387 plays a crucial role in the gliding mechanism of Mycoplasma pneumoniae.
  • The protein's structure supports its proposed function in motility.
  • Further research is needed to fully understand its contribution to the gliding process.

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