Components of plant-derived food allergens: Structure, diagnostics, and immunotherapy

Maruyama, Nobuyuki

doi:10.1016/j.alit.2021.05.001

Cited by 14 publications

(10 citation statements)

References 97 publications

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“…(6,36). (36,43). Due to cross-reactivity between homologous allergenic molecules, patients hypersensitive to tree pollen (birch, hazel and alder) may experience transient oropharyngeal symptoms (mostly PFAS) after consumption of particular Bet v 1-related plant fruits (eg apple, pear, apricot, cherry, plum, hazelnut, walnut, almond, mango, avocado, kiwi) and vegetables (tomatoe, carrot, fennel, celery, soybean), those containing PR-10-P. Generally, symptoms appear often within a few minutes, (sometimes immediately) after consumption of raw plant food, not after being heat-treated or acidified (6).…”

Section: Allergenic Molecules In Clinical Practicementioning

confidence: 99%

Genuine and cross-reactive allergenic molecules of birch and hazel

Dodig¹

2021

Rad Hrvatske akademije znanosti i umjetnosti

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Birch and hazel pollen are the most common causes of allergic diseases that occur during the spring season. For decades, the method of quantitative determination of specific IgE (sIgE) against allergen extracts has been used in the laboratory diagnosis of allergies. In recent years, there has been the possibility of determining sIgE by individual allergenic molecules, either native or recombinant. This method, known as Component Resolved Diagnosis (CRD), has made it possible to identify major and cross-reactive allergenic molecules. Genuine allergenic molecules in birch (Bet v 1), hazel (Cor a 1) and hazelnut (Cor a 8, 9, 11, 14) are responsible for allergic reactions in most patients. Moreover, they cause a severe clinical picture in patients with hypersensitivity, in contrast to cross-reactive molecules, eg. Bet v 1 homologues in vegetables (celery, soy) and fruits (apple, cherry, pear), or Bet v 2 homologues in vegetables (celery, carrot) and fruits (muskmelon, peach, banana), that cause milder symptoms. In the diagnostic context, future research will make it possible to determine the diagnostic significance of the detection of individual allergen molecules responsible for allergy symptoms in each individual patient. The application of bioinformatics will certainly help in the interpretation of the findings, especially in cases when multiplex assays are applied. Particular progress is also expected in the application of allergen molecules to allergen-specific immunotherapy.

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Section: Allergenic Molecules In Clinical Practicementioning

confidence: 99%

Genuine and cross-reactive allergenic molecules of birch and hazel

Dodig¹

2021

Rad Hrvatske akademije znanosti i umjetnosti

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“…Proteins derived from plants are often found to be associated with food allergies. These include oleosin from peanuts, gluten from wheat, or non-specific lipid transfer proteins (ns-LTPs) from seeds and fruit ( Maruyama, 2021 ). Increased incorporation of plant protein into processed foods makes it important that product labelling and manufacturing control measures are in place ( Taylor, 2021 ).…”

Section: Protein In Foodmentioning

confidence: 99%

“…In silico methods compare peptide sequences that would result from the protein entering the human digestive tract with known sequence of allergenic effect ( Krutz et al , 2019 ). Although Rubisco has been identified as containing peptide sequences similar to those with known allergenic effects ( Yakhlef et al , 2021 ), Rubisco has very low allergenicity ( Fu et al , 2002 ; Bowman and Selgrade, 2009 ; Maruyama, 2021 ), with only one case being officially detailed ( Foti et al , 2012 ).…”

Section: Potential Of Rubisco As a Food Proteinmentioning

confidence: 99%

Is now the time for a Rubiscuit or Ruburger? Increased interest in Rubisco as a food protein

Pearce

Brunke

2022

Journal of Experimental Botany

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Much of the research on Rubisco (Ribulose-1,5-bisphosphate carboxylase/oxygenase) aims at increasing crop yields, with the aim of increasing plant production to feed an increasing global population. However, since the identification of Rubisco as the most abundant protein in leaf material, it has also been touted as a direct source of dietary protein. The nutritional and functional properties of Rubisco are on par with many animal proteins, and are superior to many other plant proteins. Purified Rubisco isolates are easily digestable, nutritionally complete, and have excellent foaming, gelling and emulsifying properties. Despite this potential, challenges in efficiently extracting and separating Rubisco have limited its use as a global foodstuff. Leaves are lower in protein than seeds, requiring large amounts of biomass to be processed. This material normally needs to be processed quickly to avoid degradation of the final product. Extraction of Rubisco from the plant material requires breaking down the cell walls and rupturing the chloroplast. In order to obtain high quality protein, Rubisco needs to be separated from chlorophyll, and then concentrated for final use. However, with increased consumer demand for plant protein, there is increased interest in the potential of leaf protein, and many commercial plants are now being established aimed at producing Rubisco as a food protein, with over $US60 million of funding invested in the past 5 years. Is now the time for increased use of Rubisco in food production as a nitrogen source, rather than just providing a carbon source?

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“…Legumin and vicilin proteins belong to the cupin superfamily and contain the characteristic β-barrel structure. Legumin proteins are composed of acidic and basic subunits, held together by cysteine disulfide bonds, that assemble as hexamers into large molecular weight complexes [ 17 ]. Vicilins are often glycated, composed of a single subunit, and associate into trimers [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE

Mattison

Zhang

et al. 2023

Molecules

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Food allergy is a potentially life-threatening health concern caused by immunoglobulin E (IgE) antibodies that mistakenly recognize normally harmless food proteins as threats. Peanuts and tree nuts contain several seed storage proteins that commonly act as allergens. Glandless cottonseed, lacking the toxic compound gossypol, is a new food source. However, the seed storage proteins in cottonseed may act as allergens. To assess this risk, glandless cottonseed protein extracts were evaluated for IgE binding by peanut and tree nut allergic volunteers. ELISA demonstrated that 25% of 32 samples had significant binding to cottonseed extracts. Immunoblot analysis with pooled sera indicated that IgE recognized a pair of bands migrating at approximately 50 kDa. Excision of these bands and subsequent mass-spectrometric analysis demonstrated peptide matches to cotton C72 and GC72 vicilin and legumin A and B proteins. Further, in silico analysis indicated similarity of the cotton vicilin and legumin proteins to peanut vicilin (Ara h 1) and cashew nut legumin (Ana o 2) IgE-binding epitopes among others. The observations suggest both the cotton vicilin and legumin proteins were recognized by the nut allergic IgE, and they should be considered for future allergen risk assessments evaluating glandless cottonseed protein products.

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Components of plant-derived food allergens: Structure, diagnostics, and immunotherapy

Cited by 14 publications

References 97 publications

Genuine and cross-reactive allergenic molecules of birch and hazel

Genuine and cross-reactive allergenic molecules of birch and hazel

Is now the time for a Rubiscuit or Ruburger? Increased interest in Rubisco as a food protein

Cross-Serological Reaction of Glandless Cottonseed Proteins to Peanut and Tree Nut Allergic IgE

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