Glucose-regulated stress proteins and antibacterial immunity

Trends in Microbiology

Volumn 11, Issue 11, 2003, Pages 519-526

  Rapp, Ulrike K ^a   Kaufmann, Stefan H E ^a  

^a MAX PLANCK INSTITUTE FOR INFECTION BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CHICKEN OVALBUMIN UPSTREAM PROMOTER TRANSCRIPTION FACTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; GLUCOSE; GLUCOSE REGULATED HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN; LEUCINE ZIPPER PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; AUTOIMMUNITY; CELL ACTIVITY; CELLULAR DISTRIBUTION; CELLULAR IMMUNITY; DRUG POTENCY; ENDOPLASMIC RETICULUM; GENE CONTROL; GENE STRUCTURE; GENETIC REGULATION; IMMUNITY; INFECTION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; REVIEW; TRANSCRIPTION REGULATION;

GALLUS GALLUS;

EID: 0242289417     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2003.09.001     Document Type: Review

References (63)

1. Suto R., Srivastava P.K. A mechanism for the specific immunogenicity of HSP-chaperoned peptides. Science. 269:1995;1585-1588.
2. Udono H., et al. Cellular requirements for tumor-specific immunity elicited by HSP: tumor rejection antigen gp96 primes CD8+ T-cells in vivo. Proc. Natl. Acad. Sci. U. S. A. 91:1994;3077-3081.
3. Srivastava P.K., et al. Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics. 39:1994;93-98.
4. Robert J., et al. Minor histocompatibility antigen specific MHC-restricted CD8 T cell responses elicited by HSP. J. Immunol. 168:2002;1697-1703.
5. Harmala L.A., et al. The adjuvant effects of Mycobacterium tuberculosis heat shock protein 70 result from the rapid and prolonged activation of antigen-specific CD8+ T cells in vivo. J. Immunol. 169:2002;5622-5629.
6. Liu D.W., et al. Recombinant adeno-associated virus expressing human papillomavirus type 16 E7 peptide DNA fused with heat shock protein DNA as a potential vaccine for cervical cancer. J. Virol. 74:2000;2888-2894.
7. Ciupitu A.M., et al. Immunization with a lymphocytic choriomeningitis virus peptide mixed with heat shock protein 70 results in protective antiviral immunity and specific cytotoxic T lymphocytes. J. Exp. Med. 187:1998;685-691.
8. Oglesbee M.J., et al. Role for heat shock proteins in the immune response to measles virus infection. Viral Immunol. 15:2002;399-416.
9. Lee A. The glucose regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26:2001;504-510.
10. Horwich A.L., et al. Protein folding takes shape. EMBO Rep. 2:2001;1068-1073.
11. Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 295:2002;1852-1858.
12. Meunier L., et al. A subset of chaperones and folding enzymes form multiprotein complexes in the ER to bind nascent proteins. Mol. Biol. Cell. 13:2002;4456-4469.
13. Patil C., Walter P. Intracellular signaling from the ER to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13:2001;349-356.
14. Ma Y., Hendershot L.M. The unfolding tale of the unfolded protein response. Cell. 107:2001;827-830.
15. Pahl H.L., Baeuerle P.A. A novel signal transduction pathway from the ER to the nucleus is mediated by transcription factor NFκB. EMBO J. 14:1995;2580-2588.
16. Brewer J.W., et al. A pathway distinct from the mammalian unfolded protein response regulates expression of ER chaperones in non-stressed cells. EMBO J. 16:1997;7207-7216.
17. Matzinger P. The danger model: a renewed sense of self. Science. 296:2002;301-305.
18. Lehner T., et al. Heat shock proteins generate beta-chemokines which function as innate adjuvants enhancing adaptive immunity. Eur. J. Immunol. 30:2000;594-603.
19. Basu S., et al. Necrotic but not apoptotic cell death releases HSP, which deliver a partial maturation signal to dendritic cells and activate the NFκB signaling pathway. Int. Immunol. 12:2000;1539-1546.
20. Berwin B., et al. Virally induced lytic cell death elicits the release of immunogenic Grp94/gp96. J. Biol. Chem. 276:2001;21083-21088.
21. Van Eden W., et al. Immunopotentiating heat shock proteins: negotiators between innate danger and control of autoimmunity. Vaccine. 21:2003;897-901.
22. Van Eden W., et al. Do HSP control the balance of T-cell regulation in inflammatory diseases? Immunol. Today. 19:1998;303-307.
23. Cobelens P.M., et al. Treatment of adjuvant induced arthritis by oral administration of Mycobacterial HSP65 during disease. Arthritis Rheum. 43:2000;2694-2702.
24. Van Eden W., et al. HSP T-Cell epitopes trigger a spreading regulatory control in a diversified arthritogenic T cell response. Immunol. Rev. 164:1998;169-174.
25. Menoret A., et al. An ER protein implicated in chaperoning peptides to MHC I is an aminopeptidase. J. Biol. Chem. 276:2001;33313-33318.
26. Liu E.S., Lee A.S. Common sets of nuclear factors binding to the conserved promoter sequence motif of two coordinately regulated ER protein genes, GRP 78 and GRP 94. Nucleic Acids Res. 19:1991;5425-5431.
27. Yoshida H., et al. Identification of the cis-acting ER stress response element responsible for transcriptional induction of mammalian Grps. Involvement of basic leucine zipper transcription factors. J. Biol. Chem. 273:1998;33741-33749.
