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Volumn 54, Issue 2, 1997, Pages 137-147

Peptide-MHC complexes assembled following multiple pathways: An opportunity for the design of vaccines and therapeutic molecules

Author keywords

[No Author keywords available]

Indexed keywords

ANTIIDIOTYPIC ANTIBODY; EPITOPE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE; SYNTHETIC PEPTIDE; VACCINE; VIRUS PROTEIN;

EID: 0030752577     PISSN: 01988859     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0198-8859(97)00080-3     Document Type: Review
Times cited : (9)

References (106)
  • 2
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddisson WE, Wiley DC: Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384: 134, 1996.
    • (1996) Nature , vol.384 , pp. 134
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddisson, W.E.5    Wiley, D.C.6
  • 3
    • 0015898251 scopus 로고
    • Function of macrophages in antigen recognition by guinea pig T lymphocytes. I. Requirement for histocompatible macrophages and lymphocytes
    • Rosenthal AS, Shevach EM: Function of macrophages in antigen recognition by guinea pig T lymphocytes. I. Requirement for histocompatible macrophages and lymphocytes. J Exp Med 138:1194, 1973.
    • (1973) J Exp Med , vol.138 , pp. 1194
    • Rosenthal, A.S.1    Shevach, E.M.2
  • 4
    • 0016345568 scopus 로고
    • Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system
    • Zinkernagel RM, Doherty PC: Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic system. Nature 248:701, 1974.
    • (1974) Nature , vol.248 , pp. 701
    • Zinkernagel, R.M.1    Doherty, P.C.2
  • 5
    • 0020036538 scopus 로고
    • Lymphocyte specificity to protein antigens. V. Conformational dependence of activation of cytochrome c-specific T cells
    • Buchmuller Y, Corradin G: Lymphocyte specificity to protein antigens. V. Conformational dependence of activation of cytochrome c-specific T cells. Eur J Immunol 12:412, 1982
    • (1982) Eur J Immunol , vol.12 , pp. 412
    • Buchmuller, Y.1    Corradin, G.2
  • 6
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • Heemels MT, Ploegh H: Generation, translocation, and presentation of MHC class I-restricted peptides. Annu Rev Biochem 64:463, 1995.
    • (1995) Annu Rev Biochem , vol.64 , pp. 463
    • Heemels, M.T.1    Ploegh, H.2
  • 7
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York IA, Rock KL: Antigen processing and presentation by the class I major histocompatibility complex. Annu Rev Immunol 14:369, 1996.
    • (1996) Annu Rev Immunol , vol.14 , pp. 369
    • York, I.A.1    Rock, K.L.2
  • 8
    • 0342894676 scopus 로고    scopus 로고
    • Generation, intracellular transport and loading of peptides associated with MHC class I molecules
    • Koopmann JO, Hämmerling GJ, Momburg F: Generation, intracellular transport and loading of peptides associated with MHC class I molecules. Curr Opin Immunol 9:80, 1997.
    • (1997) Curr Opin Immunol , vol.9 , pp. 80
    • Koopmann, J.O.1    Hämmerling, G.J.2    Momburg, F.3
  • 10
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei ML, Cresswell P: HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 356:443, 1992.
    • (1992) Nature , vol.356 , pp. 443
    • Wei, M.L.1    Cresswell, P.2
  • 11
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner RD, Sitia R: Protein degradation in the endoplasmic reticulum. Cell 62:611, 1990.
    • (1990) Cell , vol.62 , pp. 611
    • Klausner, R.D.1    Sitia, R.2
  • 12
    • 0028783818 scopus 로고
    • Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein
    • Hombach J, Pircher H, Tonegawa S, Zinkernagel RM: Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein. J Exp Med 182:1615, 1995.
    • (1995) J Exp Med , vol.182 , pp. 1615
    • Hombach, J.1    Pircher, H.2    Tonegawa, S.3    Zinkernagel, R.M.4
  • 13
    • 0029032060 scopus 로고
    • MHC class I-restricted processing of transmembrane proteins
    • Siliciano RF, Soloski MJ: MHC class I-restricted processing of transmembrane proteins. J Immunol 155:2, 1995.
    • (1995) J Immunol , vol.155 , pp. 2
    • Siliciano, R.F.1    Soloski, M.J.2
  • 14
    • 0029927928 scopus 로고    scopus 로고
    • A new foreign policy: MHC class I molecules monitor the outside world
    • Rock KL: A new foreign policy: MHC class I molecules monitor the outside world. Immunol Today 17:131, 1996.
