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Volumn 46, Issue 3, 2009, Pages 366-374

Altered peptide ligands can modify the Th2 T cell response to the immunodominant 161-175 peptide of LACK (Leishmania homolog for the receptor of activated C kinase)

Author keywords

Agonists; Altered peptide ligands; Core determinant; Flanking residues; I Ad; LACK; Leishmania; T cell receptor; Th1 Th2

Indexed keywords

ALTERED PEPTIDE LIGAND; CELL PROTEIN; GAMMA INTERFERON; INTERLEUKIN 4; LACK 161-175 PEPTIDE; PEPTIDE VACCINE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 57749104693     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.10.024     Document Type: Article
Times cited : (10)

References (41)
  • 1
    • 33645122173 scopus 로고    scopus 로고
    • Antagonists and non-toxic variants of the dominant wheat gliadin T cell epitope in coeliac disease
    • Anderson R.P., van Heel D.A., Tye-Din J.A., Jewell D.P., and Hill A.V. Antagonists and non-toxic variants of the dominant wheat gliadin T cell epitope in coeliac disease. Gut 55 (2006) 485-491
    • (2006) Gut , vol.55 , pp. 485-491
    • Anderson, R.P.1    van Heel, D.A.2    Tye-Din, J.A.3    Jewell, D.P.4    Hill, A.V.5
  • 2
    • 0037100296 scopus 로고    scopus 로고
    • The majority of immunogenic epitopes generate CD4+ T cells that are dependent on MHC class II-bound peptide-flanking residues
    • Arnold P.Y., La Gruta N.L., Miller T., Vignali K.M., Adams P.S., Woodland D.L., and Vignali D.A. The majority of immunogenic epitopes generate CD4+ T cells that are dependent on MHC class II-bound peptide-flanking residues. J. Immunol. 169 (2002) 739-749
    • (2002) J. Immunol. , vol.169 , pp. 739-749
    • Arnold, P.Y.1    La Gruta, N.L.2    Miller, T.3    Vignali, K.M.4    Adams, P.S.5    Woodland, D.L.6    Vignali, D.A.7
  • 3
    • 17044415359 scopus 로고    scopus 로고
    • Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design
    • Borbulevych O.Y., Baxter T.K., Yu Z., Restifo N.P., and Baker B.M. Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design. J. Immunol. 174 (2005) 4812-4820
    • (2005) J. Immunol. , vol.174 , pp. 4812-4820
    • Borbulevych, O.Y.1    Baxter, T.K.2    Yu, Z.3    Restifo, N.P.4    Baker, B.M.5
  • 4
    • 0030802693 scopus 로고    scopus 로고
    • T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TCR V region usage
    • Carson R.T., Vignali K.M., Woodland D.L., and Vignali D.A. T cell receptor recognition of MHC class II-bound peptide flanking residues enhances immunogenicity and results in altered TCR V region usage. Immunity 7 (1997) 387-399
    • (1997) Immunity , vol.7 , pp. 387-399
    • Carson, R.T.1    Vignali, K.M.2    Woodland, D.L.3    Vignali, D.A.4
  • 6
    • 34147119079 scopus 로고    scopus 로고
    • Synthetic anticancer vaccine candidates: rational design of antigenic peptide mimetics that activate tumor-specific T-cells
    • Douat-Casassus C., Marchand-Geneste N., Diez E., Gervois N., Jotereau F., and Quideau S. Synthetic anticancer vaccine candidates: rational design of antigenic peptide mimetics that activate tumor-specific T-cells. J. Med. Chem. 50 (2007) 1598-1609
    • (2007) J. Med. Chem. , vol.50 , pp. 1598-1609
    • Douat-Casassus, C.1    Marchand-Geneste, N.2    Diez, E.3    Gervois, N.4    Jotereau, F.5    Quideau, S.6
  • 7
    • 0028827374 scopus 로고
    • Molecular analysis of a heteroclitic T cell response to the immunodominant epitope of sperm whale myoglobin. Implications for peptide partial agonists
