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Volumn 61, Issue 3, 2013, Pages 747-754

Immunogenic peptides can be detected in whole gluten by transamidating highly susceptible glutamine residues: Implication in the search for gluten-free cereals

Author keywords

celiac disease; cereals; gluten epitopes; tissue transglutaminase

Indexed keywords

CELIAC DISEASE; CEREALS; GLUTEN EPITOPES; GLUTEN PEPTIDES; GLUTEN-FREE; IMMUNE ACTIVATION; IMMUNOGENICITY; INTESTINAL MUCOSA; MONODANSYLCADAVERINE; NANOSPRAY; PROTEIN EXTRACT; T CELLS; TANDEM MASS SPECTROMETRY; TISSUE TRANSGLUTAMINASE;

EID: 84872868221     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf3040435     Document Type: Article
Times cited : (7)

References (37)
  • 2
    • 0027319208 scopus 로고
    • Gliadin-specific, HLA-DQ(α 1*0501,β 1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients
    • Lundin, K. E.; Scott, H.; Hansen, T.; Paulsen, G.; Halstensen, T. S. Gliadin-specific, HLA-DQ(α 1*0501,β 1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients J. Exp. Med. 1993, 188, 187-196
    • (1993) J. Exp. Med. , vol.188 , pp. 187-196
    • Lundin, K.E.1    Scott, H.2    Hansen, T.3    Paulsen, G.4    Halstensen, T.S.5
  • 3
    • 0030877557 scopus 로고    scopus 로고
    • Gliadin specific, HLA DQ2-restricted T cells are commonly found in small intestinal biopsies from coeliac disease patients, but not from controls
    • Molberg, O.; Kett, K.; Scott, H.; Thorsby, E.; Sollid, L. M.; Lundin, K. E. Gliadin specific, HLA DQ2-restricted T cells are commonly found in small intestinal biopsies from coeliac disease patients, but not from controls Scand. J. Immunol. 1997, 46, 103-109
    • (1997) Scand. J. Immunol. , vol.46 , pp. 103-109
    • Molberg, O.1    Kett, K.2    Scott, H.3    Thorsby, E.4    Sollid, L.M.5    Lundin, K.E.6
  • 4
    • 13144283626 scopus 로고    scopus 로고
    • Small intestinal T cells of celiac disease patients recognize a natural pepsin fragment of gliadin
    • Van de Wal, Y.; Kooy, Y.; van Veelen, P.; Peña, S.; Mearin, L. Small intestinal T cells of celiac disease patients recognize a natural pepsin fragment of gliadin Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 10050-10054
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10050-10054
    • Van De Wal, Y.1    Kooy, Y.2    Van Veelen, P.3    Peña, S.4    Mearin, L.5
  • 5
    • 0031891459 scopus 로고    scopus 로고
    • The majority of gliadin-specific T cell clones from the coeliac small intestinal mucosa produce both interferon and IL4
    • Troncone, R.; Gianfrani, C.; Mazzarella, G.; Greco, L.; Guardiola, J. The majority of gliadin-specific T cell clones from the coeliac small intestinal mucosa produce both interferon and IL4 Dig. Dis. Sci. 1998, 43, 156-161
    • (1998) Dig. Dis. Sci. , vol.43 , pp. 156-161
    • Troncone, R.1    Gianfrani, C.2    Mazzarella, G.3    Greco, L.4    Guardiola, J.5
  • 6
    • 77955634105 scopus 로고    scopus 로고
    • Design of peptide-based immunotherapy and diagnostics for celiac disease based upon comprehensive, quantitative mapping of T-cellepitopes in gluten
    • Tye-Din, J. A.; Stewart, J.; Dromey, J.; Beissbarth, T.; van Heel, D. A. Design of peptide-based immunotherapy and diagnostics for celiac disease based upon comprehensive, quantitative mapping of T-cellepitopes in gluten Sci. Transl. Med. 2010, 2, 41-51
    • (2010) Sci. Transl. Med. , vol.2 , pp. 41-51
