Natural variants of alpha-gliadin peptides within wheat proteins with reduced toxicity in coeliac disease
The only generally accepted treatment of coeliac disease (CD) is a lifelong gluten-free diet. Wheat gluten proteins include gliadins, low and high molecular weight glutenins. However, we have found significant structural variations within these protein families among different cultivars. To determin...
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| Veröffentlicht in: | British journal of nutrition 2020-06, Vol.123 (12), p.1382-1389, Article 0007114520000768 |
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| creator | Japelj, Nika Suligoj, Tanja Zhang, Wei Corte-Real, Beatriz Messing, Joachim Ciclitira, Paul J. |
| description | The only generally accepted treatment of coeliac disease (CD) is a lifelong gluten-free diet. Wheat gluten proteins include gliadins, low and high molecular weight glutenins. However, we have found significant structural variations within these protein families among different cultivars. To determine which structural motifs might be less toxic than others, we assessed five variants of alpha-gliadin immunodominant CD-toxic peptides synthesised as 16mers in CD T cell stimulation assays with gluten-sensitive T cell lines generated from duodenal biopsies from CD-affected individuals. The peptides harboured the overlapping T cell epitopes DQ 2.5-glia-alpha-2 and naturally occurring variants that differed in certain amino acids (AA). The results revealed that introduction of two selected AA substitutions in alpha-gliadin peptides reduced immunogenicity. A peptide with three AA substitutions involving two glutamic acids (E) and one glutamine residue (G) revealed the peptide was negative in 5:5 samples. We used CD small-intestinal organ culture to assess CD toxicity that revealed two peptides with selected substitution of both glutamic acid (E) and proline (P) residues abrogated evidence of CD toxicity. |
| doi_str_mv | 10.1017/S0007114520000768 |
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Wheat gluten proteins include gliadins, low and high molecular weight glutenins. However, we have found significant structural variations within these protein families among different cultivars. To determine which structural motifs might be less toxic than others, we assessed five variants of alpha-gliadin immunodominant CD-toxic peptides synthesised as 16mers in CD T cell stimulation assays with gluten-sensitive T cell lines generated from duodenal biopsies from CD-affected individuals. The peptides harboured the overlapping T cell epitopes DQ 2.5-glia-alpha-2 and naturally occurring variants that differed in certain amino acids (AA). The results revealed that introduction of two selected AA substitutions in alpha-gliadin peptides reduced immunogenicity. A peptide with three AA substitutions involving two glutamic acids (E) and one glutamine residue (G) revealed the peptide was negative in 5:5 samples. We used CD small-intestinal organ culture to assess CD toxicity that revealed two peptides with selected substitution of both glutamic acid (E) and proline (P) residues abrogated evidence of CD toxicity.</description><identifier>ISSN: 0007-1145</identifier><identifier>EISSN: 1475-2662</identifier><identifier>DOI: 10.1017/S0007114520000768</identifier><identifier>PMID: 32100654</identifier><language>eng</language><publisher>CAMBRIDGE: Cambridge Univ Press</publisher><subject>Amino Acids ; Antigens ; Autoimmune diseases ; Biopsy ; Cadmium ; Celiac disease ; Celiac Disease - immunology ; Cell culture ; Cell growth ; Cell lines ; Cereals ; Cultivars ; Duodenum - immunology ; Enzymes ; Epitopes ; Females ; Flour ; Gliadin ; Gliadin - immunology ; Glutamic acid ; Glutamic Acid - immunology ; Glutamine ; Glutamine - immunology ; Gluten ; Glutens - immunology ; Humans ; Immunogenetic Phenomena ; Immunogenicity ; Intestine ; Life Sciences & Biomedicine ; Lymphocytes ; Lymphocytes T ; Molecular weight ; Nutrition ; Nutrition & Dietetics ; Organ culture ; Pathogenesis ; Patients ; Peptides ; Peptides - immunology ; Proline ; Proline - immunology ; Protein families ; Proteins ; Residues ; Science & Technology ; T cell receptors ; T-Lymphocytes - immunology ; Toxic diseases ; Toxicity ; Triticum - chemistry ; Wheat</subject><ispartof>British journal of nutrition, 2020-06, Vol.123 (12), p.1382-1389, Article 0007114520000768</ispartof><rights>The Authors 2020</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>1</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000530062800007</woscitedreferencesoriginalsourcerecordid><cites>FETCH-LOGICAL-c324t-1528d1b6acf9035c0d4f48b85cab8bab2c05ce5e85fe284961bf717963fa405f3</cites><orcidid>0000-0002-9230-0646</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930,28253</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32100654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Japelj, Nika</creatorcontrib><creatorcontrib>Suligoj, Tanja</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Corte-Real, Beatriz</creatorcontrib><creatorcontrib>Messing, Joachim</creatorcontrib><creatorcontrib>Ciclitira, Paul J.