2S albumins and 11S globulins, two storage proteins involved in pumpkin seeds allergy

Allergy ◽  
2020 ◽  
Vol 76 (1) ◽  
pp. 383-386
Author(s):  
Cristina Bueno‐Díaz ◽  
Laura Martín‐Pedraza ◽  
Laura León ◽  
Elisa Haroun‐Díaz ◽  
Carlos Pastor‐Vargas ◽  
...  
Keyword(s):  
Storage Proteins ◽  
2S Albumins ◽  
Pumpkin Seeds ◽  
11S Globulins

scholarly journals Anaphylaxis following the consumption of pumpkin seeds in a two-year-old child tolerant to its pulp – a case study and a minireview

2020 ◽  
Author(s):  
Julia Gawryjołek ◽  
Hanna Ludwig ◽  
Magdalena Żbikowska-Gotz ◽  
Zbigniew Bartuzi ◽  
Aneta Krogulska
Keyword(s):  
Storage Proteins ◽  
Sesame Seed ◽  
Specific Ige ◽  
Elimination Diet ◽  
Cross Reactivity ◽  
Amino Acid Sequences ◽  
Pumpkin Seed ◽  
Potential Health ◽  
Prick Test ◽  
Pumpkin Seeds

Abstract BackgroundPumpkin and its seeds are increasingly consumed by children for their potential health benefits. Each day, around 30% of teenagers consume nuts and seeds, including pumpkin seeds. However, there is some evidence that pumpkin seeds may exert allergenic effects and induce severe life-threatening anaphylaxis. Allergy for melon, cucumber, and zucchini, which belong to the same Cucurbitaceae family as pumpkin, are well known, opposite to pumpkin allergy. Few descriptions of allergic reactions associated with pumpkin have been published, especially in children. To date, three cases of pumpkin pulp and two seed cases have been reported among children. Our case report describes a case of pumpkin seed anaphylaxis in a child with good tolerance of pulp.Case presentationIn the present study, a two-year-old child experienced anaphylaxis: generalized urticaria, swollen lips and increasing dyspnea following the consumption of pumpkin seeds. The history showed that although the child had been receiving elimination diet because of atopic dermatitis, the basic dietary element was pumpkin pulp. The skin-prick test was positive for pumpkin seeds (5 mm) but negative for pumpkin pulp (1 mm); allergen-specific IgE was 1.34 kUA/L for seed, and 0.37 kUA/L for pulp. The component resolved diagnosis found IgE to sesame seed, buckwheat and walnut (storage proteins). Based on these findings, severe anaphylactic reaction to pumpkin seeds was identified.ConclusionsIt is possible to develop pumpkin seed anaphylaxis in a child with a tolerance to pumpkin pulp. Pumpkin seeds allergens have not been well characterized. Homology between the amino acid sequences in storage proteins may indicate cross reactivity between different edible seeds and nuts.

scholarly journals Anaphylaxis to Sunflower Seed with Tolerance to Sunflower Oil: A Case Report

Medicina ◽  
2021 ◽  
Vol 57 (7) ◽  
pp. 661
Author(s):  
Jin An
Keyword(s):  
Sunflower Oil ◽  
Sunflower Seed ◽  
Storage Proteins ◽  
Lipid Transfer ◽  
Sunflower Seeds ◽  
Lipid Transfer Proteins ◽  
Prick Test ◽  
Severe Anaphylaxis ◽  
Provocation Tests ◽  
2S Albumins

Sunflower seeds (Helianthus annuus) are an uncommon source of allergy; however, some cases of allergy to sunflower seeds have been reported. Sunflower seed sensitization occurs to storage proteins (2S albumins) and lipid transfer proteins (LTPs). A 46-year-old female presented three allergic reactions within minutes of consuming sunflower seeds. A prick-to-prick test indicated a positive reaction only to sunflower seeds and a negative reaction to other nuts, such as almond, hazelnut, pistachio, cashew, peanut, macadamia, sesame, and walnut. Prick-to-prick and oral provocation tests of sunflower oil were performed, and a negative result was obtained. The patient was prescribed a 0.3 mg epinephrine autoinjector device for emergency intramuscular administration. The patient is currently under avoidance of sunflower seed but eats food cooked in sunflower seed oil. Based on this case, we should recognize that sunflower seeds have the potential to cause severe anaphylaxis, which indicates tolerance to sunflower oil. An accurate and fast diagnosis allows timely recommendation to practice strict avoidance of sunflower seeds, thus reducing the possibility of recurrence of an anaphylactic reaction.

