Mycobacterium tuberculosis chaperonin 10 stimulates bone resorption: A potential contributory factor in Pott's disease

Journal of Experimental Medicine

Volumn 186, Issue 8, 1997, Pages 1241-1246

  Meghji, Sajeda ^a   White, Peter A ^a   Nair, Sean P ^a   Reddi, Krisanavane ^a   Heron, Kyle ^a   Henderson, Brian ^a   Zaliani, Andrea ^b   Fossati, Gianluca ^c   Mascagni, Paolo ^b   Hunt, John F ^d   Roberts, Michael M ^e   Coates, Anthony R M ^e  

^a UNIVERSITY COLLEGE LONDON   (United Kingdom)

^b Italfarmaco SpA   (Italy)

^c NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^d UNIVERSITY OF TEXAS AT DALLAS   (United States)

^e ST GEORGE'S UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; CALCIUM; CHAPERONIN; HEAT SHOCK PROTEIN; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DOSE RESPONSE; MICROSCOPY; MOUSE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OSTEOBLAST; OSTEOCLAST; OSTEOLYSIS; PRIORITY JOURNAL; TUBERCULOUS SPONDYLITIS;

AMINO ACID SEQUENCE; ANIMALS; BONE RESORPTION; CALCIUM; CELL LINE; CHAPERONIN 10; DOSE-RESPONSE RELATIONSHIP, DRUG; GROWTH INHIBITORS; HUMANS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; ORGAN CULTURE TECHNIQUES; OSTEOBLASTS; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; RECOMBINANT PROTEINS; SKULL; SONICATION; TUBERCULOSIS, SPINAL;

EID: 0030728057     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.186.8.1241     Document Type: Article

References (28)

