| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan
2 Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA
3 PRESTO, JST, Sumiyoshi-ku, Osaka 558-8585, Japan
Correspondence
Makoto Miyata
miyata{at}sci.osaka-cu.ac.jp
Mycoplasma mobile has a flask-shaped cell morphology and glides toward its tapered end at a rate of 3–7 cell lengths per s (2·0–4·5 µm s–1) by an unknown mechanism. Gliding requires that the surface of the cell is in contact with a solid substrate, such as glass or plastic. In order to characterize the nature of the outer surface of M. mobile, monoclonal antibodies were raised against intact cells and screened for their ability to recognize surface proteins. Four antibodies were identified and their protein targets were determined. One antibody recognized the Gli349 protein, which is known to be involved in glass binding and gliding. This antibody was also able to displace attached M. mobile cells from glass, suggesting that Gli349 is the major adhesion protein in M. mobile. The other three antibodies recognized members of the Mvsp family of proteins, which are presumably the major surface antigens of M. mobile. Immunofluorescence studies were performed to localize these proteins on the surface of M. mobile cells. Gli349 localized to the proximal region of the tapered part of the cell (the ‘neck’), while the various Mvsp family members showed several distinct patterns of subcellular localization. MvspN and MvspO localized to the distal end of the tapered part of the cell (the ‘head’), MvspK localized to the main part of the cell (the ‘body’), and MvspI localized to both the head and body but not the neck. This analysis shows that M. mobile surprisingly expresses multiple versions of its major surface antigen at once but differentiates its surface by differential localization of the various paralogues.
Present address: Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya 464-8602, Japan.
Present address: Department of Oral Microbiology, Meikai University School of Dentistry, 1-1 Keyakidai, Sakado, Saitama, 350-0283, Japan.
Present address: Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
This article has been cited by other articles:
|
|
 |
|
  D. Nakane and M. Miyata Cytoskeletal Asymmetrical Dumbbell Structure of a Gliding Mycoplasma, Mycoplasma gallisepticum, Revealed by Negative-Staining Electron Microscopy J. Bacteriol., May 15, 2009; 191(10): 3256 - 3264. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Uenoyama, S. Seto, D. Nakane, and M. Miyata Regions on Gli349 and Gli521 Protein Molecules Directly Involved in Movements of Mycoplasma mobile Gliding Machinery, Suggested by Use of Inhibitory Antibodies and Mutants J. Bacteriol., March 15, 2009; 191(6): 1982 - 1985. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Nakane and M. Miyata Cytoskeletal "jellyfish" structure of Mycoplasma mobile PNAS, December 4, 2007; 104(49): 19518 - 19523. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Nagai and M. Miyata Gliding Motility of Mycoplasma mobile Can Occur by Repeated Binding to N-Acetylneuraminyllactose (Sialyllactose) Fixed on Solid Surfaces. J. Bacteriol., September 1, 2006; 188(18): 6469 - 6475. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Adan-Kubo, A. Uenoyama, T. Arata, and M. Miyata Morphology of Isolated Gli349, a Leg Protein Responsible for Mycoplasma mobile Gliding via Glass Binding, Revealed by Rotary Shadowing Electron Microscopy. J. Bacteriol., April 1, 2006; 188(8): 2821 - 2828. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. W. Charon Mycoplasma takes a walk PNAS, September 27, 2005; 102(39): 13713 - 13714. [Full Text] [PDF]
|
|
|
|
|
|
A. Uenoyama and M. Miyata From the Cover: Gliding ghosts of Mycoplasma mobile PNAS, September 6, 2005; 102(36): 12754 - 12758. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Uenoyama and M. Miyata Identification of a 123-Kilodalton Protein (Gli123) Involved in Machinery for Gliding Motility of Mycoplasma mobile J. Bacteriol., August 15, 2005; 187(16): 5578 - 5584. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Seto, A. Uenoyama, and M. Miyata Identification of a 521-Kilodalton Protein (Gli521) Involved in Force Generation or Force Transmission for Mycoplasma mobile Gliding J. Bacteriol., May 15, 2005; 187(10): 3502 - 3510. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Seto, T. Kenri, T. Tomiyama, and M. Miyata Involvement of P1 Adhesin in Gliding Motility of Mycoplasma pneumoniae as Revealed by the Inhibitory Effects of Antibody under Optimized Gliding Conditions J. Bacteriol., March 1, 2005; 187(5): 1875 - 1877. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