    • Tye-Din, J.A.1    Stewart, J.2    Dromey, J.3    Beissbarth, T.4    Van Heel, D.A.5
  • 7
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • Shan, L.; Molberg, Ø.; Parrot, I.; Hausch, F.; Filiz, F. Structural basis for gluten intolerance in celiac sprue Science 2002, 297, 2275-2279
    • (2002) Science , vol.297 , pp. 2275-2279
    • Shan, L.1    Molberg Ø2    Parrot, I.3    Hausch, F.4    Filiz, F.5
  • 8
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • Dieterich, W.; Ehnis, T.; Bauer, M.; Donner, P.; Volta, U. Identification of tissue transglutaminase as the autoantigen of celiac disease Nat. Med. 1997, 3, 797-801
    • (1997) Nat. Med. , vol.3 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2    Bauer, M.3    Donner, P.4    Volta, U.5
  • 9
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • Molberg, Ø.; McAdam, S. N.; Korner, R.; Quarsten, H.; Kristiansen, C. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease Nat. Med. 1998, 4, 713-717
    • (1998) Nat. Med. , vol.4 , pp. 713-717
    • Molberg Ø1    McAdam, S.N.2    Korner, R.3    Quarsten, H.4    Kristiansen, C.5
  • 10
    • 2142764316 scopus 로고    scopus 로고
    • Identification of a gliadin T-cell epitope in coeliac disease: General importance of gliadin deamidation for intestinal T-cell recognition
    • Sjöström, H.; Lundin, K. E.; Molberg, Ø.; Körner, R.; McAdam, S. N. Identification of a gliadin T-cell epitope in coeliac disease: general importance of gliadin deamidation for intestinal T-cell recognition Scand. J. Immunol. 1998, 48, 111-115
    • (1998) Scand. J. Immunol. , vol.48 , pp. 111-115
    • Sjöström, H.1    Lundin, K.E.2    Molberg Ø3    Körner, R.4    McAdam, S.N.5
  • 11
    • 64249115818 scopus 로고    scopus 로고
    • Intestinal T-cell responses to gluten peptides are largely heterogeneous: Implication for a peptide-based therapy in celiac disease
    • Camarca, A.; Anderson, R. P.; Mamone, G.; Fierro, O.; Facchiano, A. Intestinal T-cell responses to gluten peptides are largely heterogeneous: implication for a peptide-based therapy in celiac disease J. Immunol. 2009, 182, 4158-4166
    • (2009) J. Immunol. , vol.182 , pp. 4158-4166
    • Camarca, A.1    Anderson, R.P.2    Mamone, G.3    Fierro, O.4    Facchiano, A.5
  • 12
    • 26844558196 scopus 로고    scopus 로고
    • Identification and analysis of multivalent proteolytically resistant peptides from gluten: Implications for celiac sprue
    • Shan, L.; Qiao, S. W.; Arentz-Hansen, H.; Molberg, Ø.; Gray, G. M. Identification and analysis of multivalent proteolytically resistant peptides from gluten: implications for celiac sprue J. Prot. Res. 2005, 4, 1732-1741
    • (2005) J. Prot. Res. , vol.4 , pp. 1732-1741
    • Shan, L.1    Qiao, S.W.2    Arentz-Hansen, H.3    Molberg Ø4    Gray, G.M.5
  • 13
    • 21244462254 scopus 로고    scopus 로고
    • Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: Importance of proline spacing and glutamine deamidation
    • Qiao, S. W.; Bergseng, E.; Molberg, Ø.; Jung, G.; Fleckenstein, B.; Sollid, L. M. Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: importance of proline spacing and glutamine deamidation J. Immunol. 2005, 175, 254-261
    • (2005) J. Immunol. , vol.175 , pp. 254-261
    • Qiao, S.W.1    Bergseng, E.2    Molberg Ø3    Jung, G.4    Fleckenstein, B.5    Sollid, L.M.6
  • 14
    • 78649512556 scopus 로고    scopus 로고
    • The preferred substrates for transglutaminase 2 in a complex wheat gluten digest are peptide fragments harbouring celiac disease T-cell epitopes
