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 Belles, C.
Right arrow Articles by Carding, S. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belles, C.
Right arrow Articles by Carding, S. R.

 Previous Article  |  Next Article 

Infection and Immunity, August 1999, p. 4191-4200, Vol. 67, No. 8
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Plasma Membrane Expression of Heat Shock Protein 60 In Vivo in Response to Infection

Cindy Belles, Alicia Kuhl,dagger Rachel Nosheny, and Simon R. Carding*

Department of Clinical Studies, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6010

Received 4 February 1999/Returned for modification 29 March 1999/Accepted 16 April 1999

Heat shock protein 60 (hsp60) is constitutively expressed in the mitochondria of eukaryotic cells. However, it has been identified in other subcellular compartments in several disease states and in transformed cells, and it is an immunogenic molecule in various infectious and autoimmune diseases. To better understand the factors that influence expression of hsp60 in normal cells in vivo, we analyzed its cellular and subcellular distribution in mice infected with the intracellular bacterium Listeria monocytogenes. Western blotting of subcellular fractionated spleen cells showed that although endogenous hsp60 was restricted to the mitochondria in noninfected animals, it was associated with the plasma membrane as a result of infection. The low levels of plasma membrane-associated hsp60 seen in the livers in noninfected animals subsequently increased during infection. Plasma membrane hsp60 expression did not correlate with bacterial growth, being most evident during or after bacterial clearance and persisting at 3 weeks postinfection. Using flow cytometry, we determined that Mac-1+, T-cell receptor gamma delta +, and B220+ cells represented the major Hsp60+ populations in spleens of infected mice. By contrast, B220+ cells were the predominant hsp60+ population in livers of infected mice. Of the immune cells analyzed, the kinetic profile of the gamma delta T-cell response most closely matched that of hsp60 expression in both the spleen and liver. Collectively, these findings show that during infection hsp60 can be localized to the plasma membrane of viable cells, particularly antigen-presenting cells, providing a means by which hsp60-reactive lymphocytes seen in various infectious disease and autoimmune disorders may be generated and maintained.

* Corresponding author. Mailing address: Department of Clinical Studies, University of Pennsylvania School of Veterinary Medicine, 3900 Delancy St., Philadelphia, PA 19104-6010. Phone: (215) 573-3022. Fax: (215) 573-6168. E-mail: carding{at}vet.upenn.edu.

dagger Present address: University of Colorado Health Science Center, Denver, CO 80262.

