Dissection of relationship between small heat shock proteins and mycobacterial diseases

Indian Journal of Leprosy

Volumn 80, Issue 3, 2008, Pages 231-245

  Jee, B ^a,b   Katoch, V M ^a   Awasthi, S K ^b  

^a GOVERNMENT OF INDIA   (India)

^b CSJM UNIVERSITY   (India)

Author keywords

Acr2; Mycobacterial diseases; Small heat shock proteins; sSHP 16.3

Indexed keywords

ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; ALPHA CRYSTALLIN; ALPHA CRYSTALLIN RELATED PROTEIN 1; ALPHA CRYSTALLIN RELATED PROTEIN 2; ANTIGEN; ANTIGEN 18 KD; CHAPERONE; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 65; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; MEMBRANE PROTEIN; PROTEINASE; REGULATOR PROTEIN; SMALL HEAT SHOCK PROTEIN; SMALL HEAT SHOCK PROTEIN 16.3; UNCLASSIFIED DRUG; ALPHA CRYSTALLIN 2, MYCOBACTERIUM TUBERCULOSIS; ALPHA-CRYSTALLIN 2, MYCOBACTERIUM TUBERCULOSIS; BACTERIAL PROTEIN; CHAPERONIN; HSP16.3 PROTEIN, MYCOBACTERIUM TUBERCULOSIS;

AUTOIMMUNITY; BACTERIAL SURVIVAL; DISEASE ASSOCIATION; DRUG TARGETING; IMMUNE RESPONSE; IMMUNOMODULATION; INFLAMMATION; MOLECULAR WEIGHT; MYCOBACTERIOSIS; MYCOBACTERIUM AVIUM; MYCOBACTERIUM INTRACELLULARE; MYCOBACTERIUM LEPRAE; NONHUMAN; PATHOGENICITY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; SERODIAGNOSIS; ANIMAL; CHEMISTRY; HUMAN; IMMUNOLOGY; PHYSIOLOGY;

ALPHA-CRYSTALLINS; ANIMALS; BACTERIAL PROTEINS; CHAPERONINS; HEAT-SHOCK PROTEINS, SMALL; HUMANS; MYCOBACTERIUM INFECTIONS;

EID: 65649101835     PISSN: 02549395     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (89)