    • Dørum, S.; Arntzen, M. Ø.; Qiao, S. W.; Holm, A.; Koehler, C. J. C. The preferred substrates for transglutaminase 2 in a complex wheat gluten digest are peptide fragments harbouring celiac disease T-cell epitopes PLoS One 2010, 5, e14056
    • (2010) PLoS One , vol.5 , pp. 14056
    • Dørum, S.1    Arntzen M.Ø2    Qiao, S.W.3    Holm, A.4    Koehler, C.J.C.5
  • 15
    • 0036082955 scopus 로고    scopus 로고
    • The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides
    • Vader, W.; Kooy, Y.; Van Veelen, P.; De Ru, A.; Harris, D. The gluten response in children with celiac disease is directed toward multiple gliadin and glutenin peptides Gastroenterology 2002, 122, 1729-1737
    • (2002) Gastroenterology , vol.122 , pp. 1729-1737
    • Vader, W.1    Kooy, Y.2    Van Veelen, P.3    De Ru, A.4    Harris, D.5
  • 16
    • 22044446842 scopus 로고    scopus 로고
    • Innate and adaptive immune responses in celiac disease
    • Gianfrani, C.; Auricchio, S.; Troncone, R. Innate and adaptive immune responses in celiac disease Immunol. Lett. 2005, 99, 141-145
    • (2005) Immunol. Lett. , vol.99 , pp. 141-145
    • Gianfrani, C.1    Auricchio, S.2    Troncone, R.3
  • 17
    • 0038501062 scopus 로고    scopus 로고
    • Association between innate response to gliadin and activation of pathogenic T cells in celiac disease
    • Maiuri, L.; Ciacci, C.; Ricciardelli, I.; Vacca, L.; Raia, V. Association between innate response to gliadin and activation of pathogenic T cells in celiac disease Lancet 2003, 362, 30-37
    • (2003) Lancet , vol.362 , pp. 30-37
    • Maiuri, L.1    Ciacci, C.2    Ricciardelli, I.3    Vacca, L.4    Raia, V.5
  • 18
    • 4444251461 scopus 로고    scopus 로고
    • A direct role for NKG2D/MICA interaction in villous atrophy during celiac disease
    • Hüe, S.; Mention, J. J.; Montiero, R. C.; Zhang, S. L.; Cellier, C. A direct role for NKG2D/MICA interaction in villous atrophy during celiac disease Immunity 2004, 21, 367-377
    • (2004) Immunity , vol.21 , pp. 367-377
    • Hüe, S.1    Mention, J.J.2    Montiero, R.C.3    Zhang, S.L.4    Cellier, C.5
  • 19
    • 34147212320 scopus 로고    scopus 로고
    • Growth factor like activity of gliadin, an alimentary protein: Implications for celiac disease
    • Barone, M. V.; Gimigliano, A.; Castoria, G.; Paolella, G.; Maurano, F. Growth factor like activity of gliadin, an alimentary protein: implications for celiac disease Gut 2007, 56, 480-488
    • (2007) Gut , vol.56 , pp. 480-488
    • Barone, M.V.1    Gimigliano, A.2    Castoria, G.3    Paolella, G.4    Maurano, F.5
  • 21
    • 1642275329 scopus 로고    scopus 로고
    • Susceptibility to transglutaminase of gliadin peptides predicted by a mass spectrometry-based assay
    • Mamone, G.; Ferranti, P.; Melck, D.; Tafuro, F.; Longobardo, L. Susceptibility to transglutaminase of gliadin peptides predicted by a mass spectrometry-based assay FEBS Lett. 2004, 562, 177-182
    • (2004) FEBS Lett. , vol.562 , pp. 177-182
    • Mamone, G.1    Ferranti, P.2    Melck, D.3    Tafuro, F.4    Longobardo, L.5
  • 23
    • 0031696005 scopus 로고    scopus 로고
    • Quantitative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography
    • Wieser, H.; Antes, S.; Seilmeier, W. Quantitative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography Cereal Chem. 1998, 75, 644-650
    • (1998) Cereal Chem. , vol.75 , pp. 644-650
