Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease

Abstract

Brachypodium distachyon, a small annual grass with seed storage globulins as primary protein reserves was used in our study to analyse the toxic nature of non-prolamin seed storage proteins related to celiac disease. The main storage proteins of B. distachyon are the 7S globulin type proteins and the 11S, 12S seed storage globulins similar to oat and rice. Immunoblot analyses using serum samples from celiac disease patients were carried out followed by the identification of immune-responsive proteins using mass spectrometry. Serum samples from celiac patients on a gluten-free diet, from patients with Crohn’s disease and healthy subjects, were used as controls. The identified proteins with intense serum-IgA reactivity belong to the 7S and 11–12S seed globulin family. Structure prediction and epitope predictions analyses confirmed the presence of celiac disease-related linear B cell epitope homologs and the presence of peptide regions with strong HLA-DQ8 and DQ2 binding capabilities. These results highlight that both MHC-II presentation and B cell response may be developed not only to prolamins but also to seed storage globulins. This is the first study of the non-prolamin type seed storage proteins of Brachypodium from the aspect of the celiac disease.

Survey of High Throughput RNA-Seq Data Reveals Potential Roles for lncRNAs during Development and Stress Response in Bread Wheat

“…A few highly represented annotations were- receptor like kinases (RLK) such as leucine rich repeat (LRR) (GO: 0005515), wall associated (GO: 0006468, GO: 0005524, GO: 0004672), and cysteine rich repeat (GO:0006468, GO:0005524, GO:0004672) RLKs, photosystem II 10 kDa protein (GO:0009654, GO:0042651, GO:0015979), disease resistant protein RPM1 (GO:0043531) in leaf; pectinesterase/ pectinesterase inhibitor 13 (GO:0005618, GO:0042545, GO:0004857, GO:0030599), Rho guanine nucleotide exchange factor 8 (GO:0005089), and Cytochrome P450 86A2 (GO:0016705, GO:0055114, GO:0020037) in spike; and Serpin Z7 (GO:0005615), rab protein (GO:0006950, GO:0009415), Defensin-like protein 1 (GO:000695), globulin 3A (GO:0045735), Low temperature-induced protein (GO:0016021), WSCI proteinase inhibitor (GO:0009611, GO:0004867) and various predicted proteins in grain. Since these genes play vital role in numerous developmental and other biological processes (Ljungberg et al, 1986 ; Nordin et al, 1993 ; Hubert et al, 2003 ; Okuda et al, 2009 ; Saito and Ueda, 2009 ; Gish and Clark, 2011 ; Francis et al, 2012 ; Tedeschi et al, 2012 ; Gu et al, 2016 ; Gell et al, 2017 ; Xing et al, 2017 ); the co-expressed lncRNAs might also be responsible for similar functions.…”

Methods for the Modification and Evaluation of Cereal Proteins for the Substitution of Wheat Gluten in Dough Systems

“…Prolamins are not the only major storage proteins found in the endosperm of cereals. In rice, its storage protein content is mainly constituted of globulins and not its prolamin, orizein [ 9 , 44 ]. Globulins are protein fractions soluble in salt solutions and present a more globular structure than prolamins ( Figure 3 ), where the globulin subunits comparatively form a more spherical shape [ 45 , 46 , 47 ].…”

Biostimulant Effects of Glutacetine® and Its Derived Formulations Mixed With N Fertilizer on Post-heading N Uptake and Remobilization, Seed Yield, and Grain Quality in Winter Wheat

“…Foliar application of Glutacetine R also decreased other storage proteins. Regarding globulin storage proteins, Gell et al (2017) have recently characterized this family of storage proteins in Plant culture was carried out under semi-hydroponic conditions on a sand/perlite (1/1) substrate (see the Materials and Methods section for details). N was provided at the tillering (eq.…”

“…Therefore, it is difficult to conclude whether Glutacetine R application led to a significant improvement in the baking quality. However, it is well documented that α-gliadins (Zörb et al, 2013) and 12S seed storage globulins (Gell et al, 2017) are initiators of the inflammatory response in celiac disease patients. In durum wheat, Pichereaux et al (2019) have reported the effects of marine and fungal biostimulant treatments on the grain proteome, and especially proteins involved in grain technological properties, such as the gluten protein gamma-gliadin, which increased 100fold following treatment.…”

“…Because they contribute to baking quality, a balanced mixture of these components is crucial (Barak et al, 2013). However, these proteins are also related to celiac disease (Gell et al, 2017;Perrin et al, 2019) and especially the α-gliadins (Sollid et al, 2012;Zörb et al, 2013). A downregulation of these proteins, while still maintaining dough proprieties, might be a solution for celiac disease patients (Altenbach et al, 2020).…”