Skip to main content
NCBI home page
Infectious Diseases in Obstetrics and Gynecology logoLink to Infectious Diseases in Obstetrics and Gynecology
. 1999;7(1-2):58–63. doi: 10.1155/S1064744999000125

Surface-associated heat shock proteins of Legionella pneumophila and Helicobacter pylori: roles in pathogenesis and immunity.

P S Hoffman 1, R A Garduno 1
PMCID: PMC1784713  PMID: 10231011

Abstract

Bacterial heat shock proteins (Hsps) are abundantly produced during the course of most microbial infections and are often targeted by the mammalian immune response. While Hsps have been well characterized for their roles in protein folding and secretion activities, little attention has been given to their participation in pathogenesis. In the case of Legionella pneumophila, an aquatic intracellular parasite of protozoa and cause of Legionnaires' disease, Hsp60 is uniquely located in the periplasm and on the bacterial surface. Surface-associated Hsp60 promotes attachment and invasion in a HeLa cell model and may alter an early step associated with the fusion of phagosomes with lysosomes. Avirulent strains of L. pneumophila containing defined mutations in several dot/icm genes are defective in localizing Hsp60 onto their surface and are reduced approximately 1000-fold in their invasiveness towards HeLa cells. For the ulcer-causing bacterium Helicobacter pylori, surface-associated Hsp60 and Hsp70 mediate attachment to gastric epithelial cells. The increased expression of these Hsps following acid shock correlates with both increased association with and inflammation of the gastric mucosa. A role for Hsps in colonization, mucosal infection and in promoting inflammation is discussed.

