Structural, functional, and evolutionary analysis of late embryogenesis abundant proteins (LEA) in Triticum aestivum: A detailed molecular level biochemistry using in silico approach

Bhattacharya, Shreya; Dhar, Shreyeshi; Banerjee, Arundhati; Ray, Sujay

doi:10.1016/j.compbiolchem.2019.06.005

Cited by 13 publications

(16 citation statements)

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“…An additional group of proteins nearly neglected in previous proteomic investigations, but found ubiquitous in the beer samples analyzed herein, was constituted by dehydrins. These proteins belong to the late embryogenesis abundant proteins, a numerous group of versatile hydrophilic cereal proteins, involved in the protection from abiotic stress such as desiccation or temperature injury ( 31 ).…”

Section: Resultsmentioning

confidence: 99%

Immunogenic Potential of Beer Types Brewed With Hordeum and Triticum spp. Malt Disclosed by Proteomics

et al. 2020

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The protein/peptide composition of five beer kinds, including two experimental beer-like products brewed with einkorn ( Triticum monococcum ), a beer labeled as “gluten-free,” a traditional all-barley malt and a wheat ( T. aestivum ) containing beer, was characterized with HPLC-ESI MS/MS-based proteomics. To enlarge the characterization of the components, the polypeptides were fractionated according to their molecular size (cut-off 6 kDa). All the beer types contained a variety of polypeptides arising from all the gliadin subfamilies (α-/β-, γ-, and ω-gliadins) able to induce an immune response in celiac disease (CD) patients in addition to a panel of IgE-reactive food allergens. Wheat storage proteins were heavily hydrolyzed in the beer samples brewed with einkorn. The presence of gluten-like fragments, also including the 25-mer and 33-mer-like of α-gliadin, was confirmed in beer brewed with barley and wheat malt as well as in the gluten-free beer. Both CD-toxic and allergenic peptides of all beer samples were drastically degraded when subjected to a simulated gastroduodenal (GD) digestion. After in vitro digestion, the level of gluten-like peptides assayed with the G12 competitive ELISA, was below the threshold (20 ppm) for a food to be considered as “gluten-free.” A few gliadin-derived epitopes occurred in the digests of beers crafted with wheat or Norberto-ID331 line of einkorn. In contrast, digests of all barley malt and gluten-free beers did not contain detectable gluten-like epitopes, but only minor fragments of hordeins and IgE-reactive food allergens. All beer samples evoked a weak immune response on gliadin-reactive celiac T cells isolated from intestinal biopsies of celiac patients. Compared to undigested polypeptides, the response was markedly reduced by GD digestion. Although the consumption of a moderate amount of beer brewed with barley or einkorn could deliver a relatively low amount of CD-toxic epitopes, the findings of this study emphasize the urgent need of a reliable and accurate quantification of gluten epitopes in all types of beer, also including the gluten-free one, to compute realistically the contribution of beer to the overall gluten intake, which can be responsible of intestinal tissue damages in celiacs.

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Section: Resultsmentioning

confidence: 99%

Immunogenic Potential of Beer Types Brewed With Hordeum and Triticum spp. Malt Disclosed by Proteomics

et al. 2020

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“…Similarly, 242 LEAPs were identified in upland cotton, G. hirsutum , classified into eight groups ranging from LEA1 to LEA6, dehydrin, and SMP [ 15 ]. Forty identified wheat LEAPs were classified into six classes: LEApdB classes 1–4 containing the dehydrin domain (PF00257), LEApdB class 5 containing the PF00477 domain, and LEApdB class 6 containing the PF02987 domain [ 17 ]. Noticeably, the LEA6 protein family group was absent in R. serbica , as well as in Oryza sativa [ 19 ].…”

Section: Discussionmentioning

confidence: 99%

“…The range of pI values for R. serbica was following the one presented for the wheat LEAPs [ 17 ]. The average pI values obtained for the R. serbica LEA protein family groups showed better correlation with the G. hirsutum LEA groups, namely for dehydrins, SMPs, and LEA2 proteins, while neutral R. serbica LEA3 protein group members differed from significantly basic cotton LEA3 proteins [ 15 ].…”