1. Abou-Zeid C, Smith I, Grange JMet al (1988). The secreted antigens of Mycobacterium tuberculosis and their relationship to those recognized by the available antibodies. J Gen Microbiol. 134: 531-538.
2. Abulimiti A, Fu X, Gu L et al (2003). Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-assembled via trimer and hexamer intermediates. J Mol Biol. 326: 1013-1023.
3. Adams E, Basten A, Prestidge R et al (1995). T cell clones from a nonleprosy exposed subject recognize the Mycobacterium leprae 18-kDprotein. Clin Exp Immunol. 102: 58-64.
4. Augusteyn RC (2004). α-crystallin: a reviewof its structure and function. Clin Exp Optom. 87: 356-366.
5. Beck ST, Leite OM, Arroda RS et al (2005). Humoral response to low molecular weight antigens of Mycoabcetrium tuberculosis by tuberculosis patients and contacts. Braz J Med Biol Res. 38: 587-596.
6. Booth RJ, Williams DL, Moudgil KD et al (1993). Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium tuberculosis 19-kilodalton antigens in other mycobacteria. Infect Immun. 61: 1509-1515.
7. Brady JP, Garland D, Duglas-Tabor Y et al (1997). Targeted disruption of the mouse αA-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein αB-crystallin. Proc Natl Acad Sci USA. 94: 884-889.
8. Bruey JM, Ducasse C, Bonniaud P et al (2000). Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol. 2: 645-652.
9. Chang Z, Primm TP, Jakana J et al (1996). Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as anoligomeric structure in vitro to suppress thermal aggregation. J Biol Chem. 271: 7218-7223.
10. Cole ST, Borsch R, Parkhill J et al (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393: 537-544.
11. Cole ST, Eiglmeier K, Parkhill J et al (2001). Massive gene decay in the leprosy bacillus. Nature. 409: 1007-1011.
12. Cunningham AF and Spreadbury CL (1998). Mycobacterial stationary phase induced by low oxygen tension: cell wall thickening and localization of the 16-kilodalton α-crystallin homolog. J Bacteriol. 180: 801-808.
13. Dannenberg AM Jr (1993). Immunopathogenesis of pulmonary tuberculosis. Host Pract (OffEd). 28: 51-58.
14. Dasgupta N, Kapur V, Singh KK et al (2000). Characterization of a two-component system, devR-devS, of Mycobacteriun tuberculosis. Tuberc Lung Dis. 80: 141-159.
15. de Jong WW, Leunissen JAM and Vooter CEM (1993). Evolutuion of the α-crystallin/small heat-shock protein family. Mol Biol Evol. 10: 103-126.
16. Desjardin LE, Hayes LG, Sohaskey CD et al (2001). Microaerophilic induction of the alpha- crys ta llin chape rone prote in homologue (hspX) mRNA of Mycobacterium tuberculosis. J Bacteriol. 183: 5311-5316.
17. Dickinson JM and Mitchison DA (1981). Experimental models to explain the high sterlizing activity of rifampin in the chemotherapy of tuberculosis. Am Rev Respir Dis. 123: 367-371.
18. Euzeby JP (2008). List of bacterial names with standing in nomenclature-Genus Mycobacterium. http://www.bacterio.cict.fr/m/ mycobacterium.html. Last access on 17th May 2008.
19. Flynn JL and Chan J (2001). Immunology of tuberculosis. Annu Rev Immunol. 19: 93-129.
20. Fu X and Chang Z (2004).Temperaturedependent subunit exchange and chaperonelike activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis Biochem Biophys Res Commun. 316: 291-299.
21. Fu X, Liu C, Liu Y et al (2003). Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation. Biochem Biophys Res Commun. 310: 412-420.
22. Garbe TR, Hibler NS and Deretic V (1999). Response to reactive nitrogen intermediates in Mycobacterium tuberculosis : induction of the l6-kilodalton α-crystallin homolog by exposure to nitric oxide donors. Infect Immun. 67: 460-465.
23. Garnier T, Eiglmeier K, Camus JC et al (2003). The complete genome sequence of Mycobacterium bovis. Proc Natl Acad Sci USA. 100: 7877-7882.
