메뉴 건너뛰기




Volumn 9, Issue 1, 1996, Pages 67-77

MHC class II presentation of human acetylcholine receptor in Myasthenia gravis: Binding of synthetic gamma subunit sequences to DR molecules

Author keywords

Acetylcholine receptor; CD4+ T cell epitopes; DR binding; Myasthenia gravis

Indexed keywords

AUTOANTIGEN; CD4 ANTIGEN; CHOLINERGIC RECEPTOR; HLA DR ANTIGEN; SYNTHETIC PEPTIDE;

EID: 0029916221     PISSN: 08968411     EISSN: None     Source Type: Journal    
DOI: 10.1006/jaut.1996.0009     Document Type: Article
Times cited : (6)

References (51)
  • 1
  • 3
    • 0022454719 scopus 로고
    • Molecular distinction between fetal and adult forms of muscle acetylcholine receptor
    • Mishina M., Takai T., Imoto K., Noda M., Takahashi T., Numa S. et al. 1986. Molecular distinction between fetal and adult forms of muscle acetylcholine receptor. Nature 321: 406-411
    • (1986) Nature , vol.321 , pp. 406-411
    • Mishina, M.1    Takai, T.2    Imoto, K.3    Noda, M.4    Takahashi, T.5    Numa, S.6
  • 4
    • 0023986105 scopus 로고
    • Immunological evidence for a change in subunits of the acetylcholine receptor in developing and denervated rat muscle
    • Gu Y., Hall Z.W. 1988. Immunological evidence for a change in subunits of the acetylcholine receptor in developing and denervated rat muscle. Neuron 1: 117-125
    • (1988) Neuron , vol.1 , pp. 117-125
    • Gu, Y.1    Hall, Z.W.2
  • 6
    • 0025144459 scopus 로고
    • Adult thymus expresses an embryonic nicotinic acetylcholine receptor-like protein
    • Nelson S., Conti-Tronconi B.M. 1990. Adult thymus expresses an embryonic nicotinic acetylcholine receptor-like protein. J. Neuroimmunol. 29: 81-92
    • (1990) J. Neuroimmunol. , vol.29 , pp. 81-92
    • Nelson, S.1    Conti-Tronconi, B.M.2
  • 8
    • 0024600918 scopus 로고
    • Autoimmune T lymphocytes in myasthenia gravis: Determination of target epitopes using T lines and recombinant products of the mouse nicotinic acetylcholine receptor gene
    • Melms A., Chrestel S., Schalke B.C.G., Wekerle H., Mauron A., Ballivet M. et al. 1988. Autoimmune T lymphocytes in myasthenia gravis: determination of target epitopes using T lines and recombinant products of the mouse nicotinic acetylcholine receptor gene. J. Clin. Invest. 83: 285-289
    • (1988) J. Clin. Invest. , vol.83 , pp. 285-289
    • Melms, A.1    Chrestel, S.2    Schalke, B.C.G.3    Wekerle, H.4    Mauron, A.5    Ballivet, M.6
  • 9
    • 0022474111 scopus 로고
    • Antibodies to acetylcholine receptor and tetanus toxoid: In vitro synthesis by thymic lymphocytes
    • Lisak R.P., Levinson A.I., Zweiman B., Kornstein M.J. 1986. Antibodies to acetylcholine receptor and tetanus toxoid: in vitro synthesis by thymic lymphocytes. J. Immunol. 1376: 1221-1225
    • (1986) J. Immunol. , vol.1376 , pp. 1221-1225
    • Lisak, R.P.1    Levinson, A.I.2    Zweiman, B.3    Kornstein, M.J.4
  • 10
    • 0026648331 scopus 로고
    • Transplantation of thymic autoimmune microenvironment to severe combined immunodeficiency mice
    • Schöenbeck S., Padberg F., Hohlfeld R., Wekerle H. 1992. Transplantation of thymic autoimmune microenvironment to severe combined immunodeficiency mice. J. Clin. Invest. 90: 245-250
    • (1992) J. Clin. Invest. , vol.90 , pp. 245-250
    • Schöenbeck, S.1    Padberg, F.2    Hohlfeld, R.3    Wekerle, H.4
  • 11
