Cyclophilin – A novel cross‐reactive determinant in peanut

Mattsson, Lars; Valcour, André; Holmqvist, Marie; Larsson, Håkan; Lidholm, Jonas

doi:10.1111/cea.13833

Cited by 20 publications

(11 citation statements)

References 13 publications

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“…Another cyclophilin, Ara h 18, was recently detected in peanut. In patients with grass pollen allergy, it was responsible for serological cross-reactions that could not be explained with other peanut allergens identified so far (e.g., CCD or profilins) [ 6 ]. Due to their thermal and acid instability, profilins (and probably also cyclophilins) mostly only cause allergic symptoms when raw plant products are ingested, and symptoms are limited to the mouth and throat.…”

Section: Discussionmentioning

confidence: 99%

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Molecular allergy diagnosis using pollen marker allergens and pollen panallergens: Five patterns seen in multiple test reactions to pollen extracts

Kleine‐Tebbe¹,

Ackermann-Simon²,

Hanf³

2021

ALS

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Polysensitizations to tree, grass, and weed pollen are found in ~ 20% of pollen-allergic individuals. They are often based on broad IgE cross-reactivities to pollen panallergens belonging to highly conserved protein families: 1. profilins, 2. polcalcins (calcium-binding proteins in pollen), 3. cyclophilins. They represent highly conserved cross-reactive minor allergens present in all pollen species, but also in plant foods and other organisms. Despite being rarely clinically relevant they can hamper allergy diagnostic tests with extracts. In this situation, molecular allergy diagnosis is able to distinguish broad cross-reactivity due to allergen-specific IgE to pollen panallergens (i.e. profilins Bet v 2 or Phl p 12; polcalcins Bet v 4 or Phl p 7; and, in the future, cyclophilins Bet v 7 or Ole e 15) from primary IgE sensitizations to so-called marker allergens represented by important pollen major allergens: Bet v 1 for the birch and beech family ( Fagales ), Ole e 1 for olive and ash ( Oleaceae ), Phl p 1 for temperate climate grasses ( Poaceae ), Art v 1 for mugwort ( Artemisia ), Amb a 1 for Ambrosia species ( Ambrosia ). Five typical cases (A – E) with positive skin prick test results to tree, grass, and weed pollen extracts demonstrate typical patterns of IgE sensitization with a variable impact of pollen panallergens: A – profilins, B – polcalcins, C – profilins and polcalcins, D – presumably cyclophilins, E – primary polysensitization to tree, grass, and weed pollen without interference from profilins or polcalcins. Differences between pollen extract-based skin prick test diagnosis and molecular allergen-specific IgE testing are explained using the presented concept. This approach allows to reduce the number of allergen extracts – presuming they are also clinically relevant – for allergen immunotherapy (i.e., only tree and/or grass pollen extracts), particularly in pollen-polysensitized patients.

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Section: Discussionmentioning

confidence: 99%

“…Cyclophilins, in pollen [ 5 ] and plant-based foods [ 6 ], but also in other organisms [ 5 , 7 ]. The frequency of IgE sensitization to cyclophilins among pollen-allergic patients is unclear.…”

Section: Introductionmentioning

confidence: 99%

Molecular allergy diagnosis using pollen marker allergens and pollen panallergens: Five patterns seen in multiple test reactions to pollen extracts

Kleine‐Tebbe¹,

Ackermann-Simon²,

Hanf³

2021

ALS

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“…Ara h 18 is an approximately 21‐kDa protein that is a novel cross‐reactive determinant in peanut (Mattsson et al., 2021).…”

Section: Basic Structure Of Peanut Allergensmentioning

confidence: 99%

Allergenicity of peanut allergens and its dependence on the structure

Geng

Zhang

Song

et al. 2023

Comp Rev Food Sci Food Safe

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Food allergies are a global food safety problem. Peanut allergies are common due, in part, to their popular utilization in the food industry. Peanut allergy is typically an immunoglobulin E-mediated reaction, and peanuts contain 17 allergens belonging to different families in peanut. In this review, we first introduce the mechanisms and management of peanut allergy, followed by the basic structures of associated allergens. Subsequently, we summarize methods of epitope localization for peanut allergens. These methods can be instrumental in speeding up the discovery of allergenicity-dependent structures. Many attempts have been made to decrease the allergenicity of peanuts. The structures of hypoallergens, which are manufactured during processing, were analyzed to strengthen the desensitization process and allergen immunotherapy. The identification of conformational epitopes is the bottleneck in both peanut and food allergies. Further, the identification and modification of such epitopes will lead to improved strategies for managing and preventing peanut allergy. Combining traditional wet chemistry research with structure simulation studies will help in the epitopes' localization.

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“…The most abundant allergens of peanut seed are the 2S albumins (Ara h 2 and 6) and the cupins (Ara h 1 and 3) ( 1 ), where Ara h 2 has been regarded as the most important effector cell responses and diagnosis of peanut allergy ( 6 ). Less abundant allergens of the peanut seed include the profilin (Ara h 5), a 2S albumin (Ara h 7), the non-specific lipid-transfer proteins (nsLTP) (Ara h 9, 16, and 17), the defensins (Ara h 12 and 13), the Bet v 1-type protein (Ara h 8), the oleosins (Ara h 10, 11, 14, and 15) ( 1 ), and cyclophilin (Ara h 18) ( 7 ). Post-translational modifications may also play a significant role in allergenicity, as Bernard et al evaluated that hydroxyprolination (HyP) of Ara h 2 was shown to be important in the elicitation of an immune response ( 8 ).…”

Section: Introductionmentioning

confidence: 99%

Determination of Allergen Levels, Isoforms, and Their Hydroxyproline Modifications Among Peanut Genotypes by Mass Spectrometry

Marsh¹,

Palmer²,

Koppelman³

et al. 2022

Front. Allergy

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The recently published reference genome of peanuts enables a detailed molecular description of the allergenic proteins of the seed. We used LC-MS/MS to investigate peanuts of different genotypes to assess variability and to better describe naturally occurring allergens and isoforms. Using relative quantification by mass spectrometry, minor variation of some allergenic proteins was observed, but total levels of Ara h 1, 2, 3, and 6 were relatively consistent among 20 genotypes. Previously published RP-HPLC methodology was used for comparison. The abundance of three Ara h 3 isoforms were variable among the genotypes and contributed to a large proportion of total Ara h 3 where present. Previously unpublished hydroxyproline sites were identified in Ara h 1 and 3. Hydroxylation did not vary significantly where sites were present. Peanut allergen composition was largely stable, with only some isoforms displaying differences between genotypes. The resulting differences in allergenicity are of unknown clinical significance but are likely to be minor. The data presented herein allow for the design of targeted MS methodology to allow the quantitation and therefore control of peanut allergens of clinical relevance and observed variability.

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Cyclophilin – A novel cross‐reactive determinant in peanut

Cited by 20 publications

References 13 publications

Molecular allergy diagnosis using pollen marker allergens and pollen panallergens: Five patterns seen in multiple test reactions to pollen extracts

Molecular allergy diagnosis using pollen marker allergens and pollen panallergens: Five patterns seen in multiple test reactions to pollen extracts

Allergenicity of peanut allergens and its dependence on the structure

Determination of Allergen Levels, Isoforms, and Their Hydroxyproline Modifications Among Peanut Genotypes by Mass Spectrometry

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