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18 - Molecular Chaperones as Inducers of Tumour Immunity

Published online by Cambridge University Press:  10 August 2009

Pinaki P. Banerjee
Affiliation:
Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A.
Zihai Li
Affiliation:
Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A.
Brian Henderson
Affiliation:
University College London
A. Graham Pockley
Affiliation:
University of Sheffield
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Summary

Introduction

Tumour antigens can be broadly classified into four categories: (i) those that are expressed in larger quantities in tumours than their normal counterparts (e.g., tumour-associated carbohydrate antigens) [1], (ii) onco-fetal antigens (e.g., carcinoembryonic antigen) [2], (iii) differentiation antigens (e.g., melanoma differentiation antigen) [3, 4] and (iv) tumour-specific antigens. Tumour antigens in the first three categories could serve as useful markers for diagnostic and prognostic purposes. Although some of these antigens are being used in immunotherapy, none can be called tumour-specific in a true sense. Only the last group includes antigens that are truly specific for tumour cells, in that they contain tumour-specific mutations that are unique for individual tumours such as the tumour-specific point mutation that is found in cyclin-dependent kinase-4. Such a mutation gives rise to a novel antigenic epitope which can be recognised by cytotoxic T lymphocytes (CTLs) [5]. However, for these antigens to be of any value as therapeutic agents, they must be detected in and epitopes isolated from a large range of cancers, and this makes the general use of these antigens difficult.

In the past two decades, evidence has accumulated to support the concept that molecular chaperones or heat shock proteins can be used as a potent source of cancer vaccines [6, 7]. Molecular chaperones, particularly those derived from the Hsp70 and Hsp90 families, are now being tested in the clinical arena for therapeutic efficacy against a range of cancers (Table 18.1).

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Publisher: Cambridge University Press
Print publication year: 2005

