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 Garduño, R. A.
Right arrow Articles by Hoffman, P. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Garduño, R. A.
Right arrow Articles by Hoffman, P. S.

 Previous Article  |  Next Article 

J Bacteriol, February 1998, p. 505-513, Vol. 180, No. 3
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Immunolocalization of Hsp60 in Legionella pneumophila

Rafael A. Garduño,1,2 Gary Faulkner,1,3 Mary A. Trevors,1,3 Neeraj Vats,1 and Paul S. Hoffman1,2,*

Department of Microbiology and Immunology,1 Division of Infectious Diseases, Department of Medicine,2 and Electron Microscopy Laboratory,3 Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7

Received 3 September 1997/Accepted 4 December 1997

One of the most abundant proteins synthesized by Legionella pneumophila, particularly during growth in a variety of eukaryotic host cells, is Hsp60, a member of the GroEL family of molecular chaperones. The present study was initiated in response to a growing number of reports suggesting that for some bacteria, including L. pneumophila, Hsp60 may exist in extracytoplasmic locations. Immunolocalization techniques with Hsp60-specific monoclonal and polyclonal antibodies were used to define the subcellular location and distribution of Hsp60 in L. pneumophila grown in vitro, or in vivo inside of HeLa cells. For comparative purposes Escherichia coli, expressing recombinant L. pneumophila Hsp60, was employed. In contrast to E. coli, where Hsp60 was localized exclusively in the cytoplasm, in L. pneumophila Hsp60 was predominantly associated with the cell envelope, conforming to a distribution pattern typical of surface molecules that included the major outer membrane protein OmpS and lipopolysaccharide. Interestingly, heat-shocked L. pneumophila organisms exhibited decreased overall levels of cell-associated Hsp60 epitopes and increased relative levels of surface epitopes, suggesting that Hsp60 was released by stressed bacteria. Putative secretion of Hsp60 by L. pneumophila was further indicated by the accumulation of Hsp60 in the endosomal space, between replicating intracellular bacteria. These results are consistent with an extracytoplasmic location for Hsp60 in L. pneumophila and further suggest both the existence of a novel secretion mechanism (not present in E. coli) and a potential role in pathogenesis.


* Corresponding author. Mailing address: Department of Microbiology and Immunology, Faculty of Medicine, Sir Charles Tupper Medical Bldg., Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7. Phone: (902) 494-3889. Fax: (902) 494-5125. E-mail: hoffmanp{at}tupdean1.med.dal.ca.




This article has been cited by other articles:

  • Galka, F., Wai, S. N., Kusch, H., Engelmann, S., Hecker, M., Schmeck, B., Hippenstiel, S., Uhlin, B. E., Steinert, M. (2008). Proteomic Characterization of the Whole Secretome of Legionella pneumophila and Functional Analysis of Outer Membrane Vesicles. Infect. Immun. 76: 1825-1836 [Abstract] [Full Text]  
  • Berk, S. G., Faulkner, G., Garduno, E., Joy, M. C., Ortiz-Jimenez, M. A., Garduno, R. A. (2008). Packaging of Live Legionella pneumophila into Pellets Expelled by Tetrahymena spp. Does Not Require Bacterial Replication and Depends on a Dot/Icm-Mediated Survival Mechanism. Appl. Environ. Microbiol. 74: 2187-2199 [Abstract] [Full Text]  
  • Ge, Y., Rikihisa, Y. (2007). Surface-Exposed Proteins of Ehrlichia chaffeensis. Infect. Immun. 75: 3833-3841 [Abstract] [Full Text]  
  • Tsugawa, H., Ito, H., Ohshima, M., Okawa, Y. (2007). Cell adherence-promoted activity of Plesiomonas shigelloides GroEL. J Med Microbiol 56: 23-29 [Abstract] [Full Text]  
  • Henderson, B., Allan, E., Coates, A. R. M. (2006). Stress Wars: the Direct Role of Host and Bacterial Molecular Chaperones in Bacterial Infection. Infect. Immun. 74: 3693-3706 [Full Text]  
  • Lee, B.-Y., Horwitz, M. A., Clemens, D. L. (2006). Identification, Recombinant Expression, Immunolocalization in Macrophages, and T-Cell Responsiveness of the Major Extracellular Proteins of Francisella tularensis. Infect. Immun. 74: 4002-4013 [Abstract] [Full Text]  
  • Bergonzelli, G. E., Granato, D., Pridmore, R. D., Marvin-Guy, L. F., Donnicola, D., Corthesy-Theulaz, I. E. (2006). GroEL of Lactobacillus johnsonii La1 (NCC 533) Is Cell Surface Associated: Potential Role in Interactions with the Host and the Gastric Pathogen Helicobacter pylori. Infect. Immun. 74: 425-434 [Abstract] [Full Text]  
  • Lagace, T. A., Ridgway, N. D. (2005). The Rate-limiting Enzyme in Phosphatidylcholine Synthesis Regulates Proliferation of the Nucleoplasmic Reticulum. Mol. Biol. Cell 16: 1120-1130 [Abstract] [Full Text]  
  • Hiltz, M. F., Sisson, G. R., Brassinga, A. K. C., Garduno, E., Garduno, R. A., Hoffman, P. S. (2004). Expression of magA in Legionella pneumophila Philadelphia-1 Is Developmentally Regulated and a Marker of Formation of Mature Intracellular Forms. J. Bacteriol. 186: 3038-3045 [Abstract] [Full Text]  
  • Wagner, C. T., Lu, I. Y., Hoffman, M. H., Sun, W. Q., Trent, J. D., Connor, J. (2004). T-complex Polypeptide-1 Interacts with the Erythrocyte Cytoskeleton in Response to Elevated Temperatures. J. Biol. Chem. 279: 16223-16228 [Abstract] [Full Text]  
  • Trent, J. D., Kagawa, H. K., Paavola, C. D., McMillan, R. A., Howard, J., Jahnke, L., Lavin, C., Embaye, T., Henze, C. E. (2003). Intracellular localization of a group II chaperonin indicates a membrane-related function. Proc. Natl. Acad. Sci. USA 100: 15589-15594 [Abstract] [Full Text]  
  • Minnick, M. F., Smitherman, L. S., Samuels, D. S. (2003). Mitogenic Effect of Bartonella bacilliformis on Human Vascular Endothelial Cells and Involvement of GroEL. Infect. Immun. 71: 6933-6942 [Abstract] [Full Text]  
  • Belyi, I., Popoff, M. R., Cianciotto, N. P. (2003). Purification and Characterization of a UDP-Glucosyltransferase Produced by Legionella pneumophila. Infect. Immun. 71: 181-186 [Abstract] [Full Text]  
  • Long, K. H., Gomez, F. J., Morris, R. E., Newman, S. L. (2003). Identification of Heat Shock Protein 60 as the Ligand on Histoplasma capsulatum That Mediates Binding to CD18 Receptors on Human Macrophages. J. Immunol. 170: 487-494 [Abstract] [Full Text]  
  • Faulkner, G., Garduno, R. A. (2002). Ultrastructural Analysis of Differentiation in Legionella pneumophila. J. Bacteriol. 184: 7025-7041 [Abstract] [Full Text]  
  • Garduno, R. A., Garduno, E., Hiltz, M., Hoffman, P. S. (2002). Intracellular Growth of Legionella pneumophila Gives Rise to a Differentiated Form Dissimilar to Stationary-Phase Forms. Infect. Immun. 70: 6273-6283 [Abstract] [Full Text]  
  • Hennequin, C., Porcheray, F., Waligora-Dupriet, A.-J., Collignon, A., Barc, M.-C., Bourlioux, P., Karjalainen, T. (2001). GroEL (Hsp60) of Clostridium difficile is involved in cell adherence. Microbiology 147: 87-96 [Abstract] [Full Text]  
  • Resto-Ruiz, S. I., Sweger, D., Widen, R. H., Valkov, N., Anderson, B. E. (2000). Transcriptional Activation of the htrA (High-Temperature Requirement A) Gene from Bartonella henselae. Infect. Immun. 68: 5970-5978 [Abstract] [Full Text]  
  • Zaborina, O., Misra, N., Kostal, J., Kamath, S., Kapatral, V., El-Idrissi, M. E.-A., Prabhakar, B. S., Chakrabarty, A. M. (1999). P2Z-Independent and P2Z Receptor-Mediated Macrophage Killing by Pseudomonas aeruginosa Isolated from Cystic Fibrosis Patients. Infect. Immun. 67: 5231-5242 [Abstract] [Full Text]  
  • Goulhen, F., Hafezi, A., Uitto, V.-J., Hinode, D., Nakamura, R., Grenier, D., Mayrand, D. (1998). Subcellular Localization and Cytotoxic Activity of the GroEL-Like Protein Isolated from Actinobacillus actinomycetemcomitans. Infect. Immun. 66: 5307-5313 [Abstract] [Full Text]  
  • Garduno, R. A., Garduno, E., Hoffman, P. S. (1998). Surface-Associated Hsp60 Chaperonin of Legionella pneumophila Mediates Invasion in a HeLa Cell Model. Infect. Immun. 66: 4602-4610 [Abstract] [Full Text]