This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Meconi, S.
Right arrow Articles by Capo, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Meconi, S.
Right arrow Articles by Capo, C.

 Previous Article  |  Next Article 

Infection and Immunity, November 1998, p. 5527-5533, Vol. 66, No. 11
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Coxiella burnetii Induces Reorganization of the Actin Cytoskeleton in Human Monocytes

Sonia Meconi,1 Véronique Jacomo,1 Patrice Boquet,2 Didier Raoult,1 Jean-Louis Mege,1 and Christian Capo1,*

Unité des Rickettsies, CNRS ESA 6020, Faculté de Médecine, Université de la Méditerranée, 13385 Marseilles Cedex 05,1 and INSERM Unité 452, Faculté de Médecine, 06107 Nice Cedex 2,2 France

Received 5 March 1998/Returned for modification 11 May 1998/Accepted 14 August 1998

Coxiella burnetii, an obligate intracellular bacterium which survives in myeloid cells, causes Q fever in humans. We previously demonstrated that virulent C. burnetii organisms are poorly internalized by monocytes compared to avirulent variants. We hypothesized that a differential mobilization of the actin cytoskeleton may account for this distinct phagocytic behavior. Scanning electron microscopy demonstrated that virulent C. burnetii stimulated profound and polymorphic changes in the morphology of THP-1 monocytes, consisting of membrane protrusions and polarized projections. These changes were transient, requiring 5 min to reach their maximum extent and vanishing after 60 min of incubation. In contrast, avirulent variants of C. burnetii did not induce any significant changes in cell morphology. The distribution of filamentous actin (F-actin) was then studied with a specific probe, bodipy phallacidin. Virulent C. burnetii induced a profound and transient reorganization of F-actin, accompanied by an increase in the F-actin content of THP-1 cells. F-actin was colocalized with myosin in cell protrusions, suggesting that actin polymerization and the tension of actin-myosin filaments play a role in C. burnetii-induced morphological changes. In addition, contact between the cell and the bacterium seems to be necessary to induce cytoskeleton reorganization. Bacterial supernatants did not stimulate actin remodeling, and virulent C. burnetii organisms were found in close apposition with F-actin protrusions. The manipulation of the actin cytoskeleton by C. burnetii may therefore play a critical role in the internalization strategy of this bacterium.

* Corresponding author. Mailing address: Unité des Rickettsies, CNRS ESA 6020, Faculté de Médecine, 27 Bd J. Moulin, 13385 Marseille Cedex 05, France. Phone: (33) 4 91 32 43 75. Fax: (33) 4 91 38 77 72. E-mail: Jean-Louis.Mege{at}medecine.univ-mrs.fr.

Infection and Immunity, November 1998, p. 5527-5533, Vol. 66, No. 11
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Honstettre, A., Ghigo, E., Moynault, A., Capo, C., Toman, R., Akira, S., Takeuchi, O., Lepidi, H., Raoult, D., Mege, J.-L. (2004). Lipopolysaccharide from Coxiella burnetii Is Involved in Bacterial Phagocytosis, Filamentous Actin Reorganization, and Inflammatory Responses through Toll-Like Receptor 4. J. Immunol. 172: 3695-3703 [Abstract] [Full Text]  
  • Seshadri, R., Paulsen, I. T., Eisen, J. A., Read, T. D., Nelson, K. E., Nelson, W. C., Ward, N. L., Tettelin, H., Davidsen, T. M., Beanan, M. J., Deboy, R. T., Daugherty, S. C., Brinkac, L. M., Madupu, R., Dodson, R. J., Khouri, H. M., Lee, K. H., Carty, H. A., Scanlan, D., Heinzen, R. A., Thompson, H. A., Samuel, J. E., Fraser, C. M., Heidelberg, J. F. (2003). Complete genome sequence of the Q-fever pathogen Coxiellaburnetii. Proc. Natl. Acad. Sci. USA 100: 5455-5460 [Abstract] [Full Text]  
  • Capo, C., Moynault, A., Collette, Y., Olive, D., Brown, E. J., Raoult, D., Mege, J.-L. (2003). Coxiella burnetii Avoids Macrophage Phagocytosis by Interfering with Spatial Distribution of Complement Receptor 3. J. Immunol. 170: 4217-4225 [Abstract] [Full Text]  
  • Rolain, J. M., La Scola, B., Liang, Z., Davoust, B., Raoult, D. (2001). Immunofluorescent Detection of Intraerythrocytic Bartonella henselae in Naturally Infected Cats. J. Clin. Microbiol. 39: 2978-2980 [Abstract] [Full Text]  
  • Meconi, S., Capo, C., Remacle-Bonnet, M., Pommier, G., Raoult, D., Mege, J.-L. (2001). Activation of Protein Tyrosine Kinases by Coxiella burnetii: Role in Actin Cytoskeleton Reorganization and Bacterial Phagocytosis. Infect. Immun. 69: 2520-2526 [Abstract] [Full Text]  
  • Dellacasagrande, J., Ghigo, E., Machergui-El, S., Hammami, , Toman, R., Raoult, D., Capo, C., Mege, J.-L. (2000). alpha vbeta 3 Integrin and Bacterial Lipopolysaccharide Are Involved in Coxiella burnetii-Stimulated Production of Tumor Necrosis Factor by Human Monocytes. Infect. Immun. 68: 5673-5678 [Abstract] [Full Text]  
  • Dellacasagrande, J., Ghigo, E., Capo, C., Raoult, D., Mege, J.-L. (2000). Coxiella burnetii Survives in Monocytes from Patients with Q Fever Endocarditis: Involvement of Tumor Necrosis Factor. Infect. Immun. 68: 160-164 [Abstract] [Full Text]  
  • Capo, C., Lindberg, F. P., Meconi, S., Zaffran, Y., Tardei, G., Brown, E. J., Raoult, D., Mege, J.-L. (1999). Subversion of Monocyte Functions by Coxiella burnetii: Impairment of the Cross-Talk Between {alpha}v{beta}3 Integrin and CR3. J. Immunol. 163: 6078-6085 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»