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References

Livingston, P.Ganglioside vaccines with emphasis on GM2. Semin Oncol 1998, 25: 636–645Google ScholarPubMed
Greiner, J W, Zeytin, H, Anver, M R and Schlom, J.Vaccine-based therapy directed against carcinoembryonic antigen demonstrates antitumor activity on spontaneous intestinal tumors in the absence of autoimmunity. Cancer Res 2002, 62: 6944–6951Google ScholarPubMed
Boon, T, Cerottini, J C, Eynde, B, Bruggen, P and Pel, A.Tumor antigens recognized by T lymphocytes. Ann Rev Immunol 1994, 12: 337–365CrossRefGoogle ScholarPubMed
Denkberg, G, Lev, A, Eisenbach, L, Benhar, I and Reiter, Y.Selective targeting of melanoma and APCs using a recombinant antibody with TCR-like specificity directed toward a melanoma differentiation antigen. J Immunol 2003, 171: 2197–2207CrossRefGoogle Scholar
Wolfel, T, Hauer, M, Schneider, J, Serrano, M, Wolfel, C, Klehmann-Hieb, E, Plaen, E, Hankeln, T, Meyer zum Buschenfelde, K H and Beach, D.A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma. Science 1995, 269: 1281–1284CrossRefGoogle Scholar
Srivastava, P K.Immunotherapy of human cancer: lessons from mice. Nat Immunol 2000, 1: 363–366CrossRefGoogle ScholarPubMed
Srivastava, P.Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2002, 2: 185–194CrossRefGoogle ScholarPubMed
Foley, E J.Antigenic properties of methylcholanthrene-induced tumors in mice of the strain of origin. Cancer Res 1953, 13: 835–837Google ScholarPubMed
Li, Z, Dai, J, Zheng, H, Liu, B and Caudill, M.An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in immune response. Frontiers Biosci 2002, 7: 731–751CrossRefGoogle ScholarPubMed
Prehn, R T and Main, J M.Immunity to methylcholanthrene-induced sarcomas. J Nat Cancer Inst 1957, 18: 769–778Google ScholarPubMed
Srivastava, P K, DeLeo, A B and Old, L J.Tumor rejection antigens of chemically induced sarcomas of inbred mice. Proc Natl Acad Sci USA 1986, 83: 3407–3411CrossRefGoogle ScholarPubMed
Li, Z and Srivastava, P K.Tumor rejection antigen gp96/grp94 is an ATPse: implications for protein folding and antigen presentation. EMBO J 1993, 12: 3143–3151Google Scholar
Linderoth, N A, Popowicz, A and Sastry, S.Identification of the peptide-binding site in the heat shock chaperone/tumor rejection antigen gp96 (Grp94). J Biol Chem 2000, 275: 5472–5477CrossRefGoogle Scholar
Arnold, D, Faath, S, Rammensee, H-G and Schild, H.Cross-priming of minor histocompatibility antigen-specific cytotoxic T cells upon immunization with the heat shock protein gp96. J Exp Med 1995, 182: 885–889CrossRefGoogle ScholarPubMed
Blachere, N E, Li, Z L, Chandawarkar, R Y, Suto, R, Jaikaria, N S, Basu, S, Udono, H and Srivastava, P K.Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J Exp Med 1997, 186: 1315–1322CrossRefGoogle ScholarPubMed
Blachere, N E and Srivastava, P K.Heat shock protein-based cancer vaccines and related thoughts on immunogenicity of human tumors. Semin Cancer Biol 1995, 6: 349–355CrossRefGoogle ScholarPubMed
Nieland, T J F, Tan, M C A A, Monee-van Muijen, M, Koning, F, Kruisbeek, A M and Bleek, G M.Isolation of an immunodominant viral peptide that is endogenously bound to the stress protein GP96/GRP94. Proc Natl Acad Sci USA 1996, 93: 6135–6139CrossRefGoogle ScholarPubMed
Breloer, M, Fleischer, B and Bonin, A.In vivo and in vitro activation of T cells after administration of Ag-negative heat shock proteins. J Immunol 1999, 162: 3141–3147Google ScholarPubMed
Banerjee, P P, Vinay, D S, Mathew, A, Raje, M, Parekh, V, Prasad, D V, Kumar, A, Mitra, D and Mishra, G C.Evidence that glycoprotein 96 (B2), a stress protein, functions as a Th2-specific costimulatory molecule. J Immunol 2002, 169: 3507–3518CrossRefGoogle Scholar
Welch, W J, Garrels, J I, Thomas, G P, Lin, J J and Feramisco, J R.Biochemical characterization of the mammalian stress proteins and identification of two stress proteins as glucose- and Ca2+-ionophore-regulated proteins. J Biol Chem 1983, 258: 7102–7111Google ScholarPubMed
Csermely, P, SchnaiderT, C. S T, C. S, Prohászka, Z and Nardai, G.The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 1998, 79: 129–168CrossRefGoogle ScholarPubMed
Lee, A S.The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12. J Cell Physiol 1981, 106: 119–125CrossRefGoogle Scholar
