Structure and Function of the Peanut Panallergen Ara h 8

Hurlburt, Barry K.; Offermann, L.R.; McBride, Jane; Majorek, K.A.; Maleki, Soheila J.; Chruszcz, M.

doi:10.1074/jbc.m113.517797

Cited by 56 publications

(68 citation statements)

References 57 publications

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“…It is believed that a similar protein structure, rather than a similar linear sequence, is the reason for cross- reactivity among pollen (i.e., Bet v 1) and plant food [26], but it has also been demonstrated that isolated Api g 1- specific antibodies could not recognize Bet v 1 [27]. In keeping with that observation, we report significant associations of IgE-recognizing PR-10 molecules bearing the highest amino acid sequence identities, i.e., Bet v 1, Cor a 1.0101, and Aln g 1 on the one hand, and Mal d 1 and Pru p 1 on the other hand, as was observed on a more limited scale [28].…”

Section: Discussionmentioning

confidence: 99%

Molecular Recognition Profiles and Clinical Patterns of PR-10 Sensitization in a Birch-Free Mediterranean Area

Scala

Abeni

Cecchi³

et al. 2017

Int Arch Allergy Immunol

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Background: The order Fagales represents an important cause of tree-pollen allergy in northern countries. We investigated the IgE recognition profiles, mutual relationships, and association with clinical symptoms of a panel of allergens belonging to the PR-10 family, the main proteins responsible for Fagales allergy (Act d 8, Aln g 1, Api g 1, Ara h 8, Bet v 1, Cor a 1.0101, Cor a 1.0401, Gly m 4, Mal d 1, and Pru p 1). Methods: A total of 526 PR-10-reactive subjects living in central and southern Italy were studied by ImmunoCAP-ISAC-112 microarray analysis. Results: Overall, Bet v 1 reactivity was the most commonly (74%) observed among PR-10 proteins, but Cor a 1.0101 was the most prevalent in participants aged <6 years, and between 15 and 65 years. Overall, 26% of the PR-10-reactive persons were Bet v 1 negative, whilst 93.6% of the PR-10 polyreactive individuals were Bet v 1 positive. Among the 10 PR-10s evaluated, 100 combinations were recorded. The strongest association was observed between molecules with the highest sequence identities (Bet v 1 and Cor a 1.0101, Cor a 1.0401 or Aln g 1; Mal d 1 and Pru p 1). Bet v 1-, Cor a 1.0101-, and Aln g 1-specific IgE recognition was associated with respiratory symptoms, whilst Ara h 8, Cor a 1.0401, Gly m 4, Mal d 1, and Pru p 1 were selectively linked to an oral allergic syndrome. Conclusions: Testing IgE reactivity to a panel of PR-10s in a birch-free area discloses peculiar relationships between clinical phenotypes and sensitization profiles, allowing the identification of novel cluster patterns.

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Section: Discussionmentioning

confidence: 99%

Molecular Recognition Profiles and Clinical Patterns of PR-10 Sensitization in a Birch-Free Mediterranean Area

Scala

Abeni

Cecchi³

et al. 2017

Int Arch Allergy Immunol

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“…In general, Bet v 1 related allergens are characterized as labile proteins, in contrast to other food allergens, which are more stable upon heating and digestion (Bollen et al, 2010). However, it is worth mentioning, that despite this general characteristic, Ara h 8 which is a peanut PR-10 is stable during purification which involves heating up to 70°C (Hurlburt et al, 2013;Petersen et al, 2014).…”

Section: Pathogenesis Related Class 10 (Pr-10) Proteinsmentioning

confidence: 97%

“…Hurlburt et al, demonstrated that Ara h 8.0101 has indeed an overall fold similar to Bet v 1 (Fig. 6) and is able to bind different ligands (Hurlburt et al, 2013). Ara h 8.0201, the second isoform, was discovered relatively late (Riecken et al, 2008) and is not well characterized.…”