    • England R.D., Kullberg M.C., Cornette J.L., and Berzofsky J.A. Molecular analysis of a heteroclitic T cell response to the immunodominant epitope of sperm whale myoglobin. Implications for peptide partial agonists. J. Immunol. 155 (1995) 4295-4306
    • (1995) J. Immunol. , vol.155 , pp. 4295-4306
    • England, R.D.1    Kullberg, M.C.2    Cornette, J.L.3    Berzofsky, J.A.4
  • 8
    • 34848898406 scopus 로고    scopus 로고
    • Quantitative challenges in understanding ligand discrimination by alphabeta T cells
    • Feinerman O., Germain R.N., and Altan-Bonnet G. Quantitative challenges in understanding ligand discrimination by alphabeta T cells. Mol. Immunol. 45 (2008) 619-631
    • (2008) Mol. Immunol. , vol.45 , pp. 619-631
    • Feinerman, O.1    Germain, R.N.2    Altan-Bonnet, G.3
  • 9
    • 0345222527 scopus 로고    scopus 로고
    • A single intramuscular injection with an adenovirus-expressing IL-12 protects BALB/c mice against Leishmania major infection, while treatment with an IL-4-expressing vector increases disease susceptibility in B10.D2 mice
    • Gabaglia C.R., Pedersen B., Hitt M., Burdin N., Sercarz E.E., Graham F.L., Gauldie J., and Braciak T.A. A single intramuscular injection with an adenovirus-expressing IL-12 protects BALB/c mice against Leishmania major infection, while treatment with an IL-4-expressing vector increases disease susceptibility in B10.D2 mice. J. Immunol. 162 (1999) 753-760
    • (1999) J. Immunol. , vol.162 , pp. 753-760
    • Gabaglia, C.R.1    Pedersen, B.2    Hitt, M.3    Burdin, N.4    Sercarz, E.E.5    Graham, F.L.6    Gauldie, J.7    Braciak, T.A.8
  • 10
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke J., Carfi A., and Wiley D.C. Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. Embo J. 19 (2000) 5611-5624
    • (2000) Embo J. , vol.19 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 11
    • 30744477705 scopus 로고    scopus 로고
    • Impairment of alternative macrophage activation delays cutaneous leishmaniasis in nonhealing BALB/c mice
    • Holscher C., Arendse B., Schwegmann A., Myburgh E., and Brombacher F. Impairment of alternative macrophage activation delays cutaneous leishmaniasis in nonhealing BALB/c mice. J. Immunol. 176 (2006) 1115-1121
    • (2006) J. Immunol. , vol.176 , pp. 1115-1121
    • Holscher, C.1    Arendse, B.2    Schwegmann, A.3    Myburgh, E.4    Brombacher, F.5
  • 14
    • 0029849205 scopus 로고    scopus 로고
    • Resistance to Leishmania major induced by tolerance to a single antigen
    • Julia V., Rassoulzadegan M., and Glaichenhaus N. Resistance to Leishmania major induced by tolerance to a single antigen. Science 274 (1996) 421-423
    • (1996) Science , vol.274 , pp. 421-423
    • Julia, V.1    Rassoulzadegan, M.2    Glaichenhaus, N.3
  • 15
    • 9244229564 scopus 로고    scopus 로고
    • The Leishmania major LACK antigen with an immunodominant epitope at amino acids 156-173 is not required for early Th2 development in BALB/c mice
    • Kelly B.L., and Locksley R.M. The Leishmania major LACK antigen with an immunodominant epitope at amino acids 156-173 is not required for early Th2 development in BALB/c mice. Infect. Immun. 72 (2004) 6924-6931
    • (2004) Infect. Immun. , vol.72 , pp. 6924-6931
    • Kelly, B.L.1    Locksley, R.M.2
  • 17
    • 0028849807 scopus 로고
    • Major histocompatibility complex binding affinity of an antigenic determinant is crucial for the differential secretion of interleukin 4/5 or interferon gamma by T cells