28. Haze K., et al. Identification of the G13 (cAMP-response-element-binding protein-related protein) gene product related to ATF6 as a transcriptional activator of the mammalian unfolded protein response. Biochem. J. 355:2001;19-28.
29. Okada T., et al. Distinct roles of ATF6 and double-stranded RNA-activated Protein Kinase-Like Endoplasmic Reticulum Kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366:2002;585-594.
30. Yoshida H., et al. XBP-1 mRNA is induced by ATF6 and spliced by IRE-1 in response to ER stress to produce a highly active transcription factor. Cell. 107:2001;881-891.
31. Yoshida H., et al. ER stress-induced formation of transcription factor complex ERSF including NF-Y (CBF) and activating transcription factors 6α and 6β that activates the mammalian unfolded protein response. Mol. Cell. Biol. 21:2001;1239-1248.
32. Ma Y., et al. Two distinct signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 318:2002;1351-1365.
33. Shen X., et al. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell. 107:2001;893-903.
34. Kokame K., et al. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J. Biol. Chem. 276:2001;9199-9205.
35. Helmbrecht K., et al. Chaperones in cell cycle regulation and mitogenic signal transduction: a review. Cell Prolif. 33:2000;341-365.
36. Pockley A.G. Heat shock proteins as regulators of the immune response. Lancet. 362:2003;469-476.
37. Morimoto R.I. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:1998;3788-3796.
38. Nollen E.A., Morimoto R.I. Chaperoning signaling pathways: molecular chaperones as stress-sensing HSP. J. Cell Sci. 115:2002;2809-2816.
39. Wassenberg J., et al. Receptor mediated and fluid phase pathways for internalization of the ER HSP90 chaperone Grp94 in murine macrophages. J. Cell Sci. 112:1999;2167-2175.
40. Nakamura T., et al. HSP90, HSP70, and GADPH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290:2002;858-864.
41. Basu S., et al. CD91 is a common receptor for HSP gp96, HSP90, HSP70, and calreticulin. Immunity. 14:2001;303-313.
42. Binder R.J., et al. CD91: A receptor for HSP gp96. Nat. Immunol. 1:2000;151-155.
43. O'Riordan M., et al. Innate recognition of bacteria by a macrophage cytosolic surveillance pathway. Proc. Natl. Acad. Sci. U. S. A. 99:2002;13861-13866.
44. Asea A., et al. Novel signal transduction pathway utilized by extracellular HSP70: role of TLR2 and TLR4. J. Biol. Chem. 277:2002;15028-15034.
45. Vabulas R., et al. HSP70 as endogenous stimulus of the Toll/IL-1 receptor pathway. J. Biol. Chem. 277:2002;15107-15112.
46. Kirschning C.J., Schumann R.R. TLR2: Cellular sensor for microbial and endogenous molecular patterns. Curr. Top. Microbiol. Immunol. 270:2002;121-144.
47. Beg A. Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends Immunol. 23:2002;509-512.
48. Becker T., et al. CD40 an extracellular receptor for binding and uptake of HSP70 peptide complexes. J. Cell Biol. 158:2002;1277-1285.
49. Bulut Y., et al. Chlamydial HSP60 activates macrophages and endothelial cells through TLR 4 and MD2 in a MyD88-dependent pathway. J. Immunol. 168:2002;1435-1440.
50. Binder R.J., et al. Cutting Edge: HSP gp96 induces maturation and migration of CD11c+ cells in vivo. J. Immunol. 165:2000;6029-6035.
51. Wallin R.P.A., et al. HSP as activators of the innate immune system. Trends Immunol. 23:2002;130-135.
52. Wang Y., et al. Stimulation of Th1-polarizing cytokines, C-C chemokines, maturation of dendritic cells, and adjuvant function by the peptide binding fragment of HSP 70. J. Immunol. 169:2002;2422-2429.
53. Banerjee P., et al. Evidence that glycoprotein 96 (B2), a stress protein, functions as a Th2-specific costimulatory molecule. J. Immunol. 169:2002;3507-3518.
54. Castellino F., et al. Receptor-mediated uptake of antigen-heat shock protein complexes results in MHC I antigen presentation via two distinct processing pathways. J. Exp. Med. 191:2000;1957-1964.
55. Binder R., et al. HSP-chaperoned peptides but not free peptides introduced to the cytosol are presented efficiently by MHC I molecules. J. Biol. Chem. 276:2001;17163-17171.
56. Cho B., et al. A proposed mechanism for the induction of cytotoxic T lymphocyte production by HSP fusion proteins. Immunity. 12:2000;263-272.
57. Arnold-Schild D., et al. Cutting edge: receptor-mediated endocytosis of heat shock proteins by professional antigen presenting cells. J. Immunol. 162:1999;3757-3760.
58. Kleijmeer M., et al. Antigen loading of MHC class I molecules in the endocytic tract. Traffic. 2:2001;124-137.
59. Li Z., Srivastava P.K. Tumor rejection antigen gp96/Grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J. 12:1993;3143-3151.
60. Srivastava P.K., et al. Endo-beta-d-glucuronidase (heparanase) activity of HSP/tumor rejection antigen gp96. Biochem. J. 301:1994;919.
61. Reed R., et al. Grp94 associated enzymatic activities: resolution by chromatographic fractionation. J. Biol. Chem. 277:2002;25082-25089.
62. Berwin B., et al. Cutting Edge: CD91 independent cross-presentation of Grp94 (gp96) associated peptides. J. Immunol. 168:2002;4282-4286.
63. Berwin B., et al. Transfer of Grp94 (gp96) associated peptides onto endosomal MHC I molecules. Traffic. 3:2002;358-366.