    • (1996) Immunol Today , vol.17 , pp. 131
    • Rock, K.L.1
  • 16
    • 0028965525 scopus 로고
    • Hepatitis B virus small surface antigen particles are processed in a novel endosomal pathway for major histocompatibility complex class I-restricted epitope presentation
    • Schirmbeck R, Melber K, Reimann J: Hepatitis B virus small surface antigen particles are processed in a novel endosomal pathway for major histocompatibility complex class I-restricted epitope presentation. Eur J Immunol 25:1063, 1995.
    • (1995) Eur J Immunol , vol.25 , pp. 1063
    • Schirmbeck, R.1    Melber, K.2    Reimann, J.3
  • 18
    • 0028152358 scopus 로고
    • A role for calnexin (IP90) in the assembly of class II MHC molecules
    • Anderson KS, Cresswell P: A role for calnexin (IP90) in the assembly of class II MHC molecules. EMBO J 13: 675, 1994.
    • (1994) EMBO J , vol.13 , pp. 675
    • Anderson, K.S.1    Cresswell, P.2
  • 19
    • 0031059765 scopus 로고    scopus 로고
    • MHC class II restricted antigen presentation
    • Pieters J: MHC class II restricted antigen presentation. Curr Opin Immunol 9:89, 1997.
    • (1997) Curr Opin Immunol , vol.9 , pp. 89
    • Pieters, J.1
  • 20
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • Cresswell P: Assembly, transport, and function of MHC class II molecules. Annu Rev Immunol 12:259, 1994.
    • (1994) Annu Rev Immunol , vol.12 , pp. 259
    • Cresswell, P.1
  • 21
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invaraint chain negative cells
    • Schaiff WT, Hruska KA Jr, McCourt DW, Green M, Schwartz BD: HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invaraint chain negative cells. J Exp Med 176:657, 1992.
    • (1992) J Exp Med , vol.176 , pp. 657
    • Schaiff, W.T.1    Hruska K.A., Jr.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 23
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke O, Dobberstein B: MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 63:707, 1990.
    • (1990) Cell , vol.63 , pp. 707
    • Bakke, O.1    Dobberstein, B.2
  • 26
    • 0029615496 scopus 로고
    • How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway
    • Wolf PR, Ploegh HL: How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Annu Rev Cell Dev Biol 11:267, 1995.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 267
    • Wolf, P.R.1    Ploegh, H.L.2
  • 27
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
    • Peters PJ, Neefjes JJ, Oorschot V, Ploegh HL, Geuze HJ: Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349:669, 1991.
    • (1991) Nature , vol.349 , pp. 669
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 28
    • 0025331726 scopus 로고
    • Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding
    • Roche PA, Cresswell P: Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature 345:615, 1990.
    • (1990) Nature , vol.345 , pp. 615
    • Roche, P.A.1    Cresswell, P.2
  • 29
    • 0027272815 scopus 로고
    • DR αβ dimers released from complexes with invariant chain fail to stimulate alloreactive T cell clones
    • Demotz S: DR αβ dimers released from complexes with invariant chain fail to stimulate alloreactive T cell clones. Eur J Immunol 23:2100, 1993.
    • (1993) Eur J Immunol , vol.23 , pp. 2100
    • Demotz, S.1
  • 30
    • 0028877058 scopus 로고
    • T cell recognition of major histocompatibility complex class II complexes with invariant chain processing intermediates
    • Morkowski S, Goldrath AW, Eastman S, Ramachandra L, Freed DC, Whiteley P, Rudensky AY: T cell recognition of major histocompatibility complex class II complexes with invariant chain processing intermediates. J Exp Med 182:1403, 1995.
    • (1995) J Exp Med , vol.182 , pp. 1403
    • Morkowski, S.1    Goldrath, A.W.2    Eastman, S.3    Ramachandra, L.4    Freed, D.C.5    Whiteley, P.6    Rudensky, A.Y.7
  • 31
    • 0029845011 scopus 로고    scopus 로고
    • Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP)
    • Zhong G, Castellino F, Romagnoli P, Germain R: Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP). J Exp Med 184:2061, 1996.
    • (1996) J Exp Med , vol.184 , pp. 2061
    • Zhong, G.1    Castellino, F.2    Romagnoli, P.3    Germain, R.4
  • 32
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh P, Amaya M, Mellins E, Wiley DC: The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378:457, 1995.
    • (1995) Nature , vol.378 , pp. 457
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 33
    • 0028845966 scopus 로고
    • Evidence for invariant chain 85-101 (CLIP) binding in the antigen binding site of MHC class II molecules
    • Bangia N, Watts TH: Evidence for invariant chain 85-101 (CLIP) binding in the antigen binding site of MHC class II molecules. Int Immunol 7:1585, 1995.