Infection and Immunity, August 1999, p. 4191-4200, Vol. 67, No. 8
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Osterloh, A., Geisinger, F., Piedavent, M., Fleischer, B., Brattig, N., Breloer, M. (2009). Heat shock protein 60 (HSP60) stimulates neutrophil effector functions. J. Leukoc. Biol. 86: 423-434 [Abstract] [Full Text]  
  • Hirsh, M. I., Junger, W. G. (2008). Roles of Heat Shock Proteins and {gamma}{delta}T Cells in Inflammation. Am. J. Respir. Cell Mol. Bio. 39: 509-513 [Abstract] [Full Text]  
  • Walsh, A., Whelan, D., Bielanowicz, A., Skinner, B., Aitken, R. J., O'Bryan, M. K., Nixon, B. (2008). Identification of the Molecular Chaperone, Heat Shock Protein 1 (Chaperonin 10), in the Reproductive Tract and in Capacitating Spermatozoa in the Male Mouse. Biol. Reprod. 78: 983-993 [Abstract] [Full Text]  
  • Osterloh, A., Veit, A., Gessner, A., Fleischer, B., Breloer, M. (2008). Hsp60-mediated T cell stimulation is independent of TLR4 and IL-12. Int Immunol 20: 433-443 [Abstract] [Full Text]  
  • Kettner, S., Kalthoff, F., Graf, P., Priller, E., Kricek, F., Lindley, I., Schweighoffer, T. (2007). EWI-2/CD316 Is an Inducible Receptor of HSPA8 on Human Dendritic Cells. Mol. Cell. Biol. 27: 7718-7726 [Abstract] [Full Text]  
  • Lin, L., Kim, S. C., Wang, Y., Gupta, S., Davis, B., Simon, S. I., Torre-Amione, G., Knowlton, A. A. (2007). HSP60 in heart failure: abnormal distribution and role in cardiac myocyte apoptosis. Am. J. Physiol. Heart Circ. Physiol. 293: H2238-H2247 [Abstract] [Full Text]  
  • Osterloh, A., Kalinke, U., Weiss, S., Fleischer, B., Breloer, M. (2007). Synergistic and Differential Modulation of Immune Responses by Hsp60 and Lipopolysaccharide. J. Biol. Chem. 282: 4669-4680 [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]  
  • Andrew, E. M., Newton, D. J., Dalton, J. E., Egan, C. E., Goodwin, S. J., Tramonti, D., Scott, P., Carding, S. R. (2005). Delineation of the Function of a Major {gamma}{delta} T Cell Subset during Infection. J. Immunol. 175: 1741-1750 [Abstract] [Full Text]  
  • Bredberg, A., Henriksson, G., Larsson, A., Manthorpe, R., Sallmyr, A. (2005). Sjogren's syndrome and the danger model. Rheumatology (Oxford) 44: 965-970 [Full Text]  
  • Pfister, G., Stroh, C. M., Perschinka, H., Kind, M., Knoflach, M., Hinterdorfer, P., Wick, G. (2005). Detection of HSP60 on the membrane surface of stressed human endothelial cells by atomic force and confocal microscopy. J. Cell Sci. 118: 1587-1594 [Abstract] [Full Text]  
  • Johnson, B. J., Le, T. T. T., Dobbin, C. A., Banovic, T., Howard, C. B., Flores, F. d. M. L., Vanags, D., Naylor, D. J., Hill, G. R., Suhrbier, A. (2005). Heat Shock Protein 10 Inhibits Lipopolysaccharide-induced Inflammatory Mediator Production. J. Biol. Chem. 280: 4037-4047 [Abstract] [Full Text]  
  • Wampler, J. L., Kim, K.-P., Jaradat, Z., Bhunia, A. K. (2004). Heat Shock Protein 60 Acts as a Receptor for the Listeria Adhesion Protein in Caco-2 Cells. Infect. Immun. 72: 931-936 [Abstract] [Full Text]  
  • Michaelsson, J., Teixeira de Matos, C., Achour, A., Lanier, L. L., Karre, K., Soderstrom, K. (2002). A Signal Peptide Derived from hsp60 Binds HLA-E and Interferes with CD94/NKG2A Recognition. JEM 196: 1403-1414 [Abstract] [Full Text]  
  • Ranford, J C, Henderson, B (2002). Chaperonins in disease: mechanisms, models, and treatments. Mol. Pathol. 55: 209-213 [Abstract] [Full Text]  
  • Moore, B.B., Moore, T.A., Toews, G.B. (2001). Role of T- and B-;lymphocytes in pulmonary host defences. Eur Respir J 18: 846-856 [Abstract] [Full Text]  
  • Rook, G.A.W., Seah, G., Ustianowski, A. (2001). M. tuberculosis: immunology and vaccination. Eur Respir J 17: 537-557 [Abstract] [Full Text]  
  • Dziewanowska, K., Carson, A. R., Patti, J. M., Deobald, C. F., Bayles, K. W., Bohach, G. A. (2000). Staphylococcal Fibronectin Binding Protein Interacts with Heat Shock Protein 60 and Integrins: Role in Internalization by Epithelial Cells. Infect. Immun. 68: 6321-6328 [Abstract] [Full Text]  
  • Egan, P. J., Carding, S. R. (2000). Downmodulation of the Inflammatory Response to Bacterial Infection by {gamma}{delta} T Cells Cytotoxic for Activated Macrophages. JEM 191: 2145-2158 [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»