Full Text

The Full Text of this article is available as a PDF (815.3 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews H. L., Vogel J. P., Isberg R. R. Identification of linked Legionella pneumophila genes essential for intracellular growth and evasion of the endocytic pathway. Infect Immun. 1998 Mar;66(3):950–958. doi: 10.1128/iai.66.3.950-958.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Benkirane R., Guinet R., Delaunay T. Purification and immunological studies of the cross-reaction between the 65-kilodalton gonococcal parietal lectin and an antigen common to a wide range of bacteria. Infect Immun. 1992 Aug;60(8):3468–3471. doi: 10.1128/iai.60.8.3468-3471.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bockova J., Elias D., Cohen I. R. Treatment of NOD diabetes with a novel peptide of the hsp60 molecule induces Th2-type antibodies. J Autoimmun. 1997 Aug;10(4):323–329. doi: 10.1006/jaut.1997.0150. [DOI] [PubMed] [Google Scholar]
  4. Domeika M., Domeika K., Paavonen J., Mårdh P. A., Witkin S. S. Humoral immune response to conserved epitopes of Chlamydia trachomatis and human 60-kDa heat-shock protein in women with pelvic inflammatory disease. J Infect Dis. 1998 Mar;177(3):714–719. doi: 10.1086/514218. [DOI] [PubMed] [Google Scholar]
  5. Fernandez R. C., Logan S. M., Lee S. H., Hoffman P. S. Elevated levels of Legionella pneumophila stress protein Hsp60 early in infection of human monocytes and L929 cells correlate with virulence. Infect Immun. 1996 Jun;64(6):1968–1976. doi: 10.1128/iai.64.6.1968-1976.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Frisk A., Ison C. A., Lagergård T. GroEL heat shock protein of Haemophilus ducreyi: association with cell surface and capacity to bind to eukaryotic cells. Infect Immun. 1998 Mar;66(3):1252–1257. doi: 10.1128/iai.66.3.1252-1257.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Garduño R. A., Faulkner G., Trevors M. A., Vats N., Hoffman P. S. Immunolocalization of Hsp60 in Legionella pneumophila. J Bacteriol. 1998 Feb;180(3):505–513. doi: 10.1128/jb.180.3.505-513.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Garduño R. A., Garduño E., Hoffman P. S. Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model. Infect Immun. 1998 Oct;66(10):4602–4610. doi: 10.1128/iai.66.10.4602-4610.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Garduño R. A., Quinn F. D., Hoffman P. S. HeLa cells as a model to study the invasiveness and biology of Legionella pneumophila. Can J Microbiol. 1998 May;44(5):430–440. [PubMed] [Google Scholar]
  10. Huesca M., Borgia S., Hoffman P., Lingwood C. A. Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization. Infect Immun. 1996 Jul;64(7):2643–2648. doi: 10.1128/iai.64.7.2643-2648.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Huesca M., Goodwin A., Bhagwansingh A., Hoffman P., Lingwood C. A. Characterization of an acidic-pH-inducible stress protein (hsp70), a putative sulfatide binding adhesin, from Helicobacter pylori. Infect Immun. 1998 Sep;66(9):4061–4067. doi: 10.1128/iai.66.9.4061-4067.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kaufmann S. H. Heat shock proteins and the immune response. Immunol Today. 1990 Apr;11(4):129–136. doi: 10.1016/0167-5699(90)90050-j. [DOI] [PubMed] [Google Scholar]
  13. Kligman I., Jeremias J., Rosenwaks Z., Witkin S. S. Cell-mediated immunity to human and Escherichia coli 60-kDa heat shock protein in women: association with a history of spontaneous abortion and endometriosis. Am J Reprod Immunol. 1998 Jul;40(1):32–36. doi: 10.1111/j.1600-0897.1998.tb00385.x. [DOI] [PubMed] [Google Scholar]
  14. Macellaro A., Tujulin E., Hjalmarsson K., Norlander L. Identification of a 71-kilodalton surface-associated Hsp70 homologue in Coxiella burnetii. Infect Immun. 1998 Dec;66(12):5882–5888. doi: 10.1128/iai.66.12.5882-5888.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Phadnis S. H., Parlow M. H., Levy M., Ilver D., Caulkins C. M., Connors J. B., Dunn B. E. Surface localization of Helicobacter pylori urease and a heat shock protein homolog requires bacterial autolysis. Infect Immun. 1996 Mar;64(3):905–912. doi: 10.1128/iai.64.3.905-912.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Retzlaff C., Yamamoto Y., Okubo S., Hoffman P. S., Friedman H., Klein T. W. Legionella pneumophila heat-shock protein-induced increase of interleukin-1 beta mRNA involves protein kinase C signalling in macrophages. Immunology. 1996 Oct;89(2):281–288. doi: 10.1046/j.1365-2567.1996.d01-735.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Segal G., Shuman H. A. How is the intracellular fate of the Legionella pneumophila phagosome determined? Trends Microbiol. 1998 Jul;6(7):253–255. doi: 10.1016/s0966-842x(98)01308-0. [DOI] [PubMed] [Google Scholar]
  18. Skeen M. J., Miller M. A., Shinnick T. M., Ziegler H. K. Regulation of murine macrophage IL-12 production. Activation of macrophages in vivo, restimulation in vitro, and modulation by other cytokines. J Immunol. 1996 Feb 1;156(3):1196–1206. [PubMed] [Google Scholar]
  19. Yamaguchi H., Osaki T., Kurihara N., Taguchi H., Hanawa T., Yamamoto T., Kamiya S. Heat-shock protein 60 homologue of Helicobacter pylori is associated with adhesion of H. pylori to human gastric epithelial cells. J Med Microbiol. 1997 Oct;46(10):825–831. doi: 10.1099/00222615-46-10-825. [DOI] [PubMed] [Google Scholar]
  20. Young D., Lathigra R., Hendrix R., Sweetser D., Young R. A. Stress proteins are immune targets in leprosy and tuberculosis. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4267–4270. doi: 10.1073/pnas.85.12.4267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Young R. A., Elliott T. J. Stress proteins, infection, and immune surveillance. Cell. 1989 Oct 6;59(1):5–8. doi: 10.1016/0092-8674(89)90861-1. [DOI] [PubMed] [Google Scholar]
  22. van der Zee R., Anderton S. M., Prakken A. B., Liesbeth Paul A. G., van Eden W. T cell responses to conserved bacterial heat-shock-protein epitopes induce resistance in experimental autoimmunity. Semin Immunol. 1998 Feb;10(1):35–41. doi: 10.1006/smim.1997.0103. [DOI] [PubMed] [Google Scholar]

Articles from Infectious Diseases in Obstetrics and Gynecology are provided here courtesy of Wiley

RESOURCES