    • 0018352431 scopus 로고
    • Antibody from patients with myasthenia gravis recognize determinants unique to extrajunctional acetylcholine receptors
    • Weinberg C.B., Hall Z.W. 1979. Antibody from patients with myasthenia gravis recognize determinants unique to extrajunctional acetylcholine receptors. Proc. Natl. Acad. Sci. USA 76: 504-508
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 504-508
    • Weinberg, C.B.1    Hall, Z.W.2
  • 12
    • 0026090812 scopus 로고
    • T cells in myasthenia gravis specific for embryonic muscle acetylcholine receptor
    • Protti M.P., Manfredi A.A., Howard J.F. Jr., Conti-Tronconi B.M. 1991. T cells in myasthenia gravis specific for embryonic muscle acetylcholine receptor. Neurology 41: 1809-1814
    • (1991) Neurology , vol.41 , pp. 1809-1814
    • Protti, M.P.1    Manfredi, A.A.2    Howard J.F., Jr.3    Conti-Tronconi, B.M.4
  • 14
    • 0027176664 scopus 로고
    • Myasthenia gravis: Epitopes recognized by autoimmune Th cells on the γ and δ subunit of the muscle acetylcholine receptor
    • Manfredi A.A., Protti M.P., Wu X.D., Howard J.F. Jr., Conti-Tronconi B.M. 1993. Myasthenia gravis: epitopes recognized by autoimmune Th cells on the γ and δ subunit of the muscle acetylcholine receptor. J. Clin. Invest. 92: 1055-1067
    • (1993) J. Clin. Invest. , vol.92 , pp. 1055-1067
    • Manfredi, A.A.1    Protti, M.P.2    Wu, X.D.3    Howard J.F., Jr.4    Conti-Tronconi, B.M.5
  • 15
    • 0025094484 scopus 로고
    • Why are eye muscles frequently involved in myasthenia gravis?
    • Kaminski H.J., Maas E., Spiegel P., Ruff R.L. 1990. Why are eye muscles frequently involved in myasthenia gravis? Neurology 40: 1663-1669
    • (1990) Neurology , vol.40 , pp. 1663-1669
    • Kaminski, H.J.1    Maas, E.2    Spiegel, P.3    Ruff, R.L.4
  • 16
    • 0027315047 scopus 로고
    • The 'embryonic' gamma subunit of the nicotinic acetylcholine receptor is expressed in adult extraocular muscle
    • Horton R.M., Manfredi A.A., Conti-Tronconi B.M. 1993. The 'embryonic' gamma subunit of the nicotinic acetylcholine receptor is expressed in adult extraocular muscle. Neurology 43: 983-986
    • (1993) Neurology , vol.43 , pp. 983-986
    • Horton, R.M.1    Manfredi, A.A.2    Conti-Tronconi, B.M.3
  • 17
    • 0022397922 scopus 로고
    • Genetic restriction of autoreactive acetylcholine receptor-specific T lymphocytes in Myasthenia Gravis
    • Hohlfeld R., Conti-Tronconi B.M., Kalies I., Bertrams J., Toyka K.V. 1985. Genetic restriction of autoreactive acetylcholine receptor-specific T lymphocytes in Myasthenia Gravis. J. Immunol. 135: 2393-2399
    • (1985) J. Immunol. , vol.135 , pp. 2393-2399
    • Hohlfeld, R.1    Conti-Tronconi, B.M.2    Kalies, I.3    Bertrams, J.4    Toyka, K.V.5
  • 18
    • 0026575557 scopus 로고
    • T cells from normal and myasthenic individuals recognize the human acetylcholine receptor: Heterogeneity of antigenic sites on the α-subunit
    • Melms A., Malcherek G., Gern U., Wietholter H., Muller C.A., Schoepfer R. et al. 1992. T cells from normal and myasthenic individuals recognize the human acetylcholine receptor: heterogeneity of antigenic sites on the α-subunit. Ann. Neurol. 31: 311-318
    • (1992) Ann. Neurol. , vol.31 , pp. 311-318
    • Melms, A.1    Malcherek, G.2    Gern, U.3    Wietholter, H.4    Muller, C.A.5    Schoepfer, R.6
  • 21
