The wheat low-molecular-weight glutenin genes: characterization of six new genes and progress in understanding gene family structure

Cassidy, B. G.; Dvořák, Jan; Anderson, Olin D.

doi:10.1007/s001220050797

Cited by 143 publications

(100 citation statements)

References 24 publications

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“…The ␣-gliadin has QQLPQEQ, QQQPQEQ, and QPYPQQQ sequences (35); therefore, this may cross-react with -5 gliadin as well as ␥-gliadin and slow -gliadin. Moreover, the IgE-binding epitope of -5 gliadin QQLPQQQ was seen in the VolckA3 and LMW21 and QQFPQQQ was seen in the VolckB3, respectively, all of which belong to the LMW glutenins (36), suggesting that -5 gliadin also cross-reacted with LMW glutenin. These results might account partly for the diversity of the reactivity in the dot-blot analysis with the sera of the patients.…”

Section: Discussionmentioning

confidence: 95%

Identification of the IgE-binding Epitope in ω-5 Gliadin, a Major Allergen in Wheat-dependent Exercise-induced Anaphylaxis

Matsuo

Morita

Tatham

et al. 2004

Journal of Biological Chemistry

166

186

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Wheat-dependent exercise-induced anaphylaxis (WDEIA) is a severe IgE-mediated allergic reaction provoked by the combination of wheat-ingestion with intensive physical exercise over the next few hours. Among wheat proteins, -5 gliadin, which is one of the components of fast -gliadin, has been reported as a major allergen in the anaphylaxis. In this study, we detected IgE-binding epitopes within the primary sequence of -5 gliadin using arrays of overlapping peptides synthesized on derivatized cellulose membranes. Sera from four patients with WDEIA having specific IgE to the fast -gliadin were used to probe the membrane. Seven epitopes, QQIPQQQ, QQLPQQQ, QQFPQQQ, QQSPEQQ, QQSPQQQ, QQYPQQQ, and PYPP, were detected within the primary sequence of -5 gliadin. By using sera of 15 patients, 4 of them, QQIPQQQ, QQFPQQQ, QQSPEQQ, and QQSPQQQ, were found to be dominant epitopes. Mutational analysis of the QQIPQQQ and QQFPQQQ indicated that amino acids at positions Gln 1 , Pro 4 , Gln 5 , Gln 6 , and Gln 7 were critical for IgE binding. These results will provide a useful tool for developing safer wheat products in addition to diagnostic and immunotherapy techniques for WDEIA.Food-dependent exercise-induced anaphylaxis is a distinct form of food allergy induced by physical exercise (1). Food items such as shrimp (2), hazelnut (3), buckwheat (4), corn (5), and celery (6) are responsible for the development of food-dependent exercise-induced anaphylaxis. However, of all of the various kinds of food, wheat is reported to be the allergen with the highest frequency in Japan (7). Symptoms are typically generalized urticaria and severe allergic reactions such as shock or hypotension. Because of this serious reaction, it is important to determine the causative food to avoid the allergic reaction. A challenge test consisting of ingestion of the assumed food followed by intense physical exercise is the only reliable method to determine the causative food and to diagnose the disease. However, the challenge test is not always safe because in some cases the test induces an anaphylactic shock. In addition, the most reliable treatment for this disease is to avoid taking the causative food or, alternatively, to take a rest after meals. However, in the case of wheat allergy, elimination causes a decline in the quality of life for the patients. Thus, an in vitro diagnostic method as well as hypoallergenic wheat is necessary for patients with wheat-dependent exercise-induced anaphylaxis (WDEIA). 1Recent studies have revealed the IgE-binding epitopes of several food allergens including egg (8), milk (9, 10), soybean (11), and peanut (12), whereas the IgE-binding epitopes for wheat allergen are controversial. Wheat protein is composed of water/salt-soluble proteins and water/salt-insoluble proteins. Proteins in the water/salt-soluble fraction, such as ␣-amylase inhibitor, peroxidase, glycerinaldehyde-3-phosphate dehydrogenase, serpin, and triosephosphate isomerase, have been considered to be major allergens in patients with bakers' asthma (13-15...

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Section: Discussionmentioning

confidence: 95%

Identification of the IgE-binding Epitope in ω-5 Gliadin, a Major Allergen in Wheat-dependent Exercise-induced Anaphylaxis

Matsuo

Morita

Tatham

et al. 2004

Journal of Biological Chemistry

166

186

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“…Figure 2 summarizes the alignment of amino acid sequences of BZ26-1 to BZ26-7 and BZ09-1 with those of B-hordeins from H. vulgare, H. chilense and LMW-GS from T. aestivum. Three major structural regions were identified, including a signal peptide, a repetitive domain (Domain II) and a C-terminal region (Cassidy et al 1998). Comparison of amino acid sequences from the BZ09-1 and BZ26 clones revealed length variations within domain II.…”

