Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains
Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary struc...
Ausführliche Beschreibung
Autor*in: |
Mameri, Hamza [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2015 |
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Übergeordnetes Werk: |
Enthalten in: Journal of agricultural and food chemistry - Columbus, Ohio : American Chemical Soc., 1953, 63(2015), 29, Seite 6546 |
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Übergeordnetes Werk: |
volume:63 ; year:2015 ; number:29 ; pages:6546 |
Links: |
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520 | |a Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had a wheat food allergy or baker's asthma. The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains of α- and γ-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other members of the prolamin superfamily, disulfide bonds appear to be of high importance for IgE binding. | ||
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700 | 1 | |a Gohon, Yann |4 oth | |
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700 | 1 | |a Beaudouin, Etienne |4 oth | |
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PQ20160617 (DE-627)OLC196301412X (DE-599)GBVOLC196301412X (PRQ)p837-10c7fda0daab17f020b072102202c168ed8cb21112f36d48ccd9e446faf150280 (KEY)0011841920150000063002906546structuralbasisofigebindingtoandgliadinscontributi DE-627 ger DE-627 rakwb eng 630 640 540 DNB 58.27 bkl 58.34 bkl 42.63 bkl Mameri, Hamza verfasserin aut Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had a wheat food allergy or baker's asthma. The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains of α- and γ-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other members of the prolamin superfamily, disulfide bonds appear to be of high importance for IgE binding. Brossard, Chantal oth Gaudin, Jean-Charles oth Gohon, Yann oth Paty, Evelyne oth Beaudouin, Etienne oth Moneret-Vautrin, Denise-Anne oth Drouet, Martine oth Solé, Véronique oth Wien, Frank oth Lupi, Roberta oth Larré, Colette oth Snégaroff, Jacques oth Denery-Papini, Sandra oth Enthalten in Journal of agricultural and food chemistry Columbus, Ohio : American Chemical Soc., 1953 63(2015), 29, Seite 6546 (DE-627)129602795 (DE-600)241619-0 (DE-576)015096610 0021-8561 nnns volume:63 year:2015 number:29 pages:6546 http://www.ncbi.nlm.nih.gov/pubmed/26186140 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_70 GBV_ILN_2006 GBV_ILN_4219 58.27 AVZ 58.34 AVZ 42.63 AVZ AR 63 2015 29 6546 |
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Mameri, Hamza @@aut@@ Brossard, Chantal @@oth@@ Gaudin, Jean-Charles @@oth@@ Gohon, Yann @@oth@@ Paty, Evelyne @@oth@@ Beaudouin, Etienne @@oth@@ Moneret-Vautrin, Denise-Anne @@oth@@ Drouet, Martine @@oth@@ Solé, Véronique @@oth@@ Wien, Frank @@oth@@ Lupi, Roberta @@oth@@ Larré, Colette @@oth@@ Snégaroff, Jacques @@oth@@ Denery-Papini, Sandra @@oth@@ |
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Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains |
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Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains |
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structural basis of ige binding to α- and γ-gliadins: contribution of disulfide bonds and repetitive and nonrepetitive domains |
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Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains |
abstract |
Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had a wheat food allergy or baker's asthma. The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains of α- and γ-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other members of the prolamin superfamily, disulfide bonds appear to be of high importance for IgE binding. |
abstractGer |
Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had a wheat food allergy or baker's asthma. The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains of α- and γ-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other members of the prolamin superfamily, disulfide bonds appear to be of high importance for IgE binding. |
abstract_unstemmed |
Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of α- and γ-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had a wheat food allergy or baker's asthma. The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains of α- and γ-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other members of the prolamin superfamily, disulfide bonds appear to be of high importance for IgE binding. |
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title_short |
Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains |
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