    • 0028345550 scopus 로고
    • Human acetylcholine receptor presentation in Myasthenia gravis: DR restriction of autoimmune T epitopes and binding of synthetic receptor sequences to DR molecules
    • Manfredi A.A., Yuen M.H., Moiola L., Maria P.P., Conti-Tronconi B.M. 1994. Human acetylcholine receptor presentation in Myasthenia gravis: DR restriction of autoimmune T epitopes and binding of synthetic receptor sequences to DR molecules. J. Immunol. 152: 4165-4174
    • (1994) J. Immunol. , vol.152 , pp. 4165-4174
    • Manfredi, A.A.1    Yuen, M.H.2    Moiola, L.3    Maria, P.P.4    Conti-Tronconi, B.M.5
  • 22
    • 0025013141 scopus 로고
    • Characterization of the specificity of peptide binding to four DR haplotypes
    • O'Sullivan D., Sidney J., Appella E., Walker L., Phillips L., Colon S.M. et al. 1990. Characterization of the specificity of peptide binding to four DR haplotypes. J. Immunol. 145: 1799-1808
    • (1990) J. Immunol. , vol.145 , pp. 1799-1808
    • O'Sullivan, D.1    Sidney, J.2    Appella, E.3    Walker, L.4    Phillips, L.5    Colon, S.M.6
  • 23
    • 0025273755 scopus 로고
    • Limit of T cell tolerance to self protein by peptide presentation
    • Schild H., Rotzschke O., Kalbacher H., Rammensee H.-G. 1990. Limit of T cell tolerance to self protein by peptide presentation. Science 247: 1587-1589
    • (1990) Science , vol.247 , pp. 1587-1589
    • Schild, H.1    Rotzschke, O.2    Kalbacher, H.3    Rammensee, H.-G.4
  • 24
    • 0027217789 scopus 로고
    • Three-dimensional structure of the human class I histocompatibility antigen HLA-DR1
    • Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L. et al. 1993. Three-dimensional structure of the human class I histocompatibility antigen HLA-DR1. Nature 364: 33-39
    • (1993) Nature , vol.364 , pp. 33-39
    • Brown, J.H.1    Jardetzky, T.S.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Strominger, J.L.6
  • 25
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern L.J., Brown J.H., Jardetzky T.S., Gorga J.C., Urban R.G., Strominger J.L. et al. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368: 215-221
    • (1994) Nature , vol.368 , pp. 215-221
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0021925942 scopus 로고
    • Cloning and sequence analysis of human genomic DNA encoding the γ subunit precursor of muscle acetylcholine receptor
    • Shibahara S., Kubo T., Perski H.J., Takahashi H., Noda M., Numa S. 1985. Cloning and sequence analysis of human genomic DNA encoding the γ subunit precursor of muscle acetylcholine receptor. Eur. J. Biochem. 146: 15-21
    • (1985) Eur. J. Biochem. , vol.146 , pp. 15-21
    • Shibahara, S.1    Kubo, T.2    Perski, H.J.3    Takahashi, H.4    Noda, M.5    Numa, S.6
  • 28
    • 0000478940 scopus 로고
    • General method for the rapid solid phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual amino acids
    • Houghten R.A. 1985. General method for the rapid solid phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual amino acids. Proc. Natl. Acad. Sci. USA 82: 5131-5135
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5131-5135
    • Houghten, R.A.1
  • 29
    • 0026703523 scopus 로고
    • Use of universally antigenic tetanus toxin T cell epitopes as carriers for human vaccination