    • Kumar V., Bhardwaj V., Soares L., Alexander J., Sette A., and Sercarz E. Major histocompatibility complex binding affinity of an antigenic determinant is crucial for the differential secretion of interleukin 4/5 or interferon gamma by T cells. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 9510-9514
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9510-9514
    • Kumar, V.1    Bhardwaj, V.2    Soares, L.3    Alexander, J.4    Sette, A.5    Sercarz, E.6
  • 19
    • 8444236620 scopus 로고    scopus 로고
    • Clonal selection of helper T cells is determined by an affinity threshold with no further skewing of TCR binding properties
    • Malherbe L., Hausl C., Teyton L., and McHeyzer-Williams M.G. Clonal selection of helper T cells is determined by an affinity threshold with no further skewing of TCR binding properties. Immunity 21 (2004) 669-679
    • (2004) Immunity , vol.21 , pp. 669-679
    • Malherbe, L.1    Hausl, C.2    Teyton, L.3    McHeyzer-Williams, M.G.4
  • 20
    • 0031595750 scopus 로고    scopus 로고
    • Modulation of the immunogenicity of antigenic determinants by their flanking residues
    • Moudgil K.D., Sercarz E.E., and Grewal I.S. Modulation of the immunogenicity of antigenic determinants by their flanking residues. Immunol. Today 19 (1998) 217-220
    • (1998) Immunol. Today , vol.19 , pp. 217-220
    • Moudgil, K.D.1    Sercarz, E.E.2    Grewal, I.S.3
  • 22
    • 0031966005 scopus 로고    scopus 로고
    • How the MHC selects Th1/Th2 immunity
    • Murray J.S. How the MHC selects Th1/Th2 immunity. Immunol. Today 19 (1998) 157-163
    • (1998) Immunol. Today , vol.19 , pp. 157-163
    • Murray, J.S.1
  • 23
    • 0027989733 scopus 로고
    • Major histocompatibility complex regulation of T helper functions mapped to a peptide C terminus that controls ligand density
    • Murray J.S., Ferrandis-Edwards D., Wolfe C.J., and Schountz T. Major histocompatibility complex regulation of T helper functions mapped to a peptide C terminus that controls ligand density. Eur. J. Immunol. 24 (1994) 2337-2344
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2337-2344
    • Murray, J.S.1    Ferrandis-Edwards, D.2    Wolfe, C.J.3    Schountz, T.4
  • 24
    • 38049063424 scopus 로고    scopus 로고
    • An altered peptide ligand of type II collagen suppresses autoimmune arthritis
    • Myers L.K., Tang B., Rosioniec E.F., Stuart J.M., and Kang A.H. An altered peptide ligand of type II collagen suppresses autoimmune arthritis. Crit. Rev. Immunol. 27 (2007) 345-356
    • (2007) Crit. Rev. Immunol. , vol.27 , pp. 345-356
    • Myers, L.K.1    Tang, B.2    Rosioniec, E.F.3    Stuart, J.M.4    Kang, A.H.5
  • 25
    • 0026667402 scopus 로고
    • Identification of the naturally processed form of hen egg white lysozyme bound to the murine major histocompatibility complex class II molecule I-Ak
    • Nelson C.A., Roof R.W., McCourt D.W., and Unanue E.R. Identification of the naturally processed form of hen egg white lysozyme bound to the murine major histocompatibility complex class II molecule I-Ak. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 7380-7383
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7380-7383
    • Nelson, C.A.1    Roof, R.W.2    McCourt, D.W.3    Unanue, E.R.4
  • 26
  • 28
    • 0028261582 scopus 로고
    • Use of global amino acid replacements to define the requirements for MHC binding and T cell recognition of moth cytochrome c (93-103)
    • Reay P.A., Kantor R.M., and Davis M.M. Use of global amino acid replacements to define the requirements for MHC binding and T cell recognition of moth cytochrome c (93-103). J. Immunol. 152 (1994) 3946-3957
