Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars
Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliad...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hailegiorgis, Daniel [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of crop science and biotechnology - Seoul : Korean Soc. of Crop Science, 2009, 25(2022), 3 vom: 10. Jan., Seite 325-336 |
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| Übergeordnetes Werk: |
volume:25 ; year:2022 ; number:3 ; day:10 ; month:01 ; pages:325-336 |
| Links: |
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| DOI / URN: |
10.1007/s12892-021-00134-0 |
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| Katalog-ID: |
SPR046973311 |
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| 024 | 7 | |a 10.1007/s12892-021-00134-0 |2 doi | |
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| 100 | 1 | |a Hailegiorgis, Daniel |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
| 264 | 1 | |c 2022 | |
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| 500 | |a © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 | ||
| 520 | |a Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. | ||
| 650 | 4 | |a Amino acid variation |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Celiac disease |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Polymorphism |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Polypeptide |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Secondary structure |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Seid, Ephrem |4 aut | |
| 700 | 1 | |a Lee, Chong Ae |4 aut | |
| 700 | 1 | |a Yun, Song Joong |0 (orcid)0000-0002-4907-7055 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of crop science and biotechnology |d Seoul : Korean Soc. of Crop Science, 2009 |g 25(2022), 3 vom: 10. Jan., Seite 325-336 |w (DE-627)617512175 |w (DE-600)2534833-4 |x 2005-8276 |7 nnns |
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| 912 | |a GBV_ILN_11 | ||
| 912 | |a GBV_ILN_20 | ||
| 912 | |a GBV_ILN_22 | ||
| 912 | |a GBV_ILN_23 | ||
| 912 | |a GBV_ILN_24 | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_32 | ||
| 912 | |a GBV_ILN_39 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_65 | ||
| 912 | |a GBV_ILN_69 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_73 | ||
| 912 | |a GBV_ILN_74 | ||
| 912 | |a GBV_ILN_90 | ||
| 912 | |a GBV_ILN_95 | ||
| 912 | |a GBV_ILN_100 | ||
| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_120 | ||
| 912 | |a GBV_ILN_138 | ||
| 912 | |a GBV_ILN_150 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_152 | ||
| 912 | |a GBV_ILN_161 | ||
| 912 | |a GBV_ILN_170 | ||
| 912 | |a GBV_ILN_171 | ||
| 912 | |a GBV_ILN_187 | ||
| 912 | |a GBV_ILN_213 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_230 | ||
| 912 | |a GBV_ILN_250 | ||
| 912 | |a GBV_ILN_281 | ||
| 912 | |a GBV_ILN_285 | ||
| 912 | |a GBV_ILN_293 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_636 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2031 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2039 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2188 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2232 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2446 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2548 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4046 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4328 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4336 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4393 | ||
| 912 | |a GBV_ILN_4700 | ||
| 951 | |a AR | ||
| 952 | |d 25 |j 2022 |e 3 |b 10 |c 01 |h 325-336 | ||
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10.1007/s12892-021-00134-0 doi (DE-627)SPR046973311 (SPR)s12892-021-00134-0-e DE-627 ger DE-627 rakwb eng Hailegiorgis, Daniel verfasserin aut Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 Seid, Ephrem aut Lee, Chong Ae aut Yun, Song Joong (orcid)0000-0002-4907-7055 aut Enthalten in Journal of crop science and biotechnology Seoul : Korean Soc. of Crop Science, 2009 25(2022), 3 vom: 10. Jan., Seite 325-336 (DE-627)617512175 (DE-600)2534833-4 2005-8276 nnns volume:25 year:2022 number:3 day:10 month:01 pages:325-336 https://dx.doi.org/10.1007/s12892-021-00134-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 25 2022 3 10 01 325-336 |
| spelling |
10.1007/s12892-021-00134-0 doi (DE-627)SPR046973311 (SPR)s12892-021-00134-0-e DE-627 ger DE-627 rakwb eng Hailegiorgis, Daniel verfasserin aut Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 Seid, Ephrem aut Lee, Chong Ae aut Yun, Song Joong (orcid)0000-0002-4907-7055 aut Enthalten in Journal of crop science and biotechnology Seoul : Korean Soc. of Crop Science, 2009 25(2022), 3 vom: 10. Jan., Seite 325-336 (DE-627)617512175 (DE-600)2534833-4 2005-8276 nnns volume:25 year:2022 number:3 day:10 month:01 pages:325-336 https://dx.doi.org/10.1007/s12892-021-00134-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 25 2022 3 10 01 325-336 |
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10.1007/s12892-021-00134-0 doi (DE-627)SPR046973311 (SPR)s12892-021-00134-0-e DE-627 ger DE-627 rakwb eng Hailegiorgis, Daniel verfasserin aut Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 Seid, Ephrem aut Lee, Chong Ae aut Yun, Song Joong (orcid)0000-0002-4907-7055 aut Enthalten in Journal of crop science and biotechnology Seoul : Korean Soc. of Crop Science, 2009 25(2022), 3 vom: 10. Jan., Seite 325-336 (DE-627)617512175 (DE-600)2534833-4 2005-8276 nnns volume:25 year:2022 number:3 day:10 month:01 pages:325-336 https://dx.doi.org/10.1007/s12892-021-00134-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 25 2022 3 10 01 325-336 |
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10.1007/s12892-021-00134-0 doi (DE-627)SPR046973311 (SPR)s12892-021-00134-0-e DE-627 ger DE-627 rakwb eng Hailegiorgis, Daniel verfasserin aut Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 Seid, Ephrem aut Lee, Chong Ae aut Yun, Song Joong (orcid)0000-0002-4907-7055 aut Enthalten in Journal of crop science and biotechnology Seoul : Korean Soc. of Crop Science, 2009 25(2022), 3 vom: 10. Jan., Seite 325-336 (DE-627)617512175 (DE-600)2534833-4 2005-8276 nnns volume:25 year:2022 number:3 day:10 month:01 pages:325-336 https://dx.doi.org/10.1007/s12892-021-00134-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 25 2022 3 10 01 325-336 |