    • Valmori D., Pessi A., Bianchi E., Corradin G. 1992. Use of universally antigenic tetanus toxin T cell epitopes as carriers for human vaccination. J. Immunol. 149: 717-721
    • (1992) J. Immunol. , vol.149 , pp. 717-721
    • Valmori, D.1    Pessi, A.2    Bianchi, E.3    Corradin, G.4
  • 31
    • 0027203171 scopus 로고
    • An assay for simultaneous multiple determination of peptide binding to MHC class II molecules
    • Manfredi A.A., Yuen M.-H., Raftery M.A., Conti-Tronconi B.M. 1993. An assay for simultaneous multiple determination of peptide binding to MHC class II molecules. Anal. Biochem. 211: 267-273
    • (1993) Anal. Biochem. , vol.211 , pp. 267-273
    • Manfredi, A.A.1    Yuen, M.-H.2    Raftery, M.A.3    Conti-Tronconi, B.M.4
  • 34
    • 0024464931 scopus 로고
    • Sequences outside a minimal immunodominant site exert negative effects on recognition by staphylococcal nuclease-specific T cell clones
    • Vacchio M.S., Berzofsky J.A., Krzych U., Smith J.A., Hodes R.J., Finnegan A. 1989. Sequences outside a minimal immunodominant site exert negative effects on recognition by staphylococcal nuclease-specific T cell clones. J. Immunol. 143: 2814-2819
    • (1989) J. Immunol. , vol.143 , pp. 2814-2819
    • Vacchio, M.S.1    Berzofsky, J.A.2    Krzych, U.3    Smith, J.A.4    Hodes, R.J.5    Finnegan, A.6
  • 35
    • 0026733449 scopus 로고
    • Predominant naturally processed peptides bound to HLA DR1 are derived from MHC-related molecules and are heterogeneous in size
    • Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A. et al. 1992. Predominant naturally processed peptides bound to HLA DR1 are derived from MHC-related molecules and are heterogeneous in size. Nature 358: 764-768
    • (1992) Nature , vol.358 , pp. 764-768
    • Chicz, R.M.1    Urban, R.G.2    Lane, W.S.3    Gorga, J.C.4    Stern, L.J.5    Vignali, D.A.A.6
  • 37
    • 0024428816 scopus 로고
    • How some T cells escape tolerance induction
    • Gammon G., Sercarz E. 1989. How some T cells escape tolerance induction. Nature 342: 183-185
    • (1989) Nature , vol.342 , pp. 183-185
    • Gammon, G.1    Sercarz, E.2
  • 38
    • 0027439013 scopus 로고
    • An autoantigenic T cell epitope forms unstable complexes with class II MHC: A novel route for escape from tolerance induction
    • Fairchild P.J., Wildgoose R., Atherton E., Webb S., Wraith D.C. 1993. An autoantigenic T cell epitope forms unstable complexes with class II MHC: A novel route for escape from tolerance induction. International Immunol. 5: 1151-1158
    • (1993) International Immunol. , vol.5 , pp. 1151-1158
    • Fairchild, P.J.1    Wildgoose, R.2    Atherton, E.3    Webb, S.4    Wraith, D.C.5
  • 39
    • 0025762970 scopus 로고
    • Acetylcholine receptor specific T lymphocyte clones in the normal human immune repertoire: Target epitopes, HLA restriction, and membrane phenotypes
    • Salvetti M., Jung S., Chang S.-F., Will H., Schalke B.C.G., Wekerle H. 1991. Acetylcholine receptor specific T lymphocyte clones in the normal human immune repertoire: target epitopes, HLA restriction, and membrane phenotypes. Ann. Neurol. 29: 508-516
    • (1991) Ann. Neurol. , vol.29 , pp. 508-516
    • Salvetti, M.1    Jung, S.2    Chang, S.-F.3    Will, H.4    Schalke, B.C.G.5    Wekerle, H.6
  • 42
    • 0027151841 scopus 로고
    • Characterization of endogenous peptides bound to purified HLA-DR molecules and their absence from invariant chain-associated αβ dimers
