Assembly Formation of P65, an Intrinsically Disordered Protein Involved in Gliding Machinery of <i>Mycoplasma pneumoniae</i>

• DOI: 10.20944/preprints202502.1200.v1
• Publication Date: 2025-02-19T00:18:17Z
• Authors: Masaru Yabe; Takuma Toyonaga; Miki Kinoshita; Yukio Furukawa; Tasuku Hamaguchi; Yuhei O Tahara; Munehito Arai; Katsumi Imada; Makoto Miyata

Mycoplasma pneumoniae is a human pathogen that glides on host cell surfaces by repeated catch and release mechanism using sialylated oligosaccharides. At pole, this organism forms protrusion called an attachment organelle composed of surface structures, including adhesin complex internal core structure. To clarify the structure function organelle, we focused component, P65, which essential for stabilization adjacent proteins P30 HMW2, respectively. Analysis its amino acid sequence (405 residues) suggested P65 contains intrinsically disordered region (residues 1-217) coiled-coil regions 226-247, 255-283, 286-320). Four protein fragments full-length were analyzed size exclusion chromatography, analytical centrifugation, circular dichroism spectroscopy, small-angle X-ray scattering, limited proteolysis, negative staining electron microscopy. The results showed formed multimer central globule with 30 23 nm axes 4 to 6 projections 14 in length. Our data suggest C-terminal responsible multimerization, while N-terminal filament. These assignments roles are discussed.