    • (1994) J. Immunol. , vol.152 , pp. 3946-3957
    • Reay, P.A.1    Kantor, R.M.2    Davis, M.M.3
  • 29
    • 0027339408 scopus 로고
    • TH1 and TH2 cell antigen receptors in experimental leishmaniasis
    • Reiner S.L., Wang Z.E., Hatam F., Scott P., and Locksley R.M. TH1 and TH2 cell antigen receptors in experimental leishmaniasis. Science 259 (1993) 1457-1460
    • (1993) Science , vol.259 , pp. 1457-1460
    • Reiner, S.L.1    Wang, Z.E.2    Hatam, F.3    Scott, P.4    Locksley, R.M.5
  • 32
    • 0036831673 scopus 로고    scopus 로고
    • The immunology of susceptibility and resistance to Leishmania major in mice
    • Sacks D., and Noben-Trauth N. The immunology of susceptibility and resistance to Leishmania major in mice. Nat. Rev. Immunol. 2 (2002) 845-858
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 845-858
    • Sacks, D.1    Noben-Trauth, N.2
  • 34
    • 0030294373 scopus 로고    scopus 로고
    • MHC genotype controls the capacity of ligand density to switch T helper (Th)-1/Th-2 priming in vivo
    • Schountz T., Kasselman J.P., Martinson F.A., Brown L., and Murray J.S. MHC genotype controls the capacity of ligand density to switch T helper (Th)-1/Th-2 priming in vivo. J. Immunol. 157 (1996) 3893-3901
    • (1996) J. Immunol. , vol.157 , pp. 3893-3901
    • Schountz, T.1    Kasselman, J.P.2    Martinson, F.A.3    Brown, L.4    Murray, J.S.5
  • 35
    • 0032033678 scopus 로고    scopus 로고
    • Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • Scott C.A., Peterson P.A., Teyton L., and Wilson I.A. Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity 8 (1998) 319-329
    • (1998) Immunity , vol.8 , pp. 319-329
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 36
    • 0141832121 scopus 로고    scopus 로고
    • MHC-guided processing: binding of large antigen fragments
    • Sercarz E.E., and Maverakis E. MHC-guided processing: binding of large antigen fragments. Nat. Rev. Immunol. 3 (2003) 621-629
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 621-629
    • Sercarz, E.E.1    Maverakis, E.2
  • 37
    • 0023257028 scopus 로고
    • Structural characteristics of an antigen required for its interaction with Ia and recognition by T cells
    • Sette A., Buus S., Colon S., Smith J.A., Miles C., and Grey H.M. Structural characteristics of an antigen required for its interaction with Ia and recognition by T cells. Nature 328 (1987) 395-399
    • (1987) Nature , vol.328 , pp. 395-399
    • Sette, A.1    Buus, S.2    Colon, S.3    Smith, J.A.4    Miles, C.5    Grey, H.M.6
  • 38
    • 0023819396 scopus 로고
    • I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif
    • Sette A., Buus S., Colon S., Miles C., and Grey H.M. I-Ad-binding peptides derived from unrelated protein antigens share a common structural motif. J. Immunol. 141 (1988) 45-48
    • (1988) J. Immunol. , vol.141 , pp. 45-48
    • Sette, A.1    Buus, S.2    Colon, S.3    Miles, C.4    Grey, H.M.5
  • 40
    • 33845932421 scopus 로고    scopus 로고
    • An altered peptide ligand for naive cytotoxic T lymphocyte epitope of TRP-2(180-188) enhanced immunogenicity
    • Tang Y., Lin Z., Ni B., Wei J., Han J., Wang H., and Wu Y. An altered peptide ligand for naive cytotoxic T lymphocyte epitope of TRP-2(180-188) enhanced immunogenicity. Cancer Immunol. Immunother. 56 (2007) 319-329
    • (2007) Cancer Immunol. Immunother. , vol.56 , pp. 319-329
    • Tang, Y.1    Lin, Z.2    Ni, B.3    Wei, J.4    Han, J.5    Wang, H.6    Wu, Y.7


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