scholarly journals Onset of nut allergy in a pediatric cohort: clinical and molecular patterns. AFRUSEN study

2021 ◽  
Vol 32 (4) ◽  
Author(s):  
MD Ibáñez-Sandin ◽  
◽  
P Rodríguez del Río ◽  
MI Alvarado ◽  
BE García ◽  
...  
Keyword(s):  
Allergic Reaction ◽  
Peanut Allergy ◽  
Storage Proteins ◽  
Food Challenge ◽  
Clinical History ◽  
Preventive Strategies ◽  
Anglo Saxon ◽  
2S Albumins ◽  
Molecular Patterns ◽  
First Time

Background: Nut allergy is a growing problem, but little is known about its onset in children. Objective: Characterize the onset of nut allergy in Southern European children. Methods: Consecutive patients up to 14years of age who presented to allergy departments with an initial allergic reaction to peanut, tree nut, or seed were included. An allergy workup including clinical history, food challenge, SPT, and whole-extract sIgE and ImmunoCAP 112-ISAC assay were performed. Results: Of the 271 children included, 260 were first diagnosed with nut allergy at age 6.5years, 11.8(±21.2SD) months after the index reaction. The most common culprit nuts at onset were walnut (36.5%), peanut (28.5%), cashew(10.4%), hazelnut (8.5%), pistachio (5.4%), and almond (5%). Peanut-allergy onset was more frequent in children ≤6y.o. and walnut in those >6y.o. (p=0.032). In 65% of cases, the allergic reaction occurred the first time the patient consumed the nut, and 35% of reactions were anaphylactic. Overall, nut polysensitization was detected by SPT in 64.9% of patients, though this rate was lower among walnut- (54.7%) and peanut (54.1%)-allergic children (p<0.0001). Sensitization to 2S albumins was predominant (75%), specially Jug r1 (52.8%), whereas LTPs was less relevant (37%). Conclusion: In our population, the onset of nut allergy occured around 6years of age, slightly later than that reported in Anglo-Saxon countries. Walnut was the main trigger, followed by peanut and 2S albumins storage proteins, especially Jug r1, are the most relevant allergens. This study will help guide management and may contribute to preventive strategies in pediatric nut allergy.

Trafficking to the seed protein storage vacuole

2018 ◽  
Vol 45 (9) ◽  
pp. 895
Author(s):  
Joanne R. Ashnest ◽  
Anthony R. Gendall
Keyword(s):  
Storage Proteins ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Protein Storage ◽  
Protein Storage Vacuole ◽  
2S Albumins ◽  
Vacuolar Sorting ◽  
Mechanistic Understanding ◽  
Lytic Vacuole ◽  
Storage Vacuole

The processing and subcellular trafficking of seed storage proteins is a critical area of physiological, agricultural and biotechnological research. Trafficking to the lytic vacuole has been extensively discussed in recent years, without substantial distinction from trafficking to the protein storage vacuole (PSV). However, despite some overlap between these pathways, there are several examples of unique processing and machinery in the PSV pathway. Moreover, substantial new data has recently come to light regarding the important players in this pathway, in particular, the intracellular NHX proteins and their role in regulating lumenal pH. In some cases, these new data are limited to genetic evidence, with little mechanistic understanding. As such, the implications of these data in the current paradigm of PSV trafficking is perhaps yet unclear. Although it has generally been assumed that the major classes of storage proteins are trafficked via the same pathway, there is mounting evidence that the 12S globulins and 2S albumins may be trafficked independently. Advances in identification of vacuolar targeting signals, as well as an improved mechanistic understanding of various vacuolar sorting receptors, may reveal the differences in these trafficking pathways.