Koch, G, Smith, M, Macer, D, Webster, P and Mortara, R.Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J Cell Sci 1986, 86: 217–222Google ScholarPubMed
Lewis, M J, Mazzarella, R A and Green, M.Structure and assembly of the endoplasmic reticulum. The synthesis of three major endoplasmic reticulum proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J Biol Chem 1985, 260: 3050–3057Google ScholarPubMed
Booth, C and Koch, G L.Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell Biol Int 1989, 59: 729–737Google ScholarPubMed
Teriukova, N P, Tiuriaeva, I I, Grandilevskaia, A B and Ivanov, V A.The detection of membrane tumor-associated antigens of Zajdela's hepatoma on the surface of cultured rat cells. Tsitologiia 1997, 39: 577–581Google ScholarPubMed
Feldweg, A M and Srivastava, P K.Molecular heterogeneity of tumor rejection antigen/heat shock protein GP96. Int J Cancer 1995, 63: 310–314CrossRefGoogle ScholarPubMed
Maki, R G, Eddy, R L J, Byers, M, Shows, T B and Srivastava, P K.Mapping of the genes for human endoplasmic reticular heat shock protein gp96/grp94. Somat Cell Mol Genetics 1993, 19: 73–81CrossRefGoogle ScholarPubMed
Binder, R J, Han, D K and Srivastava, P K.CD91: a receptor for heat shock protein gp96. Nat Immunol 2000, 1: 151–155CrossRefGoogle ScholarPubMed
Singh-Jasuja, H, Toes, R E M, Spee, P, Münz, C, Hilf, N, Schoenberger, S P, Ricciardi-Castagnoli, P, Neefjes, J, Rammensee, H-G, Arnold-Schild, D and Schild, H.Cross-presentation of glycoprotein 96-associated antigens on major histocompatibility complex molecules requires receptor-mediated endocytosis. J Exp Med 2000, 191: 1965–1974CrossRefGoogle ScholarPubMed
Matzinger, P.Tolerance, danger, and the extended family. Ann Rev Immunol 1994, 12: 991–1045CrossRefGoogle ScholarPubMed
Srivastava, P.Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Ann Rev Immunol 2002, 20: 395–425CrossRefGoogle ScholarPubMed
Chandawarkar, R Y, Wagh, M S and Srivastava, P K.The dual nature of specific immunological activity of tumour-derived gp96 preparations. J Exp Med 1999, 189: 1437–1442CrossRefGoogle Scholar
Munro, S and Pelham, H R.A C-terminal signal prevents secretion of luminal ER proteins. Cell Biol Int 1987, 48: 899–907Google ScholarPubMed
Altmeyer, A, Maki, R G, Feldweg, A M, Heike, M, Protopopov, V P, Masur, S K and Srivastava, P K.Tumor-specific cell surface expression of the KDEL containing, endoplasmic reticular heat shock protein gp96. Int J Cancer 1996, 69: 340–3493.0.CO;2-9>CrossRefGoogle ScholarPubMed
Zheng, H, Dai, J, Stoilova, D and Li, Z.Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity. J Immunol 2001, 167: 6731–6735CrossRefGoogle ScholarPubMed
Dai, J, Liu, B, Caudill, M, Zheng, H, Qiao, Y, Podack, E R and Li, Z.Cell surface expression of heat shock protein gp96 enhances cross-presentation of cellular antigens and the generation of tumor-specific T cell memory. Cancer Immun 2003, 3: 1–5Google ScholarPubMed
Liu, B, Dai, J, Zheng, H, Stoilova, D, Sun, S and Li, Z.Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases. Proc Nat Acad Sci USA 2003, 100: 15824–15829CrossRefGoogle ScholarPubMed
Udono, H, Levey, D L and Srivastava, P K.Cellular requirements for tumor-specific immunity elicited by heat shock proteins: tumor rejection antigen gp96 primes CD8+ T cells in vivo. Proc Natl Acad Sci USA 1994, 91: 3077–3081CrossRefGoogle ScholarPubMed
Janetzki, S, Blachere, N E and Srivastava, P K.Generation of tumor-specific cytotoxic T lymphocytes and memory T cells by immunization with tumor-derived heat shock protein gp96. J Immunotherapy 1998, 21: 269–276CrossRefGoogle ScholarPubMed
Strbo, N, Oizumi, S, Sotosek-Tokmadzic, V and Podack, E R.Perforin is required for innate and adaptive immunity induced by heat shock protein gp96. Immunity 2003, 18: 381–390CrossRefGoogle ScholarPubMed
Strbo, N, Yamazaki, K, Lee, K, Rukavina, D and Podack, E R.Heat shock fusion protein gp96-Ig mediates strong CD8 CTL expansion in vivo. Am J Reprod Immunol 2002, 48: 220–225CrossRefGoogle ScholarPubMed
Yamazaki, K, Nguyen, T and Podack, E R.Tumour secreted heat shock-fusion protein elicits CD8 cells for rejection. J Immunol 1999, 163: 5178–5182Google ScholarPubMed
Udono, H, Yamano, T, Kawabata, Y, Ueda, M and Yui, K.Generation of cytotoxic T lymphocytes by MHC class I ligands fused to heat shock cognate protein 70. Int Immunol 2001, 13: 1233–1242CrossRefGoogle ScholarPubMed