</creatorcontrib><title>Natural variants of alpha-gliadin peptides within wheat proteins with reduced toxicity in coeliac disease</title><title>British journal of nutrition</title><addtitle>BRIT J NUTR</addtitle><addtitle>Br J Nutr</addtitle><description>The only generally accepted treatment of coeliac disease (CD) is a lifelong gluten-free diet. Wheat gluten proteins include gliadins, low and high molecular weight glutenins. However, we have found significant structural variations within these protein families among different cultivars. To determine which structural motifs might be less toxic than others, we assessed five variants of alpha-gliadin immunodominant CD-toxic peptides synthesised as 16mers in CD T cell stimulation assays with gluten-sensitive T cell lines generated from duodenal biopsies from CD-affected individuals. The peptides harboured the overlapping T cell epitopes DQ 2.5-glia-alpha-2 and naturally occurring variants that differed in certain amino acids (AA). The results revealed that introduction of two selected AA substitutions in alpha-gliadin peptides reduced immunogenicity. A peptide with three AA substitutions involving two glutamic acids (E) and one glutamine residue (G) revealed the peptide was negative in 5:5 samples. We used CD small-intestinal organ culture to assess CD toxicity that revealed two peptides with selected substitution of both glutamic acid (E) and proline (P) residues abrogated evidence of CD toxicity.</description><subject>Amino Acids</subject><subject>Antigens</subject><subject>Autoimmune diseases</subject><subject>Biopsy</subject><subject>Cadmium</subject><subject>Celiac disease</subject><subject>Celiac Disease - immunology</subject><subject>Cell culture</subject><subject>Cell growth</subject><subject>Cell lines</subject><subject>Cereals</subject><subject>Cultivars</subject><subject>Duodenum - immunology</subject><subject>Enzymes</subject><subject>Epitopes</subject><subject>Females</subject><subject>Flour</subject><subject>Gliadin</subject><subject>Gliadin - immunology</subject><subject>Glutamic acid</subject><subject>Glutamic Acid - immunology</subject><subject>Glutamine</subject><subject>Glutamine - immunology</subject><subject>Gluten</subject><subject>Glutens - immunology</subject><subject>Humans</subject><subject>Immunogenetic Phenomena</subject><subject>Immunogenicity</subject><subject>Intestine</subject><subject>Life Sciences & Biomedicine</subject><subject>Lymphocytes</subject><subject>Lymphocytes T</subject><subject>Molecular weight</subject><subject>Nutrition</subject><subject>Nutrition & Dietetics</subject><subject>Organ culture</subject><subject>Pathogenesis</subject><subject>Patients</subject><subject>Peptides</subject><subject>Peptides - 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Wheat gluten proteins include gliadins, low and high molecular weight glutenins. However, we have found significant structural variations within these protein families among different cultivars. To determine which structural motifs might be less toxic than others, we assessed five variants of alpha-gliadin immunodominant CD-toxic peptides synthesised as 16mers in CD T cell stimulation assays with gluten-sensitive T cell lines generated from duodenal biopsies from CD-affected individuals. The peptides harboured the overlapping T cell epitopes DQ 2.5-glia-alpha-2 and naturally occurring variants that differed in certain amino acids (AA). The results revealed that introduction of two selected AA substitutions in alpha-gliadin peptides reduced immunogenicity. A peptide with three AA substitutions involving two glutamic acids (E) and one glutamine residue (G) revealed the peptide was negative in 5:5 samples. We used CD small-intestinal organ culture to assess CD toxicity that revealed two peptides with selected substitution of both glutamic acid (E) and proline (P) residues abrogated evidence of CD toxicity.</abstract><cop>CAMBRIDGE</cop><pub>Cambridge Univ Press</pub><pmid>32100654</pmid><doi>10.1017/S0007114520000768</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-9230-0646</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acids Antigens Autoimmune diseases Biopsy Cadmium Celiac disease Celiac Disease - immunology Cell culture Cell growth Cell lines Cereals Cultivars Duodenum - immunology Enzymes Epitopes Females Flour Gliadin Gliadin - immunology Glutamic acid Glutamic Acid - immunology Glutamine Glutamine - immunology Gluten Glutens - immunology Humans Immunogenetic Phenomena Immunogenicity Intestine Life Sciences & Biomedicine Lymphocytes Lymphocytes T Molecular weight Nutrition Nutrition & Dietetics Organ culture Pathogenesis Patients Peptides Peptides - immunology Proline Proline - immunology Protein families Proteins Residues Science & Technology T cell receptors T-Lymphocytes - immunology Toxic diseases Toxicity Triticum - chemistry Wheat |
| title | Natural variants of alpha-gliadin peptides within wheat proteins with reduced toxicity in coeliac disease |
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