    • (1995) Int Immunol , vol.7 , pp. 1585
    • Bangia, N.1    Watts, T.H.2
  • 34
    • 0028945021 scopus 로고
    • Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules
    • Malcherek G, Gnau V, Jung G, Rammensee HG, Melms A: Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules. J Exp Med 181:527, 1995.
    • (1995) J Exp Med , vol.181 , pp. 527
    • Malcherek, G.1    Gnau, V.2    Jung, G.3    Rammensee, H.G.4    Melms, A.5
  • 35
    • 0028921633 scopus 로고
    • Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II
    • Sette A, Southwood S, Miller J, Appella E: Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II. J Exp Med 181:677, 1995.
    • (1995) J Exp Med , vol.181 , pp. 677
    • Sette, A.1    Southwood, S.2    Miller, J.3    Appella, E.4
  • 36
    • 0026440236 scopus 로고
    • HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
    • Riberdy JM, Newcomb JR, Surman MJ, Barbosa JA, Cresswell P: HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 360:474, 1992.
    • (1992) Nature , vol.360 , pp. 474
    • Riberdy, J.M.1    Newcomb, J.R.2    Surman, M.J.3    Barbosa, J.A.4    Cresswell, P.5
  • 38
    • 0028789889 scopus 로고
    • HLA-DM: An in vivo facilitator of MHC class II peptide loading
    • Roche PA: HLA-DM: an in vivo facilitator of MHC class II peptide loading. Immunity 3:259, 1995.
    • (1995) Immunity , vol.3 , pp. 259
    • Roche, P.A.1
  • 39
    • 0029824101 scopus 로고    scopus 로고
    • Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM
    • Weber DA, Evavold BD, Jensen PE: Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM. Science 274:618, 1996.
    • (1996) Science , vol.274 , pp. 618
    • Weber, D.A.1    Evavold, B.D.2    Jensen, P.E.3
  • 40
    • 0023784882 scopus 로고
    • Kinetics of MHC-antigen complex formation on antigen-presenting cells
    • Roosnek E, Demotz S, Corradin G, Lanzavecchia A: Kinetics of MHC-antigen complex formation on antigen-presenting cells. J Immunol 140:4079, 1988.
    • (1988) J Immunol , vol.140 , pp. 4079
    • Roosnek, E.1    Demotz, S.2    Corradin, G.3    Lanzavecchia, A.4
  • 41
    • 0025323546 scopus 로고
    • High-affinity binding of an influenza hemagglutinin-derived peptide to purified HLA-DR
    • Roche PA, Cresswell P: High-affinity binding of an influenza hemagglutinin-derived peptide to purified HLA-DR. J Immunol 144:1849, 1990.
    • (1990) J Immunol , vol.144 , pp. 1849
    • Roche, P.A.1    Cresswell, P.2
  • 42
    • 0031080953 scopus 로고    scopus 로고
    • How HLA-DM edits the MHC class II peptide repertoire: Survival of the fittest?
    • Kropshofer H, Hämmerling GJ, Vogt AB: How HLA-DM edits the MHC class II peptide repertoire: survival of the fittest? Immunol Today 18:77, 1997.
    • (1997) Immunol Today , vol.18 , pp. 77
    • Kropshofer, H.1    Hämmerling, G.J.2    Vogt, A.B.3
  • 43
    • 0026057743 scopus 로고
    • Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells
    • Harding CV, Collins DS, Slot JW, Geuze HJ, Unanue ER: Liposome-encapsulated antigens are processed in lysosomes, recycled, and presented to T cells. Cell 64: 393, 1991.
    • (1991) Cell , vol.64 , pp. 393
    • Harding, C.V.1    Collins, D.S.2    Slot, J.W.3    Geuze, H.J.4    Unanue, E.R.5
  • 44
    • 0026343001 scopus 로고
    • Reduction of disulfide bonds within lysosomes is a key step in antigen processing
    • Collins D, Unanue ER, Harding CV: Reduction of disulfide bonds within lysosomes is a key step in antigen processing. J Immunol 147:4054, 1991.
    • (1991) J Immunol , vol.147 , pp. 4054
    • Collins, D.1    Unanue, E.R.2    Harding, C.V.3
  • 45
    • 0028965825 scopus 로고
    • Detection of functional class II-associated antigen: Role of a low density endosomal compartment in antigen processing
    • Barnes KA, Mitchell RN: Detection of functional class II-associated antigen: role of a low density endosomal compartment in antigen processing. J Exp Med 181: 1715, 1995.
