73 research outputs found

    Characterization and Phylogenetic Analysis of Allergenic Tryp_alpha_amyl Protein Family in Plants

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    Most known allergenic proteins in rice (Oryza sativa) seed belong to the Tryp_alpha_amyl family (PF00234), but the sequence characterization and the evolution of the allergenic Tryp_alpha_amyl family members in plants have not been fully investigated. In this study, two specific motifs were found besides the common alpha-amylase inhibitors (AAI) domain from the allergenic Tryp_alpha_amyl family members in rice seeds (trRSAs). To understand the evolution and functional importance of the Tryp_alpha_amy1 family and the specific motifs for the allergenic one, a BLAST search identified 75 homologous proteins of trRSAs (trHAs) from 22 plant species including main crops such as rice, maize (Zea mays), wheat (Triticum aestivum), and sorghum (Sorghum bicolor) from all available sequences in the public databases. Statistical analysis showed that the allergenicity of trHAs is closely associated with these two motifs with high number of cysteine residues (p value = 0.00026), and the trHAs with and without the two motifs were clustered into separate clades, respectively. Furthermore, significant difference was observed on the secondary and tertiary structures of allergenic and nonallergenic trHAs. In addition, expression analysis showed that trHA-encoding genes of purple false brome (Brachypodium distachyon), barrel medic (Medicago truncatula), rice, and sorghum are dominantly expressed in seeds. This work provides insight into the understanding of the properties of allergens in the Tryp_alpha_amyl family and is helpful for allergy therapy

    Additional file 8: of Ostkpr1 functions in anther cuticle development and pollen wall formation in rice

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    Figure S4. Weight/Surface area ratio of WT and ostkpr1–2 anthers. The weight/surface area ratio of the anthers in the WT (blue squares) and ostkpr1–2 (red squares). (JPG 49 kb

    Characterization and Phylogenetic Analysis of Allergenic Tryp_alpha_amyl Protein Family in Plants

    No full text
    Most known allergenic proteins in rice (Oryza sativa) seed belong to the Tryp_alpha_amyl family (PF00234), but the sequence characterization and the evolution of the allergenic Tryp_alpha_amyl family members in plants have not been fully investigated. In this study, two specific motifs were found besides the common alpha-amylase inhibitors (AAI) domain from the allergenic Tryp_alpha_amyl family members in rice seeds (trRSAs). To understand the evolution and functional importance of the Tryp_alpha_amy1 family and the specific motifs for the allergenic one, a BLAST search identified 75 homologous proteins of trRSAs (trHAs) from 22 plant species including main crops such as rice, maize (Zea mays), wheat (Triticum aestivum), and sorghum (Sorghum bicolor) from all available sequences in the public databases. Statistical analysis showed that the allergenicity of trHAs is closely associated with these two motifs with high number of cysteine residues (<i>p</i> value = 0.00026), and the trHAs with and without the two motifs were clustered into separate clades, respectively. Furthermore, significant difference was observed on the secondary and tertiary structures of allergenic and nonallergenic trHAs. In addition, expression analysis showed that trHA-encoding genes of purple false brome (Brachypodium distachyon), barrel medic (Medicago truncatula), rice, and sorghum are dominantly expressed in seeds. This work provides insight into the understanding of the properties of allergens in the Tryp_alpha_amyl family and is helpful for allergy therapy

    Characterization and Phylogenetic Analysis of Allergenic Tryp_alpha_amyl Protein Family in Plants

    No full text
    Most known allergenic proteins in rice (Oryza sativa) seed belong to the Tryp_alpha_amyl family (PF00234), but the sequence characterization and the evolution of the allergenic Tryp_alpha_amyl family members in plants have not been fully investigated. In this study, two specific motifs were found besides the common alpha-amylase inhibitors (AAI) domain from the allergenic Tryp_alpha_amyl family members in rice seeds (trRSAs). To understand the evolution and functional importance of the Tryp_alpha_amy1 family and the specific motifs for the allergenic one, a BLAST search identified 75 homologous proteins of trRSAs (trHAs) from 22 plant species including main crops such as rice, maize (Zea mays), wheat (Triticum aestivum), and sorghum (Sorghum bicolor) from all available sequences in the public databases. Statistical analysis showed that the allergenicity of trHAs is closely associated with these two motifs with high number of cysteine residues (<i>p</i> value = 0.00026), and the trHAs with and without the two motifs were clustered into separate clades, respectively. Furthermore, significant difference was observed on the secondary and tertiary structures of allergenic and nonallergenic trHAs. In addition, expression analysis showed that trHA-encoding genes of purple false brome (Brachypodium distachyon), barrel medic (Medicago truncatula), rice, and sorghum are dominantly expressed in seeds. This work provides insight into the understanding of the properties of allergens in the Tryp_alpha_amyl family and is helpful for allergy therapy

