The Discovery of 2S Albumins as Abundant Storage Proteins in Seeds

2000 ◽  
pp. 255-265
Author(s):  
Anthony H. C. Huang ◽  
Richard J. Youle
Keyword(s):  
Medicina ◽  
2021 ◽  
Vol 57 (7) ◽  
pp. 661
Author(s):  
Jin An

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.


Author(s):  
MD Ibáñez-Sandin ◽  
◽  
P Rodríguez del Río ◽  
MI Alvarado ◽  
BE García ◽  
...  

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.


Allergy ◽  
2020 ◽  
Vol 76 (1) ◽  
pp. 383-386
Author(s):  
Cristina Bueno‐Díaz ◽  
Laura Martín‐Pedraza ◽  
Laura León ◽  
Elisa Haroun‐Díaz ◽  
Carlos Pastor‐Vargas ◽  
...  

2018 ◽  
Vol 45 (9) ◽  
pp. 895
Author(s):  
Joanne R. Ashnest ◽  
Anthony R. Gendall

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.


Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.


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