    • (1995) J Exp Med , vol.181 , pp. 1715
    • Barnes, K.A.1    Mitchell, R.N.2
  • 46
    • 0028898447 scopus 로고
    • Antigen-processing organelles from DRB1*1101 and DRB1*1104 B cell lines display a differential degradation activity
    • Barbey C, Watts C, Corradin G: Antigen-processing organelles from DRB1*1101 and DRB1*1104 B cell lines display a differential degradation activity. Eur J Immunol 25:30, 1995.
    • (1995) Eur J Immunol , vol.25 , pp. 30
    • Barbey, C.1    Watts, C.2    Corradin, G.3
  • 48
  • 49
    • 0031030323 scopus 로고    scopus 로고
    • Amino-terminal trimming of peptides for presentation on major histocompatibility complex class II molecules
    • Nelson CA, Vidavsky I, Viner NJ, Gross ML, Unanue ER: Amino-terminal trimming of peptides for presentation on major histocompatibility complex class II molecules. Proc Natl Acad Sci USA 94:628, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 628
    • Nelson, C.A.1    Vidavsky, I.2    Viner, N.J.3    Gross, M.L.4    Unanue, E.R.5
  • 51
    • 0642282644 scopus 로고
    • Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis
    • Cresswell P: Intracellular class II HLA antigens are accessible to transferrin-neuraminidase conjugates internalized by receptor-mediated endocytosis. Proc Natl Acad Sci USA 82:8188, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8188
    • Cresswell, P.1
  • 52
    • 0028200118 scopus 로고
    • Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes
    • Amigorena S, Drake JR, Webster P, Mellman I: Transient accumulation of new class II MHC molecules in a novel endocytic compartment in B lymphocytes. Nature 369:113, 1994.
    • (1994) Nature , vol.369 , pp. 113
    • Amigorena, S.1    Drake, J.R.2    Webster, P.3    Mellman, I.4
  • 53
    • 0028285075 scopus 로고
    • Separation of subcellular compartments containing distinct functional forms of MHC class II
    • Qiu Y, Xu X, Wandinger-Ness A, Dalke DP, Pierce SK: Separation of subcellular compartments containing dis-tinct functional forms of MHC class II. J Cell Biol 125:595, 1994
    • (1994) J Cell Biol , vol.125 , pp. 595
    • Qiu, Y.1    Xu, X.2    Wandinger-Ness, A.3    Dalke, D.P.4    Pierce, S.K.5
  • 55
    • 0028229009 scopus 로고
    • Isolation and characterization of the intracellular MHC class II compartment
    • Tulp A, Verwoerd D, Dobberstein B, Ploegh HL, Pieters J: Isolation and characterization of the intracellular MHC class II compartment. Nature 369:120, 1994.
    • (1994) Nature , vol.369 , pp. 120
    • Tulp, A.1    Verwoerd, D.2    Dobberstein, B.3    Ploegh, H.L.4    Pieters, J.5
  • 56
    • 0028303848 scopus 로고
    • Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells
    • West MA, Lucocq JM, Watts C: Antigen processing and class II MHC peptide-loading compartments in human B-lymphoblastoid cells. Nature 369:147, 1994.
    • (1994) Nature , vol.369 , pp. 147
    • West, M.A.1    Lucocq, J.M.2    Watts, C.3
  • 57
    • 0028970286 scopus 로고
    • Extensive trafficking of MHC class II-invariant chain complexes in the endocytic pathway and appearance of peptide-loaded class II in multiple compartments
    • Castellino F, Germain RN: Extensive trafficking of MHC class II-invariant chain complexes in the endocytic pathway and appearance of peptide-loaded class II in multiple compartments. Immunity 2:73, 1995.
    • (1995) Immunity , vol.2 , pp. 73
    • Castellino, F.1    Germain, R.N.2
  • 59
    • 0027303736 scopus 로고
    • Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes surface expression of occupied molecules
    • Germain RN, Rinker AG Jr: Peptide binding inhibits protein aggregation of invariant-chain free class II dimers and promotes surface expression of occupied molecules. Nature 363:725, 1993.
    • (1993) Nature , vol.363 , pp. 725
    • Germain, R.N.1    Rinker A.G., Jr.2
  • 61
    • 0030583875 scopus 로고
    • Two Listeria monocytogenes CTL epitopes are processed from the same antigen with different efficiencies
    • Sijts AJAM, Neissig A, Neefjes J, Pamer EG: Two Listeria monocytogenes CTL epitopes are processed from the same antigen with different efficiencies. J Immunol 156: 685, 1995.