1. Murray, C.J., K. Styblo, and A. Rouillon. 1990. Tuberculosis in developing countries: burden, intervention and cost. Bull. Int. Union. Tuberc, Lung Dis. 65:6-24.
2. Boachie-Adjei, O., and R.G. Squillante. Tuberculosis of the spine. 1996. Orthop. Clin. North Am. 27:95-103.
3. Nair, S.P., S. Meghji, M. Wilson, K. Reddi, P. White, and B. Henderson. 1996. Bacterially induced bone destruction: mechanisms and misconceptions. Infect. Immun. 64:2371-2380.
4. Fenton, M.J., and M.W. Vermeulen. 1996. Immunopathology of tuberculosis: roles of macrophages and monocytes. Infect. Immun. 64:683-690.
5. Coates, A.R.M. 1996. Immunology of chaperonins. In The Chaperonins. R.J. Ellis, editor. Academic Press, London. 267-296.
6. Cavanagh, A.C., and H. Morton. 1994. The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10. Eur. J. Biochem. 222:551-560.
7. Beagley, K.W., K. Fujihashi, C.A. Black, A.S. Lagoo, M. Yamamoto, J.R. McGhee, and H. Kiyono. 1993. The Mycobacterium tuberculosis 71-kDa heat-shock protein induces proliferation and cytokine secretion by murine gut intraepithelial lymphocytes. Eur. J. Imnitinol. 23:2049-2052.
8. Kirby, A.C., S. Meghji, S.P. Nair, P. White, K. Reddi, T. Nishihara, K. Nakashima, A.C. Willis, R. Sim, M. Wilson, and B. Henderson. 1995. The potent bone-resorbing mediator of Actinobacillus actinomycetemcomitans is homologous to the molecular chaperone GroEL. J. Clin. Invest. 96:1185-1194.
9. Baird, P.N., L.M. Hall, and A.R.M. Coates. 1989. Cloning and sequence analysis of the 10K antigen gene of Mycobacterium tuberculosis. J. Gen. Microbiol. 135:931-939.
10. Seckinger, P., J. Klein-Nulend, C. Alander, R.C. Thompson, J.M. Dayer, and L.G. Raisz. 1990. Natural and recombinant human IL-1 receptor antagonists block the effects of IL-1 on bone resorption and prostaglandin production. J. Immunol. 145:4181-4184.
11. Chambers, T.J., P.M. McSheehy, B.M. Thomson, and K. Fuller. 1985. The effect of calcium-regulating hormones and prostaglandins on bone resorption by osteoclasts disaggregated from neonatal rabbit bones. Endocrinology. 116:234-239.
12. Minden, P., P.J. Kelleher, J.H. Freed, L.D. Nielsen, P.J. Brennan, L. McPheron, and J.K. McClatchy. 1984. Immunological evaluation of a component isolated from Mycobacterium bovis BCG with a monoclonal antibody to M. bovis BCG. Infect. Immun. 46:519-525.
13. Coates, A.R.M., J. Hewitt, B.W. Allen, J. Ivanyi, and D.A. Mitchison. 1981. Antigenic diversity of Mycobacterium tuberculosis and Mycobacterium bovis detected by means of monoclonal antibodies. Lancet. 2:167-169.
14. Coates, A.R.M., H. Nicolai, M.J. Pallen, A. Guy, S.D. Chaparas, and D.A. Mitchison. 1989. The 45 kilodalton molecule of Mycobacterium tuberculosis identified by immunoblotting and monoclonal antibodies as antigenic in patients with tuberculosis. Br. J. Exp. Pathol. 70:215-225.
15. Chatterjee, D., K. Lowell, B. Rivoire, M.R. McNeil, and P.J. Brennan. 1992. Lipoarabinomannan of Mycobacterium tu7 berculosis: capping with mannosyl residues in some strains. J. Biol. Chem. 267:6234-6239.
16. Fossati, G., P. Lucietto, P. Giuliani, A.R.M. Coates, S. Harding, H. Colfen, G. Legname, E. Chan, A. Zaliani, and P. Mascagni. 1995. Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures: implications for its diverse biological activities. J. Biol. Chem. 270: 26159-26167.
17. Lucietto, P., G. Fossati, H.L. Ball, P. Giuliani, and P. Mascagni. 1997. M. tuberculosis chaperonin 10 and N-truncated fragments. Their synthesis and purification by the isoelectric focusing technique carried out in solution. J. Pept. Res. 49: 308-323.
18. Nair, S., Y. Song, S. Meghji, K. Reddi, M. Harris, A. Ross, S. Poole, M. Wilson, and B. Henderson. 1995. Surface-associated proteins from Staphylococcus aureus demonstrate potent bone resorbing activity. J. Bone Miner. Res. 10:726-734.
19. Gitelman, H.J. 1967. An approved automated procedure for the determination of calcium in biological specimens. Anal. Biochem. 18:521-531.
20. Marshall, M.J., I. Holt, and M.W. Davie. 1995. The number of tartrate-resistant acid phosphatase-positive osteoclasts on neonatal mouse parietal bones is decreased when prostaglandin synthesis is inhibited and increased in response to prostaglandin E2, parathyroid hormone, and 1,25 dihydroxyvitamin D3. Calcif. Tissue Int. 56:240-245.
21. White, P.A., M. Wilson, S.P. Nair, A.C. Kirby, K. Reddi, and B. Henderson. 1995. Characterization of an antiproliferative surface-associated protein from Actinobacillus actinomycetemcomitans which can be neutralized by sera from a proportion of patients with localized juvenile periodontids. Infect. Immun. 63:2612-2618.
22. Orme, I.M., E.S. Miller, A.D. Roberts, S.K. Furney, J.P. Griffin, K.M. Dobos, D. Chi, B. Rivoire, and P.J. Brennan. 1992. T lymphocytes mediating protection and cellular cytolysis during the course of Mycobacterium tuberculosis infection. J. Immunol. 148:189-196.
23. Hunt, J.F., A.J. Weaver, S.J. Landry, L. Gierasch, and J. Deisenhofer. 1996. The crystal structure of the GroES co-chaperonin at 2.8Å resolution. Nature (Lond.). 379:37-45.
24. Chan, E., G. Fossati, P. Giuliani, P. Lucietto, A. Zaliani, A.R.M. Coates, and P. Mascagni. 1995. Sequence and structural homologies between M. tuberculosis chaperonin 10 and the MHC class I/II peptide binding cleft. Biochem. Biophys. Res. Commun. 211:14-20.
25. Zondlo, J., K.E. Fisher, Z. Liu, K.R. Ducote, and E. Eisenstein. 1995. Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES. Biochemistry. 34:10334-10339.
26. Landry, S.J., J. Zeilstra-Ryalls, O. Fayet, C. Georgopoulos, and L.M. Gierasch. 1993. Characterization of a functionally important mobile domain of GroES. Nature (Lond.). 364: 255-258.
27. Saibil, H. 1996. The lid that shapes the pot: structure and function of the chaperonin GroES. Structure (Lond.). 4:1-4.
28. Soltys, B.J., and R.S. Gupta. 1996. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222:16-27.