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. 1991 Apr;59(4):1572–1575. doi: 10.1128/iai.59.4.1572-1575.1991

Heat shock response of spirochetes.

L V Stamm 1, F C Gherardini 1, E A Parrish 1, C R Moomaw 1
PMCID: PMC257880  PMID: 2004832

Abstract

We examined the heat shock response of the pathogenic spirochetes Treponema pallidum, Borrelia burgdorferi, and Leptospira interrogans and certain saprophytic spirochetes. Cellular proteins synthesized after shifts to higher temperatures were [35S]methionine labeled and analyzed by gel electrophoresis and fluorography. Only T. pallidum failed to exhibit an obvious heat shock response. GroEL and DnaK homologs were identified in the various species, although these proteins were not thermoinducible in T. pallidum or Treponema denticola. DNA hybridization studies indicate that spirochetal groEL and dnaK genes are highly conserved.

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Selected References

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

  1. Barbour A. G. Antigenic variation of a relapsing fever Borrelia species. Annu Rev Microbiol. 1990;44:155–171. doi: 10.1146/annurev.mi.44.100190.001103. [DOI] [PubMed] [Google Scholar]
  2. Barbour A. G. Isolation and cultivation of Lyme disease spirochetes. Yale J Biol Med. 1984 Jul-Aug;57(4):521–525. [PMC free article] [PubMed] [Google Scholar]
  3. Baseman J. B., Hayes N. S. Protein synthesis by Treponema pallidum extracted from infected rabbit tissue. Infect Immun. 1974 Dec;10(6):1350–1355. doi: 10.1128/iai.10.6.1350-1355.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Beckmann R. P., Mizzen L. E., Welch W. J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 1990 May 18;248(4957):850–854. doi: 10.1126/science.2188360. [DOI] [PubMed] [Google Scholar]
  5. Carreiro M. M., Laux D. C., Nelson D. R. Characterization of the heat shock response and identification of heat shock protein antigens of Borrelia burgdorferi. Infect Immun. 1990 Jul;58(7):2186–2191. doi: 10.1128/iai.58.7.2186-2191.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cluss R. G., Boothby J. T. Thermoregulation of protein synthesis in Borrelia burgdorferi. Infect Immun. 1990 Apr;58(4):1038–1042. doi: 10.1128/iai.58.4.1038-1042.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. ELLINGHAUSEN H. C., Jr, MCCULLOUGH W. G. NUTRITION OF LEPTOSPIRA POMONA AND GROWTH OF 13 OTHER SEROTYPES: FRACTIONATION OF OLEIC ALBUMIN COMPLEX AND A MEDIUM OF BOVINE ALBUMIN AND POLYSORBATE 80. Am J Vet Res. 1965 Jan;26:45–51. [PubMed] [Google Scholar]
  8. Fayet O., Louarn J. M., Georgopoulos C. Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes. Mol Gen Genet. 1986 Mar;202(3):435–445. doi: 10.1007/BF00333274. [DOI] [PubMed] [Google Scholar]
  9. Fields P. I., Swanson R. V., Haidaris C. G., Heffron F. Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5189–5193. doi: 10.1073/pnas.83.14.5189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fieldsteel A. H., Cox D. L., Moeckli R. A. Further studies on replication of virulent Treponema pallidum in tissue cultures of Sf1Ep cells. Infect Immun. 1982 Feb;35(2):449–455. doi: 10.1128/iai.35.2.449-455.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hansen K., Bangsborg J. M., Fjordvang H., Pedersen N. S., Hindersson P. Immunochemical characterization of and isolation of the gene for a Borrelia burgdorferi immunodominant 60-kilodalton antigen common to a wide range of bacteria. Infect Immun. 1988 Aug;56(8):2047–2053. doi: 10.1128/iai.56.8.2047-2053.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hedstrom R., Culpepper J., Harrison R. A., Agabian N., Newport G. A major immunogen in Schistosoma mansoni infections is homologous to the heat-shock protein Hsp70. J Exp Med. 1987 May 1;165(5):1430–1435. doi: 10.1084/jem.165.5.1430. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hemmingsen S. M., Woolford C., van der Vies S. M., Tilly K., Dennis D. T., Georgopoulos C. P., Hendrix R. W., Ellis R. J. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 1988 May 26;333(6171):330–334. doi: 10.1038/333330a0. [DOI] [PubMed] [Google Scholar]