    • (1995) J Immunol , vol.156 , pp. 685
    • Sijts, A.J.A.M.1    Neissig, A.2    Neefjes, J.3    Pamer, E.G.4
  • 62
    • 0028354134 scopus 로고
    • Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen
    • Pinet V, Malnati MS, Long EO: Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen. J Immunol 152:4852, 1994.
    • (1994) J Immunol , vol.152 , pp. 4852
    • Pinet, V.1    Malnati, M.S.2    Long, E.O.3
  • 63
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • Pinet V, Vergelli M, Martin R, Bakke O, Long EO: Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature 375:603, 1995.
    • (1995) Nature , vol.375 , pp. 603
    • Pinet, V.1    Vergelli, M.2    Martin, R.3    Bakke, O.4    Long, E.O.5
  • 64
    • 0029155721 scopus 로고
    • Invariant chain-independent antigen presentation depends primarily upon the pool of newly synthesized MHC class II molecules
    • Swier K, Miller J: Invariant chain-independent antigen presentation depends primarily upon the pool of newly synthesized MHC class II molecules. J Immunol 155: 1851, 1995.
    • (1995) J Immunol , vol.155 , pp. 1851
    • Swier, K.1    Miller, J.2
  • 65
    • 18744430792 scopus 로고    scopus 로고
    • DR1-restricted determinants from the fusion protein of measles virus processed following two distinct pathways
    • Demotz S, Péléraux A: DR1-restricted determinants from the fusion protein of measles virus processed following two distinct pathways. Mol Immunol 33:387, 1996.
    • (1996) Mol Immunol , vol.33 , pp. 387
    • Demotz, S.1    Péléraux, A.2
  • 67
    • 0026505030 scopus 로고
    • Irreversible association of peptides with class II MHC molecules in living cells
    • Lanzavecchia A, Reid PA, Watts C: Irreversible association of peptides with class II MHC molecules in living cells. Nature 357:249, 1992.
    • (1992) Nature , vol.357 , pp. 249
    • Lanzavecchia, A.1    Reid, P.A.2    Watts, C.3
  • 68
    • 0025909318 scopus 로고
    • Free ligand-induced dissociation of MHC-antigen complexes
    • Pedrazzini T, Sette A, Albertson M, Grey HM: Free ligand-induced dissociation of MHC-antigen complexes. J Immunol 146:3496, 1991.
    • (1991) J Immunol , vol.146 , pp. 3496
    • Pedrazzini, T.1    Sette, A.2    Albertson, M.3    Grey, H.M.4
  • 69
    • 0026643116 scopus 로고
    • pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule
    • Reay PA, Wettstein DA, Davis MM: pH dependence and exchange of high and low responder peptides binding to a class II MHC molecule. EMBO J 11:2829, 1992.
    • (1992) EMBO J , vol.11 , pp. 2829
    • Reay, P.A.1    Wettstein, D.A.2    Davis, M.M.3
  • 70
    • 0028064707 scopus 로고
    • Peptides determine the lifespan of MHC class II molecules in the antigen-presenting cell
    • Nelson CA, Petzold SJ, Unanue ER: Peptides determine the lifespan of MHC class II molecules in the antigen- presenting cell. Nature 371:250, 1994.
    • (1994) Nature , vol.371 , pp. 250
    • Nelson, C.A.1    Petzold, S.J.2    Unanue, E.R.3
  • 71
    • 0027977846 scopus 로고
    • Invariant chain prevents the HLA-DR-restricted presentation of a cytosolic peptide
    • Long EO, LaVaute T, Pinet V, Jaraquemada D: Invariant chain prevents the HLA-DR-restricted presentation of a cytosolic peptide. J Immunol 153:1487, 1994.
    • (1994) J Immunol , vol.153 , pp. 1487
    • Long, E.O.1    LaVaute, T.2    Pinet, V.3    Jaraquemada, D.4
  • 72
    • 0027979948 scopus 로고
    • Early events in the assembly of major histocompatibility complex class II heterotrimers from their free subunits
    • Nijenhuis M, Neefjes J: Early events in the assembly of major histocompatibility complex class II heterotrimers from their free subunits. Eur J Immunol 24:247, 1994.
    • (1994) Eur J Immunol , vol.24 , pp. 247
    • Nijenhuis, M.1    Neefjes, J.2
  • 73
    • 0027151841 scopus 로고
    • Characterization of endogenous peptides bound to purified HLA-DR molecules and their absence from invariant chain-associated αβ dimers
    • Newcomb JR, Cresswell P: Characterization of endogenous peptides bound to purified HLA-DR molecules and their absence from invariant chain-associated αβ dimers. J Immunol 150:499, 1993.
