Rf352 rAra h 8 PR-10, Peanut

Allergens within Food of Plant Origin

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  • Latin name: Arachis hypogaea
  • Common names: A Bet v 1-homologous allergen, Group 1 Fagales-related protein, PR-10 protein.
  • Source material: An E. coli strain carrying a cloned cDNA encoding Arachis hypogaea allergen Ara h 8.
rAra h 8
rAra h 8 from peanut.
 
Biological function
A plant defence protein, a pathogenesis-related protein belonging to the PR-10