Binder, R J, Blachere, N E and Srivastava, P K.Heat shock protein-chaperoned peptides but not free peptides introduced into the cytosol are presented efficiently by major histocompatibility complex I molecules. J Biol Chem 2001, 276: 17163–17171CrossRefGoogle Scholar
Castellino, F, Boucher, P E, Eichelberg, K, Mayhew, M, Rothman, J E, Houghton, A N and Germain, R N.Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct pathways. J Exp Med 2000, 191: 1957–1964CrossRefGoogle Scholar
Baker-LePain, J C, Sarzotti, M, Fields, T A, Li, C Y and Nicchitta, C V.GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression. J Exp Med 2002, 196: 1447–1459CrossRefGoogle ScholarPubMed
Kojima, T, Yamazaki, K, Tamura, Y, Ogura, S, Tani, K, Konishi, J, Shinagawa, N, Kinoshita, I, Hizawa, N, Yamaguchi, E, Dosaka-Akita, H and Nishimura, M.Granulocyte-macrophage colony-stimulating factor gene-transduced tumor cells combined with tumor-derived gp96 inhibit tumor growth in mice. Human Gene Therapy 2003, 14: 715–728CrossRefGoogle ScholarPubMed
Basu, S, Binder, R J, Suto, R, Anderson, K M and Srivastava, P K.Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activates the NF-κB pathway. Int Immunol 2000, 12: 1539–1546CrossRefGoogle ScholarPubMed
Huynh, M L, Fadok, V A and Henson, P M.Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-β1 secretion and the resolution of inflammation. J Clin Invest 2002, 109: 41–50CrossRefGoogle ScholarPubMed
Schild, H and Rammensee, H-G.gp96 – the immune system's Swiss army knife. Nat Immunology 2000, 1: 100–101CrossRefGoogle ScholarPubMed
Berwin, B, Hart, J P, Pizzo, S V and Nicchitta, C V.CD91-independent cross-presentation of grp94(gp96)-associated peptides. J Immunol 2002, 168: 4282–4286CrossRefGoogle ScholarPubMed
Vabulas, R M, Braedel, S, Hilf, N, Singh-Jasuja, H, Herter, S, Ahmad-Nejad, P, Kirschning, C J, Da Costa, C, Rammensee, H G, Wagner, H and Schild, H.The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway. J Biol Chem 2002, 277: 20847–20853CrossRefGoogle ScholarPubMed
Berwin, B, Hart, J P, Rice, S, Gass, C, Pizzo, S V, Post, S R and Nicchitta, C V.Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells. EMBO J 2003, 22: 6127–6136CrossRefGoogle ScholarPubMed
Nicchitta, C V.Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity. Nat Rev Immunol 2003, 3: 427–432CrossRefGoogle ScholarPubMed
Bausinger, H, Lipsker, D and Hanau, D.Heat-shock proteins as activators of the innate immune system. Trends Immunol 2002, 23: 342–343CrossRefGoogle ScholarPubMed
Gaston, J S H.Heat shock proteins and innate immunity. Clin Exp Immunol 2002, 127: 1–3CrossRefGoogle ScholarPubMed
Wallin, R P A, Lundqvist, A, Moré, S H, Bonin, A, Kiessling, R and Ljunggren, H-G.Heat-shock proteins as activators of the innate immune system. Trends Immunol 2002, 23: 130–135CrossRefGoogle ScholarPubMed
Robert, J, Gantress, J, Rau, L, Bell, A and Cohen, N.Minor histocompatibility antigen-specific MHC-restricted CD8 T cell responses elicited by heat shock proteins. J Immunol 2002, 168: 1697–1703CrossRefGoogle ScholarPubMed
Ullrich, S J, Robinson, E A, Law, L W, Willingham, M and Appella, E.A mouse tumor-specific transplantation antigen is a heat shock-related protein. Proc Natl Acad Sci USA 1986, 83: 3121–3125CrossRefGoogle ScholarPubMed
Peng, P, Ménoret, A and Srivastava, P K.Purification of immunogenic heat shock protein 70-peptide complexes by ADP-affinity chromatography. J Immunol Methods 1997, 204: 13–21CrossRefGoogle ScholarPubMed
Udono, H and Srivastava, P K.Heat shock protein 70-associated peptides elicit specific cancer immunity. J Exp Med 1993, 178: 1391–1396CrossRefGoogle ScholarPubMed
Flynn, G C, Chappell, T G and Rothman, J E.Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 1989, 245: 385–390CrossRefGoogle ScholarPubMed
Noessner, E, Gastpar, R, Milani, V, Brandl, A, Hutzler, P J, Kuppner, M C, Roos, M, Kremmer, E, Asea, A, Calderwood, S K and Issels, R D.Tumor-derived heat shock protein 70 peptide complexes are cross-presented by human dendritic cells. J Immunol 2002, 169: 5424–5432CrossRefGoogle ScholarPubMed
Azuma, K, Shichijo, S, Takedatsu, H, Komatsu, N, Sawamizu, H and Itoh, K.Heat shock cognate protein 70 encodes antigenic epitopes recognised by HLA-B4601-restricted cytotoxic T lymphocytes from cancer patients. Brit J Cancer 2003, 89: 1079–1085CrossRefGoogle ScholarPubMed