24. Goodfellow M and Wayne LG (1982). Taxonomy andnomenclature. In:The Biology of Mycobacteria, Vol I. Physiology, Identification and Classification (Ratledge C and Stanford JL, Eds), Academic Press, London, pp417-521.
25. Holt JH, Krieg NR, Sneath PHA et al, Eds (1994). The mycobacteria. In : Bergey's Manual of Determinative Bacteriology, 9th edn, Lippincott Williams and Wilkins, Philadelphia, pp597-603.
26. Horwitz J (1992). Alpha-crystal1in can function as a molecular chaperone. Proc Natl Acad Sci USA. 89: 10449-10453.
27. Hu Y and Coates ARM (1999). Transcription of the stationary-phase- associated hspX gene of Mycobacterium tuberculosis is inversely related to synthesis of the 16-kilodalton protein. J Bacteriol. 181: 1380-1387.
28. Hu Y, Movahedzadeh F, Stoker NG et al (2006). Deletion of the Mycobacterium tuberculosis α-crystal1in-like hspX gene causes increased bacterial growth in vivo. Infect Immun. 74: 861-868.
29. Hussain R, Dockrell HM, Kifayet A et al (1992). Recognition of Mycobacterium leprae recombinant 18-kDa proteins in leprosy. Int J Lepr Other Mycobact Dis. 60: 368-375.
30. Jurcevic S,Hills A, Pasvol Get al (1996). T cell responses to a mixture of Mycobacterium tuberculosis peptides with complementary HLA-DR binding profiles. Clin Exp Immunol. 105: 416-421.
31. Katoch VM (2004). Infections due to nontuberculous mycobacterial. Indian J Med Res. 120: 209-304.
32. Katoch VM, Lavania M, Chauhan DS et al (2007). Environmental mycobacteria: friends and foes. Environ Biol Conserv. 12: 87-100.
33. Kennaway CK, Benesch JLP, Gohlke U et al (2005). Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis. J Biol Chem. 280: 33419-33425.
34. Kingston AE, Salgame PR, Mitchism NA et al (1987). Immunological activity of a 14-kilodalton recombinant protein of Mycobacterium tuberculosis H37Rv. Infect Immun. 55: 3149-3154.
35. Kolk AHJ, Evers R, Groothuis DG et al (1989). Production and characterization of monoclonal antibodies against specific serotypes of Mycobacterium avium and the Mycobacteriumavium-Mycobacterium intracellulare-Mycobacterium scrofulaceum complex. Infect Immun. 57: 2514-2521.
36. Lamb FI, Singh NB and Colston MJ (1990). The specific 18-kilodalton antigen of Mycobacterium leprae is present in Mycobacterium habana and functions as a heat-shock protein. J lmmunol. 144: 1922-1925.
37. Lee BY, Hefta SA and Brennan PJ (1992). Characterization of the major membrane protein of virulent Mycobacterium tuberculosis. Infect Immun. 60: 2066-2074.
38. Leroux MR, Milki R, Gordon B et al (1997). Structure-function studies on small heat shock protein oligomeric assembly and interactionwith unfolded polypeptides. J Biol Chem. 272: 24646-24656.
39. Lindquist S and Craig EA (1988). The heat shock proteins. Ann Rev Genet. 22: 631-677.
40. Macario AJL and de Macario EC (2005). Sick chaperones, cellular stress and disease. New Eng J Med. 353: 1489 -1501.
41. Manabe YC, Chen JM, Ko CG et al (1999). Conditional sigma factor expression using the inducible acetamidase promoter, reveals that the Mycobacterium tuberculosis sigF gene modulates expression of the 16-kilodalton α-crystallin homologue. J Bacteriol. 181: 7629-7633.
42. Manganelli R, Dubnau E, Tyagi S et al (1999). Differential expression of 10 sigma factor genes in Mycobacterium tuberculosis. Mol Microbiol. 31: 715-724.
43. Manganelli R, Proveddi R, Rodrigue S et al (2004). σ factors and global gene regulation in Mycobacterium tuberculosis. J Bacteriol. 186: 895-902.
44. E role in global gene expression and survival in macrophages. Mol Microbiol. 41: 423-437.
45. H in Mycobacterium tubetrculosis global gene expression. Mol Microbiol. 45: 365-374.