    • Wieser, H.1    Antes, S.2    Seilmeier, W.3
  • 24
    • 0036838698 scopus 로고    scopus 로고
    • The HLA molecules DQA1*0501/B1*0201 and DQA1*0301/ B1*0302 share an extensive overlap peptide biunding specificity
    • Sidney, J.; Del Guercio, M. F.; Southwood, S.; Sette, A. The HLA molecules DQA1*0501/B1*0201 and DQA1*0301/B1*0302 share an extensive overlap peptide biunding specificity J. Immunol. 2002, 169, 5098-5108
    • (2002) J. Immunol. , vol.169 , pp. 5098-5108
    • Sidney, J.1    Del Guercio, M.F.2    Southwood, S.3    Sette, A.4
  • 25
    • 34548486891 scopus 로고    scopus 로고
    • Transamidation of wheat flour inhibits the response to gliadin of intestinal T cells in celiac disease
    • Gianfrani, C.; Siciliano, R. A.; Facchiano, A. M.; Camarca, A.; Mazzeo, M. F. Transamidation of wheat flour inhibits the response to gliadin of intestinal T cells in celiac disease Gastroenterology 2007, 133, 780-789
    • (2007) Gastroenterology , vol.133 , pp. 780-789
    • Gianfrani, C.1    Siciliano, R.A.2    Facchiano, A.M.3    Camarca, A.4    Mazzeo, M.F.5
  • 26
    • 23044444710 scopus 로고    scopus 로고
    • Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry
    • Mamone, G.; Addeo, F.; Chianese, L.; Di Luccia, A.; De Martino, A. Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry Proteomics 2005, 5, 2859-2865
    • (2005) Proteomics , vol.5 , pp. 2859-2865
    • Mamone, G.1    Addeo, F.2    Chianese, L.3    Di Luccia, A.4    De Martino, A.5
  • 27
    • 0006280170 scopus 로고
    • The preparation and characterization of an aggregated gliadin fraction from wheat
    • Shewry, P. R.; Miflin, B. J.; Lew, E. J. L.; Kasarda, D. D. The preparation and characterization of an aggregated gliadin fraction from wheat J. Exp. Bot. 1993, 34, 1403-1410
    • (1993) J. Exp. Bot. , vol.34 , pp. 1403-1410
    • Shewry, P.R.1    Miflin, B.J.2    Lew, E.J.L.3    Kasarda, D.D.4
  • 28
    • 84864017435 scopus 로고    scopus 로고
    • Nomenclature and listing of celiac disease relevant gluten T-cell epitopes restricted by HLA-DQ molecules
    • Sollid, L. M.; Qiao, S. W.; Anderson, R. P.; Gianfrani, C.; Koning, F. Nomenclature and listing of celiac disease relevant gluten T-cell epitopes restricted by HLA-DQ molecules Immunogenetics 2012, 6, 455-460
    • (2012) Immunogenetics , vol.6 , pp. 455-460
    • Sollid, L.M.1    Qiao, S.W.2    Anderson, R.P.3    Gianfrani, C.4    Koning, F.5
  • 29
    • 84861120545 scopus 로고    scopus 로고
    • Repertoire of gluten peptides active in celiac disease patients: Perspectives for translational therapeutic applications
    • Camarca, A.; Del Mastro, A.; Gianfrani, C. Repertoire of gluten peptides active in celiac disease patients: perspectives for translational therapeutic applications Endocr. Metab. Immune Disord. Drug Targets 2012, 12, 207-219
    • (2012) Endocr. Metab. Immune Disord. Drug Targets , vol.12 , pp. 207-219
    • Camarca, A.1    Del Mastro, A.2    Gianfrani, C.3
  • 30
    • 0034695893 scopus 로고    scopus 로고
    • The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase
    • Arentz-Hansen, H.; Körner, R.; Molberg, O.; Quarsten, H.; Vader, W. The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase J. Exp. Med. 2000, 191, 603-612
    • (2000) J. Exp. Med. , vol.191 , pp. 603-612
    • Arentz-Hansen, H.1    Körner, R.2    Molberg, O.3    Quarsten, H.4    Vader, W.5
  • 31
    • 0001426758 scopus 로고
    • The structural and evolutionary relationships of the prolamine storage proteins of barley, rye and wheat
