Barley γ3-hordein: Glycosylation at an atypical site, disulfide bridge analysis, and reactivity with IgE from patients allergic to wheat

Snégaroff, Jacques; Bouchez, Isabelle; Smaali, Mohamed El Amine; Pecquet, C.; Raison‐Peyron, Nadia; Jolivet, Pascale; Laurière, Michel

doi:10.1016/j.bbapap.2012.07.016

Cited by 8 publications

(9 citation statements)

References 44 publications

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“…Asparagine (N)-linked glycosylation is the major co- and post-translational modification of proteins in plants [ 150 ]. The application of a great diversity of molecular techniques permitted the identification of glycosylated isoforms in many types of storage proteins and species: globulins (7S- and 11S-globulins and convicilin) in adzuki bean ( Vigna angularis L.), blue lupins ( Lupinus angustifolius L.), cocoa beans ( Theobroma cacao L.), common beans, hazelnuts ( Corylus avellane L.), lentils, Lotus ( Lotus japonicus L.), mung beans ( Vigna radiata L.), peas ( Pisum sativum L.), peanuts ( Arachis hipogea L.), soybeans and white lupin ( Lupinus albus L.) [ 42 , 120 , 121 , 151 , 152 , 153 , 154 , 155 , 156 , 157 , 158 , 159 , 160 , 161 , 162 , 163 , 164 , 165 , 166 , 167 , 168 , 169 , 170 , 171 , 172 , 173 , 174 , 175 , 176 , 177 , 178 , 179 ]; prolamins (γ3-hordein) in barley [ 180 ]; albumins (3S albumins) in Inca peanuts ( Plukenetia volubilis L.) [ 181 ]; glutelins in rice [ 135 , 182 ]; VSPs (patatin) in potatoes [ 30 , 43 , 183 , 184...…”

Section: Advances In the Biology Of Storage Proteinsmentioning

confidence: 99%

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

et al. 2018

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Seed storage proteins play a fundamental role in plant reproduction and human nutrition. They accumulate during seed development as reserve material for germination and seedling growth and are a major source of dietary protein for human consumption. Storage proteins encompass multiple isoforms encoded by multi-gene families that undergo abundant glycosylations and phosphorylations. Two-dimensional electrophoresis (2-DE) is a proteomic tool especially suitable for the characterization of storage proteins because of their peculiar characteristics. In particular, storage proteins are soluble multimeric proteins highly represented in the seed proteome that contain polypeptides of molecular mass between 10 and 130 kDa. In addition, high-resolution profiles can be achieved by applying targeted 2-DE protocols. 2-DE coupled with mass spectrometry (MS) has traditionally been the methodology of choice in numerous studies on the biology of storage proteins in a wide diversity of plants. 2-DE-based reference maps have decisively contributed to the current state of our knowledge about storage proteins in multiple key aspects, including identification of isoforms and quantification of their relative abundance, identification of phosphorylated isoforms and assessment of their phosphorylation status, and dynamic changes of isoforms during seed development and germination both qualitatively and quantitatively. These advances have translated into relevant information about meaningful traits in seed breeding such as protein quality, longevity, gluten and allergen content, stress response and antifungal, antibacterial, and insect susceptibility. This review addresses progress on the biology of storage proteins and application areas in seed breeding using 2-DE-based maps.

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Section: Advances In the Biology Of Storage Proteinsmentioning

confidence: 99%

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

et al. 2018

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“…Therefore, these proteins are thought to be glycosylated. 25 However, to our knowledge, there has been no previous study investigating the range of glycosylation of gliadins. We tried to determine the range of gliadins that were glycosylated and observed that the detected glycan overlapped with almost the entire range of gliadins.…”

Section: Discussionmentioning

confidence: 98%

IgE reactivity to carbohydrate moieties of glycoproteins in wheat allergy

Song

Hong²,

Lee³

et al. 2015

allergy asthma proc

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Carbohydrate moieties of different glycoproteins, such as cross-reactive carbohydrate determinants (CCDs) and galactose α-1,3-galactose, can induce IgE reactivity with varied clinical significance. In this study, the possible participation of glycan from wheat gliadin, with respect to its IgE-binding capacity, was investigated in children with food allergies to wheat. Total IgE and wheat-specific IgE quantification, documentation of history, and/or oral food challenge (OFC) were performed for 52 children. Subjects with positive wheat-specific IgE were characterized as the symptomatic group, never-exposed group, or asymptomatic group. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and glycan detection in gliadin were performed. IgE binding to gliadin and deglycosylated gliadin was measured by immunoblotting and ELISA. Gliadin-specific IgE was detected and correlated with wheat-specific IgE in the symptomatic, never-exposed, and asymptomatic groups. The glycan range overlapped significantly with the gliadin range. Deglycosylation of gliadin reduced the allergenicity of gliadin. In gliadin, the allergenicity of the glycan portion was greater in the symptomatic group than in the never-exposed and asymptomatic groups. We conclude that N-glycan in gliadin might exhibit allergenicity as a possible carbohydrate epitope in wheat allergy in children.

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“…Asparagine (N)-linked glycosylation is the major co-and post-translational modification of proteins in plants [150]. The application of a great diversity of molecular techniques permitted the identification of glycosylated isoforms in many types of storage proteins and species: globulins (7S-and 11S-globulins and convicilin) in adzuki bean (Vigna angularis L.), blue lupins (Lupinus angustifolius L.), cocoa beans (Theobroma cacao L.), common beans, hazelnuts (Corylus avellane L.), lentils, Lotus (Lotus japonicus L.), mung beans (Vigna radiata L.), peas (Pisum sativum L.), peanuts (Arachis hipogea L.), soybeans and white lupin (Lupinus albus L.) [42,120,121,; prolamins (γ3-hordein) in barley [180]; albumins (3S albumins) in Inca peanuts (Plukenetia volubilis L.) [181]; glutelins in rice [135,182]; VSPs (patatin) in potatoes [30,43,[183][184][185][186]; and lectins (monocot mannose-binding lectin, phytohemagglutinin) in air potatoes (Dioscorea bulbifera L.), common beans and lotus [121,[187][188][189][190][191][192][193].…”

Section: Seed Germinationmentioning

confidence: 99%

Analysis of Peptides and Proteins by Electrophoretic Techniques

Herrero‐Martínez¹,

Piergiovanni²

2019

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Barley γ3-hordein: Glycosylation at an atypical site, disulfide bridge analysis, and reactivity with IgE from patients allergic to wheat

Cited by 8 publications

References 44 publications

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

Advances in the Biology of Seed and Vegetative Storage Proteins Based on Two-Dimensional Electrophoresis Coupled to Mass Spectrometry

IgE reactivity to carbohydrate moieties of glycoproteins in wheat allergy

Analysis of Peptides and Proteins by Electrophoretic Techniques

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