Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Petersen, Arnd; Rennert, Sandra; Kull, Skadi; Becker, Wolf‐Meinhard; Notbohm, Holger; Goldmann, Torsten; Jappe, Uta

doi:10.1515/hsz-2013-0206

Cited by 46 publications

(58 citation statements)

References 51 publications

(65 reference statements)

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“…Due to their high polyunsaturated fatty acid content peanuts suffer lipid oxidation,during storage or roasting. Allergenicity could change if new protein-lipid complexes or changes in protein structures occur when the lipid hidroperoxides formed attack the proteins (74). …”

Section: Lipid Cargo May Affect Allergenicitymentioning

confidence: 99%

The Role of Lipids in Development of Allergic Responses

Moral

Martı́nez-Naves

2017

Immune Netw

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Most allergic diseases are caused by activation of Th2 type immune responses resulting in the production of specific IgE against proteins found in normally harmless substances such as pollen, mites, epithelia or food. Allergenic substances are composed, in addition to proteins, of other compounds such as carbohydrates and lipids. Those lipids are able to promote the development of Th2-type responses associated with allergy. There are lipids found in pollen, milk or insect venom that are specifically recognized by CD1 restricted unconventional T lymphocytes, which can promote allergic reactions. Furthermore, a large number of allergens are proteins containing hydrophobic parts that specifically bind lipids that are capable to favor allergenic immune responses. Also, lipids associated to substances like pollen, dander, epithelia or the bacteria can act on cells of the innate system, including dendritic cells, which in turn lead to the differentiation of Th2-type clones. Finally, lipids may also influence the ability of allergens to be exposed to the immune system within the oral, respiratory or intestinal mucosa where allergic response occurs with great frequency.

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Section: Lipid Cargo May Affect Allergenicitymentioning

confidence: 99%

The Role of Lipids in Development of Allergic Responses

Moral

Martı́nez-Naves

2017

Immune Netw

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“… 71 Food allergens of the Bet v 1–like family generally are susceptible to pepsin digestion and instable to thermal processing and usually provoke only mild allergic symptoms. A recent study on Ara h 8, the Bet v 1 homolog from peanut, showed that roasting of peanuts can dramatically increase not only its thermal stability but also protect the allergen against proteolysis by gastrointestinal enzymes 18 . Ara h 8 isolated from roasted peanuts showed enhanced IgE reactivity and was also recognized by more sera from patients with peanut allergy compared with Ara h 8 isolated from raw peanuts.…”

Section: Interaction Of Lipids and Food Allergensmentioning

confidence: 99%

Do lipids influence the allergic sensitization process?

Bublin

Eiwegger

Breiteneder

2014

Journal of Allergy and Clinical Immunology

130

111

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Allergic sensitization is a multifactorial process that is not only influenced by the allergen and its biological function per se but also by other small molecular compounds, such as lipids, that are directly bound as ligands by the allergen or are present in the allergen source. Several members of major allergen families bind lipid ligands through hydrophobic cavities or electrostatic or hydrophobic interactions. These allergens include certain seed storage proteins, Bet v 1–like and nonspecific lipid transfer proteins from pollens and fruits, certain inhalant allergens from house dust mites and cockroaches, and lipocalins. Lipids from the pollen coat and furry animals and the so-called pollen-associated lipid mediators are codelivered with the allergens and can modulate the immune responses of predisposed subjects by interacting with the innate immune system and invariant natural killer T cells. In addition, lipids originating from bacterial members of the pollen microbiome contribute to the outcome of the sensitization process. Dietary lipids act as adjuvants and might skew the immune response toward a TH2-dominated phenotype. In addition, the association with lipids protects food allergens from gastrointestinal degradation and facilitates their uptake by intestinal cells. These findings will have a major influence on how allergic sensitization will be viewed and studied in the future.

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“…The authentic structure of Ara h 8.0201 was confirmed by trypsin fingerprinting of isolated nAra h 8. In accordance with the Bet v 1 it was possible to show experimentally that Ara h 8 contains a hydrophobic region [68] in which lipids bind, which, according to preliminary experiments, may prevent the molecule from gastric digestion [68] . All in all these findings spotlight the significance of lipid-protein-(allergen) interaction.…”

Section: Ara H 5 and Ara Hmentioning

confidence: 65%

Peanut Allergens

Becker

Jappe

2014

Chemical Immunology and Allergy

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The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%, peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I food allergy, peanut allergy affects by far the largest group of patients. In peanuts, 12 allergens have been identified and their molecular characteristics are described herein. Ara h 1, Ara h 3.01 and Ara h 3.02 (the former Ara h 4) belong to the cupin superfamily. The conglutins Ara h 2, Ara h 6 and Ara h 7, and the non-specific lipid transfer protein Ara h 9 belong to the prolamin superfamily. Ara h 5 (profilin) and Ara h 8 (Bet v 1-homologous protein) cause class II food allergies and are associated with inhalation allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as Ara h 10 and Ara h 11 and two defensins as Ara h 12 and Ara h 13 by the WHO/IUIS Allergen Nomenclature Subcommittee. The effect of the above-specified allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.

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Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Cited by 46 publications

References 51 publications

The Role of Lipids in Development of Allergic Responses

The Role of Lipids in Development of Allergic Responses

Do lipids influence the allergic sensitization process?

Peanut Allergens

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