46. Mao Q, Ke D and Chang Z (2001). Electrostatic interactions play a critical role in Mycobacterium tuberculosis Hsp16.3 binding of substrate proteins. Biochemistry. 66: 904-908.
47. Mehra Y, Bloom BR, Bajardi AC et al (1992). Amajor T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein. J Exp Med. 175: 275-284.
48. Morimoto RI, TissieresA and Georgopopulos C, Eds (1990). Stress Proteins in Biology and Medicine. Cold Spring Harbor Laboratory, ColdSpringHarbor, NewYork.
49. Mornon JP, Halaby D, MalfoisM et al (1998). α-crystallin c-terminal domain: on the track of an Ig fold. Int J Biol Macromol. 22: 219-227.
50. Moudgil KD, Williams DL and Gillis TP (1992). DNA hybridisation analysis of mycobacterial DNA using the 18kDa protein gene of Mycobacterium leprae. FEMS Microbiol Lett. 89: 165-174.
51. Mustafa AS, Gill HK, Nerland A et al (1986). Human T-cell clones recognize a major M. leprae protein antigen expressed in E. coli. Nature (London). 319: 63-66.
52. Mustafa AS, Lundin KEA, Meloen RH et al (2000). Cross-reactive epitopes and HLA restriction elements in human T cell recognition of the Mycobacterium leprae 18-kD heat shock protein. Clin Exp Immunol. 120: 85-92.
53. Narberhaus F (2002). α-crystallin-type heat shock proteins: socializingminichaperones in the context of a multichaperones network. Microbiol Mol Biol Rev. 66: 64-93.
54. Nerland AH, Mustafa AS, Sweetser D et al (1988). A protein antigen of Mycobacterium leprae is related to a family of small heat shock proteins. J Bacteriol. 170: 5919-5921.
55. O'Toole R, Smeulders MJ, Blokpoel MC et al (2003). A two-component regulator of universal stress protein expression and adaptation to oxygen starvation in Mycobacterium smegmatis. J Bacteriol. 185: 1543-1554.
56. OharaN,OharaN,NaitoMet al (1997).HrpA, a new ribosome-associated protein which appears in heat-stressed Mycobacterium bovis Bacillus Calmette-Guerin. J Bacteriol. 179: 6495-6498.
57. Ohno H, Zhu G, Mohan VP et al (2003). The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol. 5: 637-648.
58. Orme IM, Andersen P and BoomWH (1993). T cell response to Mycobacterium tuberculosis. J Infect Dis. 167: 1481-1497.
59. Orme IM and Cooper AM (199 9) . Cytokine/chemokine cascades in immunity to tuberculosis. Immunol Today. 20: 307-312.
60. Pang X and Howard ST (2007). Regulation of the α-crystallin gene acr2 by the MprAB two-component system of Mycobacterium tubertculosis. J Bacteriol. 189: 6213-6221.
61. Parish T, Smith DA, Kendall S et al (2003). Deletion of two component regulatory system increases the virulence of Mycobacterium tuberculosis. Infect Immun. 71: 1134-1140.
62. PetersWand Ernst JD (2003). Mechanisms of cell recruitment in the immune response to Mycobacterium tuberculosis. Microbes Infect. 5: 151-158.
63. Raman S, Song T, Puyang X et al (2001). The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. J Bacteriol. 183: 6119-6125.
64. Rojas RE, Demichelis SO, Sarno EN et al (1997). IgManti-phenolic glycolipid I and IgG anti-10-kDa heat shock protein antibodies in sera and immune complexes isolated from leprosy patients with or without erythema nodosum leprosum and contacts. FEMS Immunol Med Microbiol. 19: 65-74.
65. Rook GAW and Hernandez-Pando R (1996). The pathogenesis of tuberculosis. Annu Rev Microbiol. 50: 259-284.
66. Runyon EH ( 1 9 5 9 ) . Annonymous mycobacteria in pulmonary disease. Med Clin North Amer. 43: 273-299.
67. Schnappinger D, Ehrt S, Voskuil MI et al (2003). Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J Exp Med. 198: 693-704.
68. Schoningh R, Verstijnen CP, Kuijper S et al (1990). Enzyme immunoassay for identification of heat-killed mycobacteria belonging to the Mycobacterium tuberculosis and Mycobacterium avium complexes and derived from early cultures. J Clin Microbiol. 28: 708-713.