Influence of globulin subunit composition of soybean proteins on silken tofu quality. 1. Effect of growing location and 11SA4 and 7Sα’ deficiency

2014 ◽  
Vol 65 (3) ◽  
pp. 259 ◽  
Author(s):  
Aijun Yang ◽  
Andrew T. James
Keyword(s):  
Water Loss ◽  
Storage Proteins ◽  
Subunit Composition ◽  
Major Protein ◽  
Soybean Proteins ◽  
Protein Subunits ◽  
Soybean Genotypes ◽  
Tofu Quality ◽  
Location Interaction ◽  
11S Globulins

Growing location and genotypes are known to affect the subunit composition of the major storage proteins of soybeans, β-conglycinin (7S globulins) and glycinin (11S globulins), which have been associated with tofu quality. In this study, we examined 16 soybean genotypes grown at two locations in Queensland, Australia, for the influence of globulin subunit composition, growing location and genotype × growing location interaction on seed, soymilk and silken tofu properties. These genotypes comprised four groups: with all globulin subunits, without 11SA4, without 7Sα’, or without 11SA4 and 7Sα’. There were significant differences in the major protein subunits among the genotypes and the four groups and between locations. Significant genotypic and location differences were also observed in the properties of the seed, soymilk and silken tofu. There were no significant genotype × location interactions. The group without 11SA4 had less 11S and more 7S globulins, resulting in the lowest 11S/7S ratio. The silken tofu from this group had firmer texture and less water loss than the group containing all globulin subunits. The results suggested that genotypes of differing globulin subunit composition may produce tofu with different qualities and the effect of globulin subunit composition on tofu quality could be affected by growing location and the absence of certain globulin subunits.

scholarly journals Predicting the allergenicity of legume proteins using a PBMC gene expression assay

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Mark Smits ◽  
Marjolein Meijerink ◽  
Thuy-My Le ◽  
André Knulst ◽  
Aard de Jong ◽  
...  
Keyword(s):  
Gene Expression ◽  
Human Peripheral Blood ◽  
Protein Family ◽  
Food Proteins ◽  
Gene Expression Assay ◽  
2S Albumins ◽  
White Bean ◽  
Legume Proteins ◽  
7S And 11S Globulins ◽  
11S Globulins

Abstract Background Food proteins differ in their allergenic potential. Currently, there is no predictive and validated bio-assay to evaluate the allergenicity of novel food proteins. The objective of this study was to investigate the potential of a human peripheral blood mononuclear cell (PBMC) gene expression assay to identify biomarkers to predict the allergenicity of legume proteins. Results PBMCs from healthy donors were exposed to weakly and strongly allergenic legume proteins (2S albumins, and 7S and 11S globulins from white bean, soybean, peanut, pea and lupine) in three experiments. Possible biomarkers for allergenicity were investigated by exposing PBMCs to a protein pair of weakly (white bean) and strongly allergenic (soybean) 7S globulins in a pilot experiment. Gene expression was measured by RNA-sequencing and differentially expressed genes were selected as biomarkers. 153 genes were identified as having significantly different expression levels to the 7S globulin of white bean compared to soybean. Inclusion of multiple protein pairs from 2S albumins (lupine and peanut) and 7S globulins (white bean and soybean) in a larger study, led to the selection of CCL2, CCL7, and RASD2 as biomarkers to distinguish weakly from strongly allergenic proteins. The relevance of these three biomarkers was confirmed by qPCR when PBMCs were exposed to a larger panel of weakly and strongly allergenic legume proteins (2S albumins, and 7S and 11S globulins from white bean, soybean, peanut, pea and lupine). Conclusions The PBMC gene expression assay can potentially distinguish weakly from strongly allergenic legume proteins within a protein family, though it will be challenging to develop a generic method for all protein families from plant and animal sources. Graded responses within a protein family might be of more value in allergenicity prediction instead of a yes or no classification.

Phosphorylated 11S globulins in sunflower seeds

2013 ◽  
Vol 23 (3) ◽  
pp. 199-204 ◽  
Author(s):  
Ivana Quiroga ◽  
Mariana Regente ◽  
Luciana Pagnussat ◽  
Ana Maldonado ◽  
Jesús Jorrín ◽  
...  
Keyword(s):  
Storage Proteins ◽  
Laser Desorption ◽  
Major Protein ◽  
Laser Desorption Ionization ◽  
Sunflower Seeds ◽  
Ionization Time ◽  
11S Globulin ◽  
11S Globulins ◽  
Matrix Assisted Laser ◽  
Matrix Assisted Laser Desorption

AbstractHelianthinins are storage proteins present in Helianthus annuus seeds, belonging to the 11S globulin family. Here we describe that a fraction of the helianthinins is phosphorylated. This conclusion is supported by different criteria, including identification by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry of major protein bands revealed with a specific dye for phosphoproteins, anti-phosphoserine antibody and binding to a phosphoprotein affinity matrix. Moreover, we show that the phosphorylation status of helianthinins changes following germination.

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