Section: Analysis Of B-hordein Dna and Polypeptide Sequencesmentioning

confidence: 99%

Structural and expressional analysis of the B-hordein genes in Tibetan hull-less barley

Han

Deng

et al. 2009

Genetica

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The B-hordein gene family was analyzed from two Tibetan hull-less barley cultivars Z09 and Z26 (Hordeum vulgare subsp. vulgare). Fourteen B-hordein genes, designated BZ09-2 to BZ09-5 (from Z09) and BZ26-1 to BZ26-10 (from Z26), were sequenced. Seven of them, similar to a previously reported BZ09-1 from Z09, were predicted to encode putative active proteins each with a signal peptide, a repetitive domain, and a C-terminal region; seven of them were predicted to be pseudogenes. The B-hordein gene family was analyzed using all known representatives of B-hordein sequences and two most similar LMW-GSs of Triticum aestivum. Alignment of these seven putative proteins with known B-hordeins and two most similar LMW-GSs of T. aestivum revealed that they shared a common motif. A large variation was observed between numbers of repeat units of predicted B-hordeins of Z26 and Z09. Phylogenetic analysis revealed that all BZ26 clones were clustered in a subgroup, and BZ09-1 formed another subgroup by itself in the putative eight active genes. In addition, six 5 0 -upstream regulatory sequences of the B-hordein genes were isolated from the two accessions by a single oligonucleotide nested PCR, and several different mutations were identified in the cis-acting element GLM and two distinctive sequences (Z09P-2 and Z26P-3). Phylogenetic analysis of 5 0 -upstream regulatory regions of the B-hordein genes showed that members from the same accession were clustered together except for two distinct members. Quantitative real time PCR analysis indicated distinct expression levels of B-hordein genes in four developing stages of developing grains in two accessions. These findings suggest B-hordein genes have intrinsic differences between accessions, and this knowledge will be useful for incorporating the B-hordeins protein in barley breeding programs.

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“…Some other genomes, e.g., U and M from related species, also contain similar coding loci as shown in this work. The copy numbers of LMW-GS genes in common wheat were estimated to have 10-15 (Harberd et al 1985) or 35-40 (Sabelli and Shewry 1991;Cassidy et al 1998). Until now, the precise gene organizations at Glu-3 loci of different genomes are still not clear.…”

Section: Pcr Amplification and Cloning Of Lmw-gs Genesmentioning

confidence: 99%

A Novel Chimeric Low-Molecular-Weight Glutenin Subunit Gene From the Wild Relatives of Wheat Aegilops kotschyi and Ae. juvenalis: Evolution at the Glu-3 Loci

Gao

et al. 2008

Genetics

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Four LMW-m and one novel chimeric (between LMW-i and LMW-m types) low-molecular-weight glutenin subunit (LMW-GS) genes from Aegilops neglecta (UUMM), Ae. kotschyi (UUSS), and Ae. juvenalis (DDMMUU) were isolated and characterized. Sequence structures showed that the 4 LMW-m-type genes, assigned to the M genome of Ae. neglecta, displayed a high homology with those from hexaploid common wheat. The novel chimeric gene, designed as AjkLMW-i, was isolated from both Ae. kotschyi and Ae. juvenalis and shown to be located on the U genome. Phylogentic analysis demonstrated that it had higher identity to the LMW-m-type than the LMW-i-type genes. A total of 20 single nucleotide polymorphisms (SNPs) were detected among the 4 LMW-m genes, with 13 of these being nonsynonymous SNPs that resulted in amino acid substitutions in the deduced mature proteins. Phylogenetic analysis demonstrated that it had higher identity to the LMW-m-type than the LMW-i-type genes. The divergence time estimation showed that the M and D genomes were closely related and diverged at 5.42 million years ago (MYA) while the differentiation between the U and A genomes was 6.82 MYA. We propose that, in addition to homologous recombination, an illegitimate recombination event on the U genome may have occurred 6.38 MYA and resulted in the generation of the chimeric gene AjkLMW-i, which may be an important genetic mechanism for the origin and evolution of LMW-GS Glu-3 alleles as well as other prolamin genes.

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The wheat low-molecular-weight glutenin genes: characterization of six new genes and progress in understanding gene family structure

Cited by 143 publications

References 24 publications

Identification of the IgE-binding Epitope in ω-5 Gliadin, a Major Allergen in Wheat-dependent Exercise-induced Anaphylaxis

Identification of the IgE-binding Epitope in ω-5 Gliadin, a Major Allergen in Wheat-dependent Exercise-induced Anaphylaxis

Structural and expressional analysis of the B-hordein genes in Tibetan hull-less barley

A Novel Chimeric Low-Molecular-Weight Glutenin Subunit Gene From the Wild Relatives of Wheat Aegilops kotschyi and Ae. juvenalis: Evolution at the Glu-3 Loci

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