    • (1993) J Immunol , vol.150 , pp. 499
    • Newcomb, J.R.1    Cresswell, P.2
  • 74
    • 0028341362 scopus 로고
    • Assembly of HLA DR1 molecules translated in vitro: Binding of peptide in the endoplasmic reticulum precludes association with invariant chain
    • Bijlmakers MJJE, Benaroch P, Ploegh HL: Assembly of HLA DR1 molecules translated in vitro: binding of peptide in the endoplasmic reticulum precludes association with invariant chain. EMBO J 13:2699, 1994.
    • (1994) EMBO J , vol.13 , pp. 2699
    • Bijlmakers, M.J.J.E.1    Benaroch, P.2    Ploegh, H.L.3
  • 75
    • 0028130306 scopus 로고
    • Assembly and peptide binding of major histocompatibility complex class II heterodimers in an in vitro translation system
    • Hedley ML, Urban RG, Strominger JL: Assembly and peptide binding of major histocompatibility complex class II heterodimers in an in vitro translation system. Proc Natl Acad Sci USA 91:10479, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10479
    • Hedley, M.L.1    Urban, R.G.2    Strominger, J.L.3
  • 76
    • 0029163038 scopus 로고
    • Processing of a viral glycoprotein in the endoplasmic reticulum for class II presentation
    • Bartido SM, Diment S, Reiss CS: Processing of a viral glycoprotein in the endoplasmic reticulum for class II presentation. Eur J Immunol 25:2211, 1995.
    • (1995) Eur J Immunol , vol.25 , pp. 2211
    • Bartido, S.M.1    Diment, S.2    Reiss, C.S.3
  • 79
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn WA Jr: Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol 4:139, 1994.
    • (1994) Trends Cell Biol , vol.4 , pp. 139
    • Dunn W.A., Jr.1
  • 80
    • 0027379661 scopus 로고
    • Polypeptide import and degradation by isolated lysosomes
    • Terlecky SR, Dice JF: Polypeptide import and degradation by isolated lysosomes. J Biol Chem 268:23490, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23490
    • Terlecky, S.R.1    Dice, J.F.2
  • 82
    • 0024328644 scopus 로고
    • A novel and simple procedure for determining T cell epitopes in protein antigens
    • Demotz S, Matricardi P, Lanzavecchia A, Corradin G: A novel and simple procedure for determining T cell epitopes in protein antigens. J Immunol Methods 122: 67, 1989.
    • (1989) J Immunol Methods , vol.122 , pp. 67
    • Demotz, S.1    Matricardi, P.2    Lanzavecchia, A.3    Corradin, G.4
  • 83
    • 0024796883 scopus 로고
    • Universally immunogenic T cell epitopes: Promiscuous binding to human MHC class II and promiscuous recognition by T cells
    • Panina-Bordignon P, Tan A, Termijtelen A, Demotz S, Corradin G, Lanzavecchia A: Universally immunogenic T cell epitopes: promiscuous binding to human MHC class II and promiscuous recognition by T cells. Eur J Immunol 19:2237, 1989.
    • (1989) Eur J Immunol , vol.19 , pp. 2237
    • Panina-Bordignon, P.1    Tan, A.2    Termijtelen, A.3    Demotz, S.4    Corradin, G.5    Lanzavecchia, A.6
  • 85
    • 0011235258 scopus 로고
    • The carrier effect in the secondary response to hapten-protein conjugates. I. Measurement of the effect with transferred cells and objection to the local environment hypothesis
    • Mitchison NA: The carrier effect in the secondary response to hapten-protein conjugates. I. Measurement of the effect with transferred cells and objection to the local environment hypothesis. Eur J Immunol 1:10, 1971.
    • (1971) Eur J Immunol , vol.1 , pp. 10
    • Mitchison, N.A.1
  • 86
    • 0019222660 scopus 로고
    • Carrier-priming leads to hapten-specific suppression
    • Herzenberg LA, Tokuhisa T, Herzenberg LA: Carrier-priming leads to hapten-specific suppression. Nature 285:664, 1980.
    • (1980) Nature , vol.285 , pp. 664
    • Herzenberg, L.A.1    Tokuhisa, T.2    Herzenberg, L.A.3
  • 88
    • 0026703523 scopus 로고
    • Use of human universally antigenic tetanus toxin T cell epitopes as carriers for human vaccination
    • Valmori D, Pessi A, Bianchi E, Corradin G: Use of human universally antigenic tetanus toxin T cell epitopes as carriers for human vaccination. J Immunol 149:717, 1992.
