Tubular structures of Mycoplasma gallisepticum and their possible participation in cell motility

1 Institute of Cytology, Russian Academy of Science, Tikhoretsky Avenue, 4, 194064, St Petersburg, Russia 2 Timiryazev Agricultural Academy, Timiryazev Street, 49, 127550, Moscow, Russia 5 Author for correspondence: Sergei N. Borchsenius. Tel: +7 812 247 13 13. Fax: +7 812 247 03 41. e-mail: borch@c...

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Bibliographic Details
Published in:Microbiology (Society for General Microbiology) 1994-03, Vol.140 (3), p.671-681
Main Authors: Korolev, Eugene V, Nikonov, Andrew V, Brudnaya, Margarita S, Snigirevskaya, Ekaterina S, Sabinin, George V, Komissarchik, Yan Yu, Ivanov, Peter I, Borchsenius, Sergei N
Format: Article
Language:English
Subjects:
Acholeplasma laidlawii
Animals
Antibodies, Monoclonal
Bacterial Proteins - chemistry
Bacterial Proteins - immunology
Bacterial Proteins - physiology
Cell Movement - physiology
Immunoblotting
Microscopy, Immunoelectron
Molecular Weight
Mycoplasma - chemistry
Mycoplasma - physiology
Mycoplasma - ultrastructure
Mycoplasma gallisepticum
Organelles - chemistry
Organelles - physiology
Organelles - ultrastructure
Swine
Tubulin - chemistry
Tubulin - immunology
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Summary:1 Institute of Cytology, Russian Academy of Science, Tikhoretsky Avenue, 4, 194064, St Petersburg, Russia 2 Timiryazev Agricultural Academy, Timiryazev Street, 49, 127550, Moscow, Russia 5 Author for correspondence: Sergei N. Borchsenius. Tel: +7 812 247 13 13. Fax: +7 812 247 03 41. e-mail: borch@cell.spb.su. ABSTRACT In five strains of Mycoplasma gallisepticum , a protein with a molecular mass of about 40 kDa was detected by immunoblotting with anti-pig brain tubulin polyclonal and monoclonal antibodies. In eight other mycoplasma species similarly tested no reaction was observed. Thin serial sections of M. gallisepticum and Acholeplasma laidlawii cells examined by transmission electron microscopy revealed a submembrane system of tubules 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 labelling of the tubular system. Analysis of the tubular structures by high 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 involvement of the tubular system in mycoplasma motility is suggested. Keywords: Mycoplasma gallisepticum, cytoskeleton, tubular structures, motility
ISSN:1350-0872
1465-2080
DOI:10.1099/00221287-140-3-671