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10.1007/s12892-021-00134-0 doi (DE-627)SPR046973311 (SPR)s12892-021-00134-0-e DE-627 ger DE-627 rakwb eng Hailegiorgis, Daniel verfasserin aut Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 Seid, Ephrem aut Lee, Chong Ae aut Yun, Song Joong (orcid)0000-0002-4907-7055 aut Enthalten in Journal of crop science and biotechnology Seoul : Korean Soc. of Crop Science, 2009 25(2022), 3 vom: 10. Jan., Seite 325-336 (DE-627)617512175 (DE-600)2534833-4 2005-8276 nnns volume:25 year:2022 number:3 day:10 month:01 pages:325-336 https://dx.doi.org/10.1007/s12892-021-00134-0 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 25 2022 3 10 01 325-336 |
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Enthalten in Journal of crop science and biotechnology 25(2022), 3 vom: 10. Jan., Seite 325-336 volume:25 year:2022 number:3 day:10 month:01 pages:325-336 |
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Hailegiorgis, Daniel @@aut@@ Seid, Ephrem @@aut@@ Lee, Chong Ae @@aut@@ Yun, Song Joong @@aut@@ |
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To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Amino acid variation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Celiac disease</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Polymorphism</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Polypeptide</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Secondary structure</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Seid, Ephrem</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lee, Chong Ae</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yun, Song Joong</subfield><subfield code="0">(orcid)0000-0002-4907-7055</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of crop science and biotechnology</subfield><subfield code="d">Seoul : Korean Soc. of Crop Science, 2009</subfield><subfield code="g">25(2022), 3 vom: 10. 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|
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Hailegiorgis, Daniel |
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Hailegiorgis, Daniel misc Amino acid variation misc Celiac disease misc Polymorphism misc Polypeptide misc Secondary structure Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
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2005-8276 |
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Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars Amino acid variation (dpeaa)DE-He213 Celiac disease (dpeaa)DE-He213 Polymorphism (dpeaa)DE-He213 Polypeptide (dpeaa)DE-He213 Secondary structure (dpeaa)DE-He213 |
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misc Amino acid variation misc Celiac disease misc Polymorphism misc Polypeptide misc Secondary structure |
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misc Amino acid variation misc Celiac disease misc Polymorphism misc Polypeptide misc Secondary structure |
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misc Amino acid variation misc Celiac disease misc Polymorphism misc Polypeptide misc Secondary structure |
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Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
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Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
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Hailegiorgis, Daniel |
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Journal of crop science and biotechnology |
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Hailegiorgis, Daniel Seid, Ephrem Lee, Chong Ae Yun, Song Joong |
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Hailegiorgis, Daniel |
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variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite ethiopian durum wheat cultivars |
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Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
| abstract |
Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 |
| abstractGer |
Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 |
| abstract_unstemmed |
Abstract Alpha-gliadins are the predominant immunogenic fractions of gluten proteins with strong T cell stimulatory epitopes that affect celiac disease (CD) patients. To obtain essential information on the CD epitopes of Ethiopian durum wheat, molecular characterizations were conducted using α-gliadin gene clones of three elite Ethiopian durum wheat cultivars. Deduced amino acid sequences of the three selected clones share all the known primary features of α-gliadins and core sequences of CD epitopes. Several insertions and deletions (InDels), and substitutions in the core and adjacent sequences of the epitopes are dissimilar among the deduced α-gliadins. Due mainly to these sequence variations, the core sequences of all the toxic epitopes are in one to four mismatches to their canonical sequences, showing distinct patterns among the deduced α-gliadins, except one canonical epitope from cv. Assasa. These sequence variations also result in a drastic difference in peptide cleavage patterns by proteases contained in human gastric and duodenal juices. In addition, characteristic differences in disulfide connectivity, and hydropathy and polarity of amino acid residues correlate well with noticeable variations in conformational ensembles of the peptides, especially at the region harboring multiple CD epitopes at the N-terminal region. α-Gliadin from cv. Assasa is unique in that it has mostly variant toxic epitopes and all the epitope motifs are cleaved by multiple enzymes at up to five positions. Ethiopian germplasms expressing α-gliadins with divergent sequences at the epitope motifs together with higher susceptibility to proteases in human digestive systems could be potential resources for the development of hypoallergenic cultivars. © The Author(s), under exclusive licence to Korean Society of Crop Science (KSCS) 2021 |
| collection_details |
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| container_issue |
3 |
| title_short |
Variations in immunodominant epitope and molecular conformation of alpha-gliadins in elite Ethiopian durum wheat cultivars |
| url |
https://dx.doi.org/10.1007/s12892-021-00134-0 |
| remote_bool |
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| author2 |
Seid, Ephrem Lee, Chong Ae Yun, Song Joong |
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| doi_str |
10.1007/s12892-021-00134-0 |
| up_date |
2024-07-04T01:16:59.699Z |
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| score |
7.399872 |