69. Sherman DR, Voskuil MI, Schnappinger D et al (2001). Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding α-crystallin. Proc Natl Acad Sci USA. 98: 7534-7539.
70. Shimoji Y, Ng V, Matsumura K et al (1999). A 21-kDa surface protein of Mycobacterium leprae binds peripheral nerve laminin-2 and mediates Schwann cell invasion. Proc Natl Acad Sci USA. 96: 9857-9862.
71. Smith I (2003). Mycobacterium tuberculosis pathogenesis and molecular determinants of virulence. Clin Microbiol Rev. 16: 463-496.
72. Stewart GR, Wernisch L, Stabler R et at (2002). Dissection of the heat-shock response in Mycobacterium tuberculosis usingmutants and microarrays. Microbiology. 148: 3129-3138.
73. Stewart GR, Newton SM, Wilkinson KA et al (2005). The stress-responsive chaperone α-crystallin 2 is required for pathogenesis of Mycobacterium tuberculosis. Mol Microbiol. 55: 1127-1137.
74. Tappeiner G and Wolff K (1999). Tuberculosis and other mycobacterial infections. In: Fitzpatrick's Dermatology in General Medicine, 5th edn,Vol II (Freedberg IM, Eisen AZ, Wolff K et al, Eds), McGraw Hill, New York, pp 2274-2292.
75. Timm J, Kurepina N, Kreiswirth BN et al (2006). A multidrug-resistant, acr1-deficient clinical isolate of Mycobacterium tuberculosis is unimpaired for replication in macrophages. J Infect Dis. 193: 1703-1710.
76. Valdez MM, Clark JI, Wu GJS et al (2002). Functional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP16.3 and human αβ-crystallin. Eur J Biochem. 269: 1806-1813.
77. van Eden W, ed (2003). Heat Shock Proteins andInflammation,Birkhauser, Basel.
78. vanMontfortRLM, Basha E, FriedrichKLet al (2001). Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol. 8: 1025-1030.
79. Vega-Lopez F, Stoker NG, Locniskar MF et al (1988). Recognition ofmycobacterial antigens by sera from patients with leprosy. J Clin Microbiol. 26: 2474-2479.
80. Verbon A, Kuijper S, Jansen HM et al (1990). Antigens in culture supernatant of Mycobacterium tuberculosis: epitopes defined by monoclonal and human antibodies. J Gen Microbiol. 136: 955-964.
81. Verbon A, Hartskeerl RA, Schuitema A et al (1992). The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is related to the alpha-crystallin family of low-molecular-weight heat shock proteins. J Bacteriol. 174: 1352-1359.
82. Wayne LG (1994) . Dormancy of Mycobacterium tuberculosis and latency of disease. Eur J Clin Microbiol Infect Dis. 13: 908-914.
83. Walters SB, Dubnau E, Kolesnikova I et al (2006). The Mycobacterium tuberculosis PhoPR two-component system regulates genes essential for virulence and complex lipid biosysthesis. Mol Microbiol. 60: 312-330.
84. Wei J, Dahl JL, Moulder JW et al (2000). Identification of a Myocbacterium tuberculosis gene that enhances mycobacterial survival in macrophages. J Bacteriol. 182: 377-384.
85. Wilkinson RJ, Vordermeier HM, Wilkinson KA et al (1998). Peptide-specific T cell responses to Mycobacterium tuberculosis : clinical spectrum, compartmentalization, and effect of chemotherapy. J Infect Dis. 78: 760-768.
86. Wilkinson KA, Stewart GR, Newton SM et al (2005). Infection biology of a novel α-crystallin of Mycobacterium tuberculosis : Acr2. J Immunol. 174: 4237-4243.
87. Yang H, Huang S, Dai H et al (1999). The Mycobacterium tuberculosis small heat shock protein HSP16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity. Protein Sci. 8: 174-179.
88. Yuan Y, Crane DD and Barry CE 3rd (1996). Stationary phase-associated protein expression in Mycobacterium tuberculosis: function of themycobacterial alpha-crystallin homolog. J Bacteriol. 178: 4484-4492.
89. Yuan Y, Crane DD, Simpson RM et al (1998). The 16-kDa alpha-crystallin (Acr) protein of Mycobacterium tuberculosis is required for growth in macrophages. Proc Natl Acad Sci USA. 95: 9578-9583.