title: Integrated Information and Prospects for Gliding Mechanism of the Pathogenic Bacterium Mycoplasma pneumoniae.
abstract: Mycoplasma pneumoniae forms a membrane protrusion at a cell pole and is known to adhere to solid surfaces, including animal cells, and can glide on these surfaces with a speed up to 1 μm per second. Notably, gliding appears to be involved in the infectious process in addition to providing the bacteria with a means of escaping the host's immune systems. However, the genome of M. pneumoniae does not encode any of the known genes found in other bacterial motility systems or any conventional motor proteins that are responsible for eukaryotic motility. Thus, further analysis of the mechanism underlying M. pneumoniae gliding is warranted. The gliding machinery formed as the membrane protrusion can be divided into the surface and internal structures. On the surface, P1 adhesin, a 170 kDa transmembrane protein forms an adhesin complex with other two proteins. The internal structure features a terminal button, paired plates, and a bowl (wheel) complex. In total, the organelle is composed of more than 15 proteins. By integrating the currently available information by genetics, microscopy, and structural analyses, we have suggested a working model for the architecture of the organelle. Furthermore, in this article, we suggest and discuss a possible mechanism of gliding based on the structural model, in which the force generated around the bowl complex transmits through the paired plates, reaching the adhesin complex, resulting in the repeated catch of sialylated oligosaccharides on the host surface by the adhesin complex.
authors.affiliation: Department of Biology, Graduate School of Science, Osaka City UniversityOsaka, Japan; The OCU Advanced Research Institute for Natural Science and Technology, Osaka City UniversityOsaka, Japan.
authors.forename: Makoto
authors.initials: M
authors.lastname: Miyata
authors.affiliation: Department of Biology, Graduate School of Science, Osaka City UniversityOsaka, Japan; The OCU Advanced Research Institute for Natural Science and Technology, Osaka City UniversityOsaka, Japan.
authors.forename: Tasuku
authors.initials: T
authors.lastname: Hamaguchi
keywords: Mollicute; cell architecture; electron microscopy; evolution; motility; sialylated oligosaccharide