Gehrmann, M, Schmetzer, H, Eissner, G, Haferlach, T, Hiddemann, W and Multhoff, G.Membrane-bound heat shock protein 70 (Hsp70) in acute myeloid leukemia: a tumor specific recognition structure for the cytolytic activity of autologous NK cells. Haematologica 2003, 88: 474–476Google ScholarPubMed
Gross, C, Koelch, W, DeMaio, A, Arispe, N and Multhoff, G.Cell surface-bound heat shock protein 70 (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B. J Biol Chem 2003, 278: 41173–41181CrossRefGoogle ScholarPubMed
Moser, C, Schmidbauer, C, Gurtler, U, Gross, C, Gehrmann, M, Thonigs, G, Pfister, K and Multhoff, G.Inhibition of tumor growth in mice with severe combined immunodeficiency is mediated by heat shock protein 70 (Hsp70)-peptide-activated, CD94 positive natural killer cells. Cell Stress Chaperon 2002, 7: 365–3732.0.CO;2>CrossRefGoogle ScholarPubMed
Multhoff, G.Activation of natural killer cells by heat shock protein 70. Int J Hyperthermia 2002, 18: 576–585CrossRefGoogle ScholarPubMed
Udono, H and Srivastava, P K.Comparison of tumor-specific immunogenicities of stress-induced proteins gp96, hsp90 and hsp70. J Immunol 1994, 152: 5398–5403Google ScholarPubMed
Wang, X Y, Kazim, L, Repasky, E A and Subjeck, J R.Immunization with tumor-derived ER chaperone grp170 elicits tumor-specific CD8+ T-cell responses and reduces pulmonary metastatic disease. Int J Cancer 2003, 105: 226–231CrossRefGoogle ScholarPubMed
Basu, S and Srivastava, P.Calreticulin, a peptide-binding chaperone of the endoplasmic reticulum, elicits tumor- and peptide-specific immunity. J Exp Med 1999, 189: 797–802CrossRefGoogle ScholarPubMed
Cheng, W F, Hung, C F, Chai, C Y, Hsu, K F, He, L, Ling, M and Wu, T C.Tumor-specific immunity and antiangiogenesis generated by a DNA vaccine encoding calreticulin linked to a tumor antigen. J Clin Invest 2001, 108: 669–678CrossRefGoogle ScholarPubMed
Basu, S, Binder, R J, Ramalingam, T and Srivastava, P K.CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70 and calreticulin. Immunity 2001, 14: 303–313CrossRefGoogle ScholarPubMed
Binder, R J, Harris, M L, Ménoret, A and Srivastava, P K.Saturation, competition, and specificity in interaction of heat shock proteins (hsp) gp96, hsp90, and hsp70 with CD11b+ cells. J Immunol 2000, 165: 2582–2587CrossRefGoogle ScholarPubMed
Delneste, Y, Magistrelli, G, Gauchat, J, Haeuw, J, Aubry, J, Nakamura, K, Kawakami-Honda, N, Goetsch, L, Sawamura, T, Bonnefoy, J and Jeannin, P.Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002, 17: 353–362CrossRefGoogle ScholarPubMed
Vabulas, R M, Wagner, H and Schild, H.Heat shock proteins as ligands of toll-like receptors. Cur Topics Microbiol Immunol 2002, 270: 169–184Google ScholarPubMed
Ménoret, A and Bell, G.Purification of multiple heat shock proteins from a single tumor sample. J Immunol Methods 2000, 237: 119–130CrossRefGoogle ScholarPubMed
Suto, R and Srivastava, P K.A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides. Science 1995, 269: 1585–1588CrossRefGoogle ScholarPubMed
Tamura, Y, Peng, P, Liu, K, Daou, M and Srivastava, P K.Immunotherapy of tumors with autologous tumor-derived heat shock protein preparations. Science 1997, 278: 117–120CrossRefGoogle ScholarPubMed

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  • Molecular Chaperones as Inducers of Tumour Immunity
    • By Pinaki P. Banerjee, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A., Zihai Li, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.019
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  • Molecular Chaperones as Inducers of Tumour Immunity
    • By Pinaki P. Banerjee, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A., Zihai Li, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.019
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  • Molecular Chaperones as Inducers of Tumour Immunity
    • By Pinaki P. Banerjee, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A., Zihai Li, Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, Connecticut, U.S.A.
  • Edited by Brian Henderson, University College London, A. Graham Pockley, University of Sheffield
  • Book: Molecular Chaperones and Cell Signalling
  • Online publication: 10 August 2009
  • Chapter DOI: https://doi.org/10.1017/CBO9780511546310.019
Available formats
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