Section: Discussionmentioning

confidence: 99%

“…A hallmark of desiccation tolerance is the accumulation of protective late embryogenesis abundant proteins (LEAPs), which may stabilise the correct structure of proteins and membranes during cellular dehydration [ 3 , 12 , 13 ]. In-depth studies and characterisations of LEA protein families have been carried out in various plants such as Arabidopsis [ 14 ], upland cotton [ 15 ], potato [ 16 ], common wheat [ 17 ], tea plant [ 18 ], rice [ 19 ], pearl millet [ 20 ], Sorghum bicolor [ 21 ], legumes [ 22 ], and desert plant Cleistogenes songorica [ 23 ]. An identification and detailed structural and functional analysis of LEA proteins of resurrection plant species R. serbica has not been done yet.…”

Section: Introductionmentioning

confidence: 99%

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In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc

Pantelić

Stevanović

Komić

et al. 2022

IJMS

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Ramonda serbica Panc. is an ancient resurrection plant able to survive a long desiccation period and recover metabolic functions upon watering. The accumulation of protective late embryogenesis abundant proteins (LEAPs) is a desiccation tolerance hallmark. To propose their role in R. serbica desiccation tolerance, we structurally characterised LEAPs and evaluated LEA gene expression levels in hydrated and desiccated leaves. By integrating de novo transcriptomics and homologues LEAP domains, 318 R. serbica LEAPs were identified and classified according to their conserved motifs and phylogeny. The in silico analysis revealed that hydrophilic LEA4 proteins exhibited an exceptionally high tendency to form amphipathic α-helices. The most abundant, atypical LEA2 group contained more hydrophobic proteins predicted to fold into the defined globular domains. Within the desiccation-upregulated LEA genes, the majority encoded highly disordered DEH1, LEA1, LEA4.2, and LEA4.3 proteins, while the greatest portion of downregulated genes encoded LEA2.3 and LEA2.5 proteins. While dehydrins might chelate metals and bind DNA under water deficit, other intrinsically disordered LEAPs might participate in forming intracellular proteinaceous condensates or adopt amphipathic α-helical conformation, enabling them to stabilise desiccation-sensitive proteins and membranes. This comprehensive LEAPs structural characterisation is essential to understanding their function and regulation during desiccation aiming at crop drought tolerance improvement.

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“…LEA proteins are a family of highly hydrophilic proteins that accumulate at high levels during the late stage of seed development and in response to desiccation stress (Bhattacharya, Dhar, Banerjee, & Ray, 2019). They could function as osmo‐protective molecules, remove ROS, help to stabilize proteins and maintain membrane structures under such conditions (Battaglia, Olvera‐Carrillo, Garciarrubio, Campos, & Covarrubias, 2008).…”

Section: Discussionmentioning

confidence: 99%

Enhanced defense ability facilitates the water loss of maize kernels during physiological dehydration

et al. 2020

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The kernel water concentration (KWC) varies more intensely during the physiological dehydration phase, and the dehydration process during this phase has been demonstrated to be closely associated with internal physiological processes in maize kernels. To better illustrate the physiological dehydration process (PDP) of maize kernels, moisture characteristic parameters were consecutively recorded after pollination, and the timing of the occurrence of net water loss was confirmed. Additionally, a tandem mass tag (TMT) based proteomic analysis was performed to identify the significantly differentially expressed proteins during the critical period of the PDP (PDP cp). The results showed that maize varieties presented significant variance in the KWC, kernel water content, dry-down rate (DR) and absolute DR; nevertheless, the KWC was similar (below 65%) when net water loss occurred. In addition, 20-28 days after pollination was indicated to be the PDP cp in this study. Based on proteome analysis, Yuyu 30 and Suyu 41 showed 163 and 132 differentially expressed proteins (DEPs), respectively during the PDP cp and 99 DEPs overlapped between the varieties. During the PDP cp , the desiccation tolerance, antioxidation capability, detoxification and other stress response abilities of maize kernels were significantly increased. The increased defense abilities enabled the maize kernels to establish coordinated, diverse, stable defense mechanisms that accelerated water loss from maize kernels during the PDP cp .

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Structural, functional, and evolutionary analysis of late embryogenesis abundant proteins (LEA) in Triticum aestivum: A detailed molecular level biochemistry using in silico approach

Cited by 13 publications

References 80 publications

Immunogenic Potential of Beer Types Brewed With Hordeum and Triticum spp. Malt Disclosed by Proteomics

Immunogenic Potential of Beer Types Brewed With Hordeum and Triticum spp. Malt Disclosed by Proteomics

In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc

Enhanced defense ability facilitates the water loss of maize kernels during physiological dehydration

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