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Gene Review

hsp  -  heat shock protein

Mycobacterium tuberculosis H37Rv

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Disease relevance of hsp


High impact information on hsp

  • Established clones of mycobacteria-reactive gamma/delta+ T cells specifically recognized mycobacteria, but neither PPD nor hsp 65 [5].
  • The islet cell 64,000-Mr autoantigen and hsp 65 proteins were physiologically and immunocompetitively distinct [1].
  • From our analysis of arthritogenic T cell clone A2b, obtained from an arthritic Lewis rat and specific for the 180-188 epitope of mycobacterial 65-kDa heat-shock protein (hsp 65), the possible origin of AA was explained by the existence of a molecular mimicry of the 180-188 epitope with a cartilage-associated self antigen [6].
  • In conclusion, the early inflammatory stages of arteriosclerotic lesions induced by immunization with hsp 65 can regress in the absence of additional risk factors for atherosclerosis, such as a cholesterol rich diet [7].
  • RESULTS: Both adriamycin and infectious virus treatment of myocardial cells stimulated increased hsp expression [3].

Biological context of hsp

  • Ultraviolet irradiation of the virus prevents virus replication and failed to elicit hsp production in heart cells [3].
  • HLA-DR4-restricted T-cell epitopes from the mycobacterial 60,000 MW heat shock protein (hsp 60) do not map to the sequence homology regions with the human hsp 60 [8].
  • These observations suggest that the epitopes from the mycobacterial hsp 60 presented to T cells in the context of HLA-DR4 could be relevant to autoimmunity [8].
  • The amino acid sequence alignment of the PTB65K protein with the hsp-65K homologs revealed that the M. tuberculosis and M. leprae proteins each differed by 36 amino acid residues and that the M. avium 18 protein differed by 8 residues [9].
  • In this context, we isolated and sequenced the hsp-65K-encoding gene from our M. paratuberculosis PTB65K genomic library [9].

Anatomical context of hsp

  • Therefore, our studies examined serological immunity to islet cell hsp in humans with insulin-dependent diabetes (IDD) [1].
  • In summary, human resistant cells to tuberculosis respond to different classes of antigens, including constitutive cell wall proteins, secreted antigens, and hsp [10].
  • Removal of T gamma cells from peripheral blood lymphocytes resulted in significantly increased responses to PPD and to recombinant mycobacterial hsp 65 and hsp 70 antigens [11].
  • Identification of a novel B-cell epitope of restricted specificity on the hsp 65-kDa protein of Mycobacterium tuberculosis [12].

Associations of hsp with chemical compounds


Analytical, diagnostic and therapeutic context of hsp

  • However, the results from animal models as well as human studies suggest that the mycobacterial hsp 60 may induce T-cell-mediated autoimmune conditions [8].
  • T-cell responses to hsp 70 were easily generated by immunization with the purified chaperone alone, either after primary or secondary immunization [13].


  1. No evidence for serological autoimmunity to islet cell heat shock proteins in insulin dependent diabetes. Atkinson, M.A., Holmes, L.A., Scharp, D.W., Lacy, P.E., Maclaren, N.K. J. Clin. Invest. (1991) [Pubmed]
  2. Clinical value of the measurement of Mycobacterium tuberculosis specific antibody in pulmonary tuberculosis. Bothamley, G.H., Rudd, R., Festenstein, F., Ivanyi, J. Thorax (1992) [Pubmed]
  3. Heat-shock protein induction in adriamycin and picornavirus-infected cardiocytes. Huber, S.A. Lab. Invest. (1992) [Pubmed]
  4. Delayed-type hypersensitivity elicited by synthetic peptides complexed with Mycobacterium tuberculosis hsp 70. Roman, E., Moreno, C. Immunology (1997) [Pubmed]
  5. A large fraction of human peripheral blood gamma/delta + T cells is activated by Mycobacterium tuberculosis but not by its 65-kD heat shock protein. Kabelitz, D., Bender, A., Schondelmaier, S., Schoel, B., Kaufmann, S.H. J. Exp. Med. (1990) [Pubmed]
  6. T cell reactivity to an epitope of the mycobacterial 65-kDa heat-shock protein (hsp 65) corresponds with arthritis susceptibility in rats and is regulated by hsp 65-specific cellular responses. Hogervorst, E.J., Boog, C.J., Wagenaar, J.P., Wauben, M.H., Van der Zee, R., Van Eden, W. Eur. J. Immunol. (1991) [Pubmed]
  7. Regression of arteriosclerotic lesions induced by immunization with heat shock protein 65-containing material in normocholesterolemic, but not hypercholesterolemic, rabbits. Xu, Q., Kleindienst, R., Schett, G., Waitz, W., Jindal, S., Gupta, R.S., Dietrich, H., Wick, G. Atherosclerosis (1996) [Pubmed]
  8. HLA-DR4-restricted T-cell epitopes from the mycobacterial 60,000 MW heat shock protein (hsp 60) do not map to the sequence homology regions with the human hsp 60. Mustafa, A.S., Lundin, K.E., Meloen, R.H., Shinnick, T.M., Coulson, A.F., Oftung, F. Immunology (1996) [Pubmed]
  9. Nucleotide sequence analysis and seroreactivities of the 65K heat shock protein from Mycobacterium paratuberculosis. el-Zaatari, F.A., Naser, S.A., Engstrand, L., Burch, P.E., Hachem, C.Y., Whipple, D.L., Graham, D.Y. Clin. Diagn. Lab. Immunol. (1995) [Pubmed]
  10. Specificity of T cells in human resistance to Mycobacterium tuberculosis infection. Mendez-Samperio, P., Gonzalez-Garcia, L., Pineda-Fragoso, P.R., Ramos-Sanchez, E. Cell. Immunol. (1995) [Pubmed]
  11. Lymphocytes expressing Fc gamma receptors suppress antigen-induced proliferation in cells from guinea pigs infected with virulent Mycobacterium tuberculosis. Bartow, R.A., McMurray, D.N. Cell. Immunol. (1998) [Pubmed]
  12. Identification of a novel B-cell epitope of restricted specificity on the hsp 65-kDa protein of Mycobacterium tuberculosis. Rambukkana, A., Yong, S., Das, P.K. FEMS microbiology immunology. (1991) [Pubmed]
  13. Synthetic peptides non-covalently bound to bacterial hsp 70 elicit peptide-specific T-cell responses in vivo. Román, E., Moreno, C. Immunology (1996) [Pubmed]
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