TUBULAR STRUCTURES OF MYCOPLASMA-GALLISEPTICUM AND THEIR POSSIBLE PARTICIPATION IN CELL MOTILITY

In five strains of Mycoplasma gallisepticum, a protein with a molecula r mass of about 40 kDa was detected by immunoblotting with anti-pig br ain tubulin polyclonal and monoclonal antibodies. in eight other mycop lasma species similarly tested no reaction was observed. Thin serial s ections of M. gallisepticum and Acholeplasma laidlawii cells examined by transmission electron microscopy revealed a submembrane system of t ubules in M. gallisepticum but not in A. laidlawii. The intracellular spatial distribution of the tubular structures was reconstructed. Thin sections of M. gallisepticum treated with anti-tubulin antibodies and colloidal gold particles (immunogold labelling) revealed distinct lab elling of the tubular system. Analysis of the tubular structures by hi gh resolution electron microscopy and optical diffraction showed their helical organization to be: diameter 40 nm, helix pitch approximately 20 nm and electron-transparent core 10 nm in diameter. A possible inv olvement of the tubular system in mycoplasma motility is suggested.