Newly defined allergens in the WHO/IUIS Allergen Nomenclature Database during 01/2019‐03/2021

Sudharson, Srinidhi; Kalic, Tanja; Häfner, Christine; Breiteneder, Heimo

doi:10.1111/all.15021

Cited by 43 publications

(28 citation statements)

References 90 publications

(201 reference statements)

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“…Ara h 5 is formed by three weakly bonded alpha-helices and a seven-stranded anti-parallel sheet. Feeble bonds are the reason behind its weak resistance to heat and digestion [ 45 ]. Moreover, it is found in minute amounts in peanut protein, resulting in low-frequency sensitization in peanuts.…”

Section: Peanut Allergens and Their Mechanisms Of Actionmentioning

confidence: 99%

“…Furthermore, minor peanut allergens Ara h 16, 17, and 18 are similar to pollen allergens, particularly olive pollen in the case of Ara h 18 [ 35 , 40 ]. Functions of peanut allergens, their cross-reactivity and clinical relevance [ 19 , 28 , 32 , 33 , 35 , 45 , 46 , 49 , 50 , 51 ] are summarized in Table 2 .…”

Section: Peanut Allergens and Their Mechanisms Of Actionmentioning

confidence: 99%

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Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing

Haidar

Lakkis

Karam

et al. 2023

Foods

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Peanuts are the seeds of a legume crop grown for nuts and oil production. Peanut allergy has gained significant attention as a public health issue due to its increasing prevalence, high rate of sensitization, severity of the corresponding allergic symptoms, cross-reactivity with other food allergens, and lifelong persistence. Given the importance of peanuts in several sectors, and taking into consideration the criticality of their high allergic potential, strategies aiming at mitigating their allergenicity are urgently needed. In this regard, most of the processing methods used to treat peanuts are categorized as either thermal or thermomechanical techniques. The purpose of this review is to provide the reader with an updated outlook of the peanut’s allergens, their mechanisms of action, the processing methods as applied to whole peanuts, as well as a critical insight on their impact on the allergenicity. The methods discussed include boiling, roasting/baking, microwaving, ultrasonication, frying, and high-pressure steaming/autoclaving. Their effectiveness in alleviating the allergenicity, and their capacity in preserving the structural integrity of the treated peanuts, were thoroughly explored. Research data on this matter may open further perspectives for future relevant investigation ultimately aiming at producing hypoallergenic peanuts.

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Section: Peanut Allergens and Their Mechanisms Of Actionmentioning

confidence: 99%

Section: Peanut Allergens and Their Mechanisms Of Actionmentioning

confidence: 99%

Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing

Haidar

Lakkis

Karam

et al. 2023

Foods

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“…While eight foods (crustaceans, egg, fish, milk, peanuts, soy, tree nuts, and wheat) most commonly cause food allergy, numerous other foods have been identified as allergens [ 12 , 32 ]. Despite this, a majority of allergens arise from only a few protein families [ 33 ].…”

Section: Discussionmentioning

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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“…Despite the availability of multiple established 146 databases that provide nomenclature, structure, and reference referrals for molecular allergens, 146,147 none of these databases provide a comprehensive listing of the internationally-accepted nomenclature codes and Linnean system descriptors of the ~1000 extract-based and molecular allergens used world-wide in diagnostic single-and multiplex IgE antibody assays.…”

Section: Diagnostic Allergen Database (Dadb)mentioning

confidence: 99%

EAACIMolecular Allergology User's Guide 2.0

Dramburg

Hilger

Santos

et al. 2023

Pediatric Allergy Immunology

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119

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Since the discovery of immunoglobulin E (IgE) as a mediator of allergic diseases in 1967, our knowledge about the immunological mechanisms of IgE‐mediated allergies has remarkably increased. In addition to understanding the immune response and clinical symptoms, allergy diagnosis and management depend strongly on the precise identification of the elicitors of the IgE‐mediated allergic reaction. In the past four decades, innovations in bioscience and technology have facilitated the identification and production of well‐defined, highly pure molecules for component‐resolved diagnosis (CRD), allowing a personalized diagnosis and management of the allergic disease for individual patients. The first edition of the “EAACI Molecular Allergology User's Guide” (MAUG) in 2016 rapidly became a key reference for clinicians, scientists, and interested readers with a background in allergology, immunology, biology, and medicine. Nevertheless, the field of molecular allergology is moving fast, and after 6 years, a new EAACI Taskforce was established to provide an updated document. The Molecular Allergology User's Guide 2.0 summarizes state‐of‐the‐art information on allergen molecules, their clinical relevance, and their application in diagnostic algorithms for clinical practice. It is designed for both, clinicians and scientists, guiding health care professionals through the overwhelming list of different allergen molecules available for testing. Further, it provides diagnostic algorithms on the clinical relevance of allergenic molecules and gives an overview of their biology, the basic mechanisms of test formats, and the application of tests to measure allergen exposure.

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Newly defined allergens in the WHO/IUIS Allergen Nomenclature Database during 01/2019‐03/2021

Cited by 43 publications

References 90 publications

Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing

Peanut Allergenicity: An Insight into Its Mitigation Using Thermomechanical Processing

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

EAACIMolecular Allergology User's Guide 2.0

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