  14. Hindersson P., Knudsen J. D., Axelsen N. H. Cloning and expression of treponema pallidum common antigen (Tp-4) in Escherichia coli K12. J Gen Microbiol. 1987 Mar;133(3):587–596. doi: 10.1099/00221287-133-3-587. [DOI] [PubMed] [Google Scholar]
  15. Hoffman P. S., Butler C. A., Quinn F. D. Cloning and temperature-dependent expression in Escherichia coli of a Legionella pneumophila gene coding for a genus-common 60-kilodalton antigen. Infect Immun. 1989 Jun;57(6):1731–1739. doi: 10.1128/iai.57.6.1731-1739.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Houston L. S., Cook R. G., Norris S. J. Isolation and characterization of a Treponema pallidum major 60-kilodalton protein resembling the groEL protein of Escherichia coli. J Bacteriol. 1990 Jun;172(6):2862–2870. doi: 10.1128/jb.172.6.2862-2870.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lindquist S., Craig E. A. The heat-shock proteins. Annu Rev Genet. 1988;22:631–677. doi: 10.1146/annurev.ge.22.120188.003215. [DOI] [PubMed] [Google Scholar]
  18. Miao R., Fieldsteel A. H. Genetics of Treponema: relationship between Treponema pallidum and five cultivable treponemes. J Bacteriol. 1978 Jan;133(1):101–107. doi: 10.1128/jb.133.1.101-107.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Morrison R. P., Belland R. J., Lyng K., Caldwell H. D. Chlamydial disease pathogenesis. The 57-kD chlamydial hypersensitivity antigen is a stress response protein. J Exp Med. 1989 Oct 1;170(4):1271–1283. doi: 10.1084/jem.170.4.1271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Neidhardt F. C., VanBogelen R. A. Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem Biophys Res Commun. 1981 May 29;100(2):894–900. doi: 10.1016/s0006-291x(81)80257-4. [DOI] [PubMed] [Google Scholar]
  21. SAITO H., MIURA K. I. PREPARATION OF TRANSFORMING DEOXYRIBONUCLEIC ACID BY PHENOL TREATMENT. Biochim Biophys Acta. 1963 Aug 20;72:619–629. [PubMed] [Google Scholar]
  22. Sell S., Norris S. J. The biology, pathology, and immunology of syphilis. Int Rev Exp Pathol. 1983;24:203–276. [PubMed] [Google Scholar]
  23. Stamm L. V., Bassford P. J., Jr Cellular and extracellular protein antigens of Treponema pallidum synthesized during in vitro incubation of freshly extracted organisms. Infect Immun. 1985 Mar;47(3):799–807. doi: 10.1128/iai.47.3.799-807.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Stamm L. V., Kerner T. C., Jr, Bankaitis V. A., Bassford P. J., Jr Identification and preliminary characterization of Treponema pallidum protein antigens expressed in Escherichia coli. Infect Immun. 1983 Aug;41(2):709–721. doi: 10.1128/iai.41.2.709-721.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. 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]
  26. Zhou Y. N., Kusukawa N., Erickson J. W., Gross C. A., Yura T. Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32. J Bacteriol. 1988 Aug;170(8):3640–3649. doi: 10.1128/jb.170.8.3640-3649.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. van Eden W., Thole J. E., van der Zee R., Noordzij A., van Embden J. D., Hensen E. J., Cohen I. R. Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis. Nature. 1988 Jan 14;331(6152):171–173. doi: 10.1038/331171a0. [DOI] [PubMed] [Google Scholar]

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