    • Shewry, P. R.; Miflin, B. J.; Kasarda, D. D. The structural and evolutionary relationships of the prolamine storage proteins of barley, rye and wheat Philos. Trans. R. Soc. London B 1984, 304, 297-308
    • (1984) Philos. Trans. R. Soc. London B , vol.304 , pp. 297-308
    • Shewry, P.R.1    Miflin, B.J.2    Kasarda, D.D.3
  • 32
    • 84862579962 scopus 로고    scopus 로고
    • Celiac disease T-cell epitopes from γ-gliadins: Immunoreactivity depends on the genome of origin, transcript frequency, and flanking protein variation
    • Salentijn, E. M.; Mitea, D. C.; Goryunova, S. V.; Van der Meer, I. M.; Padioleau, I. Celiac disease T-cell epitopes from γ-gliadins: immunoreactivity depends on the genome of origin, transcript frequency, and flanking protein variation BMC Genomics 2012, 13, 277
    • (2012) BMC Genomics , vol.13 , pp. 277
    • Salentijn, E.M.1    Mitea, D.C.2    Goryunova, S.V.3    Van Der Meer, I.M.4    Padioleau, I.5
  • 33
    • 0037018095 scopus 로고    scopus 로고
    • Specificity of tissue transglutaminase explains cereal toxicity in celiac disease
    • Vader, L. W.; de Ru, A.; van der Wal, Y.; Kooy, Y. M.; Benckhuijsen, W. Specificity of tissue transglutaminase explains cereal toxicity in celiac disease J. Exp. Med. 2002, 195, 643-649
    • (2002) J. Exp. Med. , vol.195 , pp. 643-649
    • Vader, L.W.1    De Ru, A.2    Van Der Wal, Y.3    Kooy, Y.M.4    Benckhuijsen, W.5
  • 34
    • 57049132880 scopus 로고    scopus 로고
    • The role of HLA-DQ8 b57 polymorphism in the anti-gluten T-cell response in celiac disease
    • Hovhannisyan, Z.; Weiss, A.; Martin, A.; Wiesner, M.; Tollefsen, S. The role of HLA-DQ8 b57 polymorphism in the anti-gluten T-cell response in celiac disease Nature 2008, 456, 534-538
    • (2008) Nature , vol.456 , pp. 534-538
    • Hovhannisyan, Z.1    Weiss, A.2    Martin, A.3    Wiesner, M.4    Tollefsen, S.5
  • 35
    • 29144480200 scopus 로고    scopus 로고
    • Identification of immunodominant epitopes of α-gliadin in HLA-DQ8 transgenic mice following of oral immunization
    • Senger, S.; Maurano, F.; Mazzeo, M. F.; Gaita, M.; Fierro, O. Identification of immunodominant epitopes of α-gliadin in HLA-DQ8 transgenic mice following of oral immunization J. Immunol. 2005, 175, 8087-8095
    • (2005) J. Immunol. , vol.175 , pp. 8087-8095
    • Senger, S.1    Maurano, F.2    Mazzeo, M.F.3    Gaita, M.4    Fierro, O.5
  • 36
    • 14944352764 scopus 로고    scopus 로고
    • Mapping of gluten T-cell epitopes in the bread wheat ancestors: Implications for celiac disease
    • Molberg, Ø.; Uhlen, A. K.; Jensen, T.; Flaete, N. S. Mapping of gluten T-cell epitopes in the bread wheat ancestors: implications for celiac disease Gastroenterology 2005, 128, 393-401
    • (2005) Gastroenterology , vol.128 , pp. 393-401
    • Molberg Ø1    Uhlen, A.K.2    Jensen, T.3    Flaete, N.S.4
  • 37
    • 33750410284 scopus 로고    scopus 로고
    • Lack of intestinal mucosal toxicity of Triticum monococcum in celiac disease patients
    • Pizzuti, D.; Buda, A.; D'Odorico, A.; D'Incà, R.; Chiarelli, S. Lack of intestinal mucosal toxicity of Triticum monococcum in celiac disease patients Scand. J. Gastroenterol. 2006, 41, 1305-1311
    • (2006) Scand. J. Gastroenterol. , vol.41 , pp. 1305-1311
    • Pizzuti, D.1    Buda, A.2    D'Odorico, A.3    D'Incà, R.4    Chiarelli, S.5


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