IgE-binding Abilities of Pentapeptides, QQPFP and PQQPF, in Wheat Gliadin

Tanabe, Soichi

doi:10.3177/jnsv.50.367

Cited by 30 publications

(28 citation statements)

References 17 publications

(23 reference statements)

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“…In contrast, B-cell epitopes are either linear or conformational and are located on the surface of the molecule accessible to antibodies. The extension of the epitope may range from 5 to 8 (or even more) amino acids for IgE to be able of binding to the epitope [60][61][62][63]. However, we have found linear B-cell epitopes in lupin β-conglutins and the other legume allergens with a wide range of amino acid lengths, and overlapping with conformational epitopes.…”

Section: Discussionmentioning

confidence: 71%

Narrow Leafed Lupin Beta-Conglutin Proteins Epitopes Identification and Molecular Features Analysis Involved in Cross-Allergenicity to Peanut and Other Legumes

Lima-Cabello¹,

Robles-Bolivar²,

Alché³

et al. 2016

Genomics Comput Biol

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The use of narrow leafed lupin -NLL (Lupinus angustifolius L.) as a new food is resulting in an increasing number of allergic reactions cases, particularly in atopic patients with other pre-existing legume allergies.In the current study, we have performed an extensive in silico analysis of the NLL seed β-conglutin proteins, a new family of major allergen proteins identified in NLL, and a comparison to other relevant food allergens such as peanut Ara h 1. We analysed the variability of surface residues involved in conformational IgE-binding epitopes, lineal B-and T-cell epitopes, and changes in 2-D structural elements and 3D motives, with the aim to investigate cross-allergenicity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes differential variability. Thus, variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-allergenicity among legumes.

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Section: Discussionmentioning

confidence: 71%

Narrow Leafed Lupin Beta-Conglutin Proteins Epitopes Identification and Molecular Features Analysis Involved in Cross-Allergenicity to Peanut and Other Legumes

Lima-Cabello¹,

Robles-Bolivar²,

Alché³

et al. 2016

Genomics Comput Biol

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“…PQQPF and QQPFP were reported as the minimum IgE-binding gliadin epitopes for atopic dermatitis (Tanabe, 2004), with 5 repeats each in wheat γ-gliadin (283 amino acids, Scheets and Hedgcoth, 1988). The hydrolyzing activity of PGW on PQQPF was high at both pH 4.5 and 7.5.…”

Section: Resultsmentioning

confidence: 99%

“…Bottari et al (1996) has reported gliadin degradation by purified wheat cysteine protease, while Sutoh et al (1999) previously hydrolyzed gliadin and glutenin by crude fractions of wheat cysteine and serine proteases. Moreover, Tanabe et al (1996) indentified an IgE-binding epitope of glutenin for atopic dermatitis (QQQPP), and then epitopes of gliadin (PQQPF and QQPFP) (Tanabe, 2004). Gliadin peptides, such as LGQQQPFPPQQPYPQPQPF, for patients with coeliac disease can be degraded by crude proteases from germinating wheat and rye seeds (Hartmann et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Degradation of Epitope Peptides of Wheat Gliadin and Glutenin for Atopic Dermatitis by Crude Proteases from Germinated Wheat Seeds

Oita

Hayashi

Ohnishi‐Kameyama

2009

FSTR

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Wheat gliadin and glutenin epitopes for atopic dermatitis were degraded by crude proteases from germinated wheat seeds (PGW). PGW contained cysteine and serine protease activities and hydrolyzed gliadin epitope peptide, PQQPF, at both pH 4.5 and 7.5. The other gliadin epitope peptide, QQPFP, and the overlapped peptide of the two epitopes, PQQPFP, were fully hydrolyzed by PGW at pH 7.5, but were weakly hydrolyzed at pH 4.5. PGW also hydrolyzed the glutenin epitope peptide, QQQPP, at pH 7.5 but only partially at pH 4.5. A 16-mer peptide, CSQQQQPPFSQQQPPF (Glu-16), which incorporated this glutenin epitope twice, was also hydrolyzed by PGW at pH 4.5. Glu-16 was degraded by PGW into QQPP, QQQPP, QQPPF and QQQPPF, as confirmed by mass spectrometry.

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“…PQQPF and QQPFP were reported as minimum IgE-binding gliadin epitopes for atopic dermatitis 16 , with 5 repeats each in wheat γ-gliadin (283 amino acids) 13 . PQQPF was completely degraded by 1/50 the amount of the proteases of S. griseus and A. oryzae.…”

Section: Degradation Of Gliadin Epitopes For Atopic Dermatitismentioning

confidence: 99%

“…Among many wheat allergen proteins, gliadins and glutenins have been well studied [10][11][12] . Tanabe et al identified a glutenin epitope (QQQPP) 15 and gliadin epitopes (PQQPF and QQPFP) 16 for atopic dermatitis. Matsuo et al demonstrated that IgE-binding epitopes for EIA were QQIPQQQ and QQF-PQQQ etc.…”

Section: Introductionmentioning

confidence: 99%

Degradation of Wheat Epitope Peptides for Atopic Dermatitis and Exercise-Induced Anaphylaxis by Microbial Proteases

Oita

2012

JARQ

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Epitope peptides of wheat gliadins and glutenins for atopic dermatitis, PQQPF and QQQPP, were degraded by the microbial proteases of Streptomyces griseus and Aspergillus oryzae. The proteases of Bacillus licheniformis and Bacillus amyloloiquefasiens degraded wheat gliadins and glutenins, but had little or no effect on the epitopes. A 16-mer peptide of CSQQQQPPFSQQQPPF, which incorporated this glutenin epitope twice, was also hydrolyzed by these proteases, and no peptide containing QQQPP was shown after the reaction with S. griseus protease. The proteases of S. griseus and A. oryzae also degraded epitope peptides of wheat gliadins and glutenins for exercise-induced anaphylaxis, QQIPQQQ, QQFPQQQ and QQPGQ.

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IgE-binding Abilities of Pentapeptides, QQPFP and PQQPF, in Wheat Gliadin

Cited by 30 publications

References 17 publications

Narrow Leafed Lupin Beta-Conglutin Proteins Epitopes Identification and Molecular Features Analysis Involved in Cross-Allergenicity to Peanut and Other Legumes

Narrow Leafed Lupin Beta-Conglutin Proteins Epitopes Identification and Molecular Features Analysis Involved in Cross-Allergenicity to Peanut and Other Legumes

Degradation of Epitope Peptides of Wheat Gliadin and Glutenin for Atopic Dermatitis by Crude Proteases from Germinated Wheat Seeds

Degradation of Wheat Epitope Peptides for Atopic Dermatitis and Exercise-Induced Anaphylaxis by Microbial Proteases

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