    • Newcombe J.R., Cresswell P. 1993. Characterization of endogenous peptides bound to purified HLA-DR molecules and their absence from invariant chain-associated αβ dimers. J. Immunol. 150: 499-507
    • (1993) J. Immunol. , vol.150 , pp. 499-507
    • Newcombe, J.R.1    Cresswell, P.2
  • 43
    • 0027296020 scopus 로고
    • HLA DR4w4-binding motifs illustrate the biochemical basis of degeneracy and specificity in peptide-DR interactions
    • Sette A., Sidney J., Oseroff C., del Guercio M.-F., Southwood S., Arrhenius T. et al. 1993. HLA DR4w4-binding motifs illustrate the biochemical basis of degeneracy and specificity in peptide-DR interactions. J. Immunol. 151: 3163-3170
    • (1993) J. Immunol. , vol.151 , pp. 3163-3170
    • Sette, A.1    Sidney, J.2    Oseroff, C.3    Del Guercio, M.-F.4    Southwood, S.5    Arrhenius, T.6
  • 44
    • 0026706746 scopus 로고
    • Identification of a motif for HLA-DR1 binding peptides using M13 display libraries
    • Hammer J., Takacs B., Sinigaglia E 1992. Identification of a motif for HLA-DR1 binding peptides using M13 display libraries. J. Exp. Med. 176: 1007-1013
    • (1992) J. Exp. Med. , vol.176 , pp. 1007-1013
    • Hammer, J.1    Takacs, B.2    Sinigaglia, E.3
  • 46
    • 0025296990 scopus 로고
    • Analysis of peptide residues interacting with MHC molecule or T cell receptor. Can a peptide bind in more than one way to the same MHC molecule?
    • Kurata A., Berzofsky J.A. 1990. Analysis of peptide residues interacting with MHC molecule or T cell receptor. Can a peptide bind in more than one way to the same MHC molecule? J. Immunol. 144: 4526-4535
    • (1990) J. Immunol. , vol.144 , pp. 4526-4535
    • Kurata, A.1    Berzofsky, J.A.2
  • 47
    • 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 H.-G., Melms A. 1995. Supermotifs enable natural invariant chain-derived peptides to interact with many major histocompatibility complex-class II molecules. J. Exp. Med. 181: 527-536
    • (1995) J. Exp. Med. , vol.181 , pp. 527-536
    • Malcherek, G.1    Gnau, V.2    Jung, G.3    Rammensee, H.-G.4    Melms, A.5
  • 48
    • 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. 1995. 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: 677-683
    • (1995) J. Exp. Med. , vol.181 , pp. 677-683
    • Sette, A.1    Southwood, S.2    Miller, J.3    Appella, E.4
  • 49
    • 0025323546 scopus 로고
    • High-affinity binding of an influence hemagglutinin-derived peptide to purified HLA-DR
    • Roche P.A., Cresswell P. 1990. High-affinity binding of an influence hemagglutinin-derived peptide to purified HLA-DR. J. Immunol. 144: 1849-1856
    • (1990) J. Immunol. , vol.144 , pp. 1849-1856
    • Roche, P.A.1    Cresswell, P.2
  • 51
    • 0027937713 scopus 로고
    • Precise prediction of major histocompatibility complex class II-peptide interaction based on peptide side chain scanning
    • Hammer J., Bono E., Gallazzi F., Belunis C., Nagy Z., Sinigaglia F. 1994. Precise prediction of major histocompatibility complex class II-peptide interaction based on peptide side chain scanning. J. Exp. Med. 180: 2353-2358
    • (1994) J. Exp. Med. , vol.180 , pp. 2353-2358
    • Hammer, J.1    Bono, E.2    Gallazzi, F.3    Belunis, C.4    Nagy, Z.5    Sinigaglia, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.