    Video_1_Heat stress responses vary during floret development in European spring barley cultivars.mp4

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    The Poaceae, or grasses, include many agriculturally important cereal crops such as rice (Oryza sativa), maize (Zea mays), barley (Hordeum vulgare) and bread wheat (Triticum aestivum). Barley is a widely grown cereal crop used for stock feed, malting and brewing. Abiotic stresses, particularly global warming, are the major causes of crop yield losses by affecting fertility and seed set. However, effects of heat stress on reproductive structures and fertility in barley have not been extensively investigated. In this study we examined three commercial European spring barley varieties under high temperature conditions to investigate the effects on floret development. Using a combination of fertility assays, X-ray micro computed tomography, 3-dimensional modelling, cytology and immunolabelling, we observed that male reproductive organs are severely impacted by increased temperature, while the female reproductive organs are less susceptible. Importantly, the timing of stress relative to reproductive development had a significant impact on fertility in a cultivar-dependent manner, this was most significant at pollen mitosis stage with fertility ranged from 31.6-56.0% depending on cultivar. This work provides insight into how heat stress, when applied during male pollen mother cell meiosis and pollen mitosis, affects barley fertility and seed set, and also describes complementary invasive and non-invasive techniques to investigate floret development. This information will be used to identify and study barley cultivars that are less susceptible to heat stress at specific stages of floral development.</p

    Detected SNPs within the amplified target DNAs of <i>Acc1</i>, <i>ALMT1</i>, and <i>PKABA1</i> gene.

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    <p>A SNP of C>T was found at the eighth nucleotide position of <i>Acc1</i> gene forward primer in durum wheat cultivar Cannizzo; A SNP of A>C was found at the second nucleotide position of <i>ALMT1</i> gene forward primer in common wheat cultivar Zhongguochun, and one SNP of G>A was at the fourth nucleotide position of <i>ALMT1</i> gene probe in common wheat cultivar Zhengmai 9023; A SNP of G>A was found at the eleventh nucleotide position of <i>PKABA1</i> gene probe in common wheat cultivars Zhoumai 16 and Zimai 12. No SNP was found in <i>Waxy-D1</i> target region.</p

    Characterization and Phylogenetic Analysis of Allergenic Tryp_alpha_amyl Protein Family in Plants

    No full text
    Most known allergenic proteins in rice (Oryza sativa) seed belong to the Tryp_alpha_amyl family (PF00234), but the sequence characterization and the evolution of the allergenic Tryp_alpha_amyl family members in plants have not been fully investigated. In this study, two specific motifs were found besides the common alpha-amylase inhibitors (AAI) domain from the allergenic Tryp_alpha_amyl family members in rice seeds (trRSAs). To understand the evolution and functional importance of the Tryp_alpha_amy1 family and the specific motifs for the allergenic one, a BLAST search identified 75 homologous proteins of trRSAs (trHAs) from 22 plant species including main crops such as rice, maize (Zea mays), wheat (Triticum aestivum), and sorghum (Sorghum bicolor) from all available sequences in the public databases. Statistical analysis showed that the allergenicity of trHAs is closely associated with these two motifs with high number of cysteine residues (<i>p</i> value = 0.00026), and the trHAs with and without the two motifs were clustered into separate clades, respectively. Furthermore, significant difference was observed on the secondary and tertiary structures of allergenic and nonallergenic trHAs. In addition, expression analysis showed that trHA-encoding genes of purple false brome (Brachypodium distachyon), barrel medic (Medicago truncatula), rice, and sorghum are dominantly expressed in seeds. This work provides insight into the understanding of the properties of allergens in the Tryp_alpha_amyl family and is helpful for allergy therapy
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