Section: Pathogenesis Related Class 10 (Pr-10) Proteinsmentioning

confidence: 99%

“…The function of PR10s however, is not fully understood. It has been suggested that some PR10s may play a role in ribonuclease activity (Moiseyev et al, 1997;Park et al, 2004), while other PR10s may be steroid hormone carriers (Hurlburt et al, 2013;MarkovicHousley et al, 2003). The overall structure of PR10s is highly conserved and generally consists of three α-helices that flank a seven-stranded, anti-parallel β-sheet.…”

Section: Pathogenesis Related Class 10 (Pr-10) Proteinsmentioning

confidence: 99%

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Structural Biology of Peanut Allergens

Offermann¹,

Perdue²,

He³

et al. 2015

JCI

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Peanuts are a cause of one of the most common food allergies. Allergy to peanuts not only affects a significant fraction of the population, but it is relatively often associated with strong reactions in sensitized individuals. Peanut and tree nut allergies, which start in childhood are often persistent and continue through life, as opposed to other food allergies that resolve with age. Therefore, peanut allergens are one of the most intensively studied food allergens. In this review we focus on the structural studies of peanut allergens.

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“…A quarter of the participants who tested negative for Ara h 2 IgE were positive for Bet v 1 IgE. The Bet v 1 IgE-positive participants were older, which could be explained by the fact that birch pollen allergy and pollen food syndrome develop later in life than peanut allergy [40, 41]. Those who tested positive for Bet v 1 IgE were also significantly more likely to be allergic to airborne allergens and they were more likely to be sensitized to Ara h 8 IgE, which further supports the possibility of a birch pollen allergy rather than a peanut allergy.…”

Section: Discussionmentioning

confidence: 99%

Ara h 1 and Ara h 6 Sensitization Causes Clinical Peanut Allergy in Ara h 2-Negative Individuals

Magnusdottir

Vidarsdottir

Lúðvíksson

et al. 2018

Int Arch Allergy Immunol

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Background: Of the major peanut allergens, sensitivity to Ara h 2 has the highest prediction for clinical allergy. In this study, we evaluated sensitization to peanut components in Iceland and related Ara h 2-negative sensitization to clinical allergy. Methods: Ara h 1, Ara h 2, Ara h 3, Ara h 8, and Bet v 1 IgEs were measured (ImmunoCAP) in 220 peanut IgE (Pn-IgE)-positive serum samples. Ara h 2 IgE-negative individuals were invited to an open peanut challenge and evaluated for Ara h 6 and 9 sensitization (ISAC microarray). Results: The Ara h 2 IgE-negative group (52.3%, 115/220) was older (p = 0.04) and more likely to have a history of pollen allergy than the Ara h 2-positive group (p < 0.001). Of the Ara h 2-negative participants, 24.3% were already consuming peanuts and 38.3% were unavailable. Of the 43 who underwent an open peanut challenge, 79% were negative, 14% were positive, and 7% were inconclusive. Those who reacted to peanuts had a higher Ara h 1 IgE than that of the tolerant participants, and 3 were positive to Ara h 6 IgE, and 2 of those subjects were monosensitized. Ara h 8 may have caused a positive reaction, while Ara h 9 did not. Conclusions: Half of the peanut-sensitized individuals in Iceland were not sensitized to the major allergen Ara h 2. Ara h 1, Ara h 3, and Ara h 6 sensitizations resulted in a positive open peanut challenge and they are therefore clinically important for individuals with a peanut allergy in Iceland.

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Structure and Function of the Peanut Panallergen Ara h 8

Cited by 56 publications

References 57 publications

Molecular Recognition Profiles and Clinical Patterns of PR-10 Sensitization in a Birch-Free Mediterranean Area

Molecular Recognition Profiles and Clinical Patterns of PR-10 Sensitization in a Birch-Free Mediterranean Area

Structural Biology of Peanut Allergens

Ara h 1 and Ara h 6 Sensitization Causes Clinical Peanut Allergy in Ara h 2-Negative Individuals

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