    • (1992) J Immunol , vol.149 , pp. 717
    • Valmori, D.1    Pessi, A.2    Bianchi, E.3    Corradin, G.4
  • 89
    • 0001331728 scopus 로고
    • Synthetic peptide vaccine design: Synthesis and properties of a high-density multiple antigenic peptide system
    • Tam JP: Synthetic peptide vaccine design: synthesis and properties of a high-density multiple antigenic peptide system. Proc Natl Acad Sci USA 85:5409, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5409
    • Tam, J.P.1
  • 90
    • 0025099759 scopus 로고
    • Incorporation of T and B epitopes of the circumsporozoite protein in a chemically defined synthetic vaccine against malaria
    • Tam JP, Clvijo P, Lu YA, Nussenzweig V, Nussenzweig R, Zavala F: Incorporation of T and B epitopes of the circumsporozoite protein in a chemically defined synthetic vaccine against malaria. J Exp Med 82:299, 1990.
    • (1990) J Exp Med , vol.82 , pp. 299
    • Tam, J.P.1    Clvijo, P.2    Lu, Y.A.3    Nussenzweig, V.4    Nussenzweig, R.5    Zavala, F.6
  • 92
    • 0028952801 scopus 로고
    • Induction of protective polyclonal antibodies by immunization with a Plasmodium yoelii circumsporozoite protein multiple antigen peptide vaccine
    • Wang R, Charonenvit Y, Corradin G, Porrozzi R, Hunter RL, Glenn G, Alving CR, Church P, Hoffman SL: Induction of protective polyclonal antibodies by immunization with a Plasmodium yoelii circumsporozoite protein multiple antigen peptide vaccine. J Immunol 154:2784, 1995.
    • (1995) J Immunol , vol.154 , pp. 2784
    • Wang, R.1    Charonenvit, Y.2    Corradin, G.3    Porrozzi, R.4    Hunter, R.L.5    Glenn, G.6    Alving, C.R.7    Church, P.8    Hoffman, S.L.9
  • 94
    • 0026515267 scopus 로고
    • "Universal" T helper cell determinants enhance immunogenicity of a Plasmodium falciparum merozoite surface antigen peptide
    • Kumar A, Arora R, Kaur P, Chauhan VS, Sharma P: "Universal" T helper cell determinants enhance immunogenicity of a Plasmodium falciparum merozoite surface antigen peptide. J Immunol 148:1499, 1992.
    • (1992) J Immunol , vol.148 , pp. 1499
    • Kumar, A.1    Arora, R.2    Kaur, P.3    Chauhan, V.S.4    Sharma, P.5
  • 96
    • 0027440690 scopus 로고
    • Mapping the major human T cell epitopes of tetanus toxin
    • Reece JC, Geysen HM, Rodda SJ: Mapping the major human T cell epitopes of tetanus toxin. J Immunol 151:6175, 1993.
    • (1993) J Immunol , vol.151 , pp. 6175
    • Reece, J.C.1    Geysen, H.M.2    Rodda, S.J.3
  • 97
    • 0027318986 scopus 로고
    • Presentation of T-cell epitopes assembled as multiple antigen peptides to murine and human T lymphocytes
    • Grilliot D, Valmori D, Lambert PH, Corradin G, Del Giudice G: Presentation of T-cell epitopes assembled as multiple antigen peptides to murine and human T lymphocytes. Infect Immun 61:3064, 1993.
    • (1993) Infect Immun , vol.61 , pp. 3064
    • Grilliot, D.1    Valmori, D.2    Lambert, P.H.3    Corradin, G.4    Del Giudice, G.5
  • 98
    • 0030236076 scopus 로고    scopus 로고
    • Recombinant fusion peptides containing single or multiple repeats of an ubiquitous T-helper epitope are highly immunogenic
    • Astori M, Kraehenbuhl JP: Recombinant fusion peptides containing single or multiple repeats of an ubiquitous T-helper epitope are highly immunogenic. Mol Immunol 13:1017, 1996.
    • (1996) Mol Immunol , vol.13 , pp. 1017
    • Astori, M.1    Kraehenbuhl, J.P.2
  • 100
    • 0026739624 scopus 로고
    • T helper epitopes enhance the cytotoxic response of mice immunized with MHC class I-restricted malaria peptides
    • Widmann C, Romero P, Maryanski JL, Corradin G, Valmori D: T helper epitopes enhance the cytotoxic response of mice immunized with MHC class I-restricted malaria peptides. J Immunol Methods 155:95, 1992.
    • (1992) J Immunol Methods , vol.155 , pp. 95
    • Widmann, C.1    Romero, P.2    Maryanski, J.L.3    Corradin, G.4    Valmori, D.5
  • 101
    • 0028306427 scopus 로고
    • Induction of a cytotoxic T cell response by co-injection of a T helper peptide and a cytotoxic T lymphocyte peptide in incomplete Freund's adjuvant: Further enhancement by pre-injection of IFA alone
    • Valmori D, Romero J, Men Y, Maryanski JM, Romero P, Corradin G: Induction of a cytotoxic T cell response by co-injection of a T helper peptide and a cytotoxic T lymphocyte peptide in incomplete Freund's adjuvant: further enhancement by pre-injection of IFA alone. Eur J Immunol 25:1458, 1994.
    • (1994) Eur J Immunol , vol.25 , pp. 1458
    • Valmori, D.1    Romero, J.2    Men, Y.3    Maryanski, J.M.4    Romero, P.5    Corradin, G.6
  • 102
    • 0029072487 scopus 로고
    • + T-cell protective immunity induced by immunization with Plasmodium berghei CS protein derived synthetic peptides: Evidence that localization of peptide-specific CTLs is crucial for protection against malaria
    • + T-cell protective immunity induced by immunization with Plasmodium berghei CS protein derived synthetic peptides: evidence that localization of peptide-specific CTLs is crucial for protection against malaria. Immunol Lett 46:199, 1995.
    • (1995) Immunol Lett , vol.46 , pp. 199
    • Renggli, J.1    Valmori, D.2    Romero, J.F.3    Eberl, G.4    Romero, P.5    Betschart, B.6    Corradin, G.7
  • 103
    • 0031255317 scopus 로고    scopus 로고
    • Induction of protective CTL responses against Plasmodium yoelii circumsporozoite protein by immunization with peptides
    • in press
    • Franke ED, Corradin G, Hoffman SL: Induction of protective CTL responses against Plasmodium yoelii circumsporozoite protein by immunization with peptides. J Immunol (in press).
    • J Immunol
    • Franke, E.D.1    Corradin, G.2    Hoffman, S.L.3
  • 104
    • 0029064432 scopus 로고
    • Identification of HIV protein derived cytotoxic T lymphocyte (CTL) epitopes for their possible use as synthetic vaccine
    • Brander C, Pichler WJ, Corradin G: Identification of HIV protein derived cytotoxic T lymphocyte (CTL) epitopes for their possible use as synthetic vaccine. Clin Exp Immunol 101:107, 1995.
    • (1995) Clin Exp Immunol , vol.101 , pp. 107
    • Brander, C.1    Pichler, W.J.2    Corradin, G.3
  • 105
    • 0028876917 scopus 로고
    • Development of a lipopeptide-based therapeutic vaccine to treat chronic HBV infection. I. Induction of a primary cytotoxic T lymphocyte response in humans
    • Vitiello A, Ishioka G, Grey HM, Rose R, Farness P, LaFond R, Yuan L, Chisari FV, Furze J, Bartholomeuz R, et al.: Development of a lipopeptide-based therapeutic vaccine to treat chronic HBV infection. I. Induction of a primary cytotoxic T lymphocyte response in humans. J Clin Invest 95:341, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 341
    • Vitiello, A.1    Ishioka, G.2    Grey, H.M.3    Rose, R.4    Farness, P.5    LaFond, R.6    Yuan, L.7    Chisari, F.V.8    Furze, J.9    Bartholomeuz, R.10
  • 106
    • 0028226287 scopus 로고
    • Peptide-antibody conjugates for tumor therapy: A MHC-class II-restricted tetanus toxin peptide coupled to an anti-Ig light chain antibody can induce cytotoxic lysis of a human B-cell lymphoma by specific CD4 T cells
    • Yu Z, Healy F, Valmori D, Escobar P, Corradin G, Mach JP: Peptide-antibody conjugates for tumor therapy: a MHC-class II-restricted tetanus toxin peptide coupled to an anti-Ig light chain antibody can induce cytotoxic lysis of a human B-cell lymphoma by specific CD4 T cells. Int J Cancer 56:244, 1994.
    • (1994) Int J Cancer , vol.56 , pp. 244
    • Yu, Z.1    Healy, F.2    Valmori, D.3    Escobar, P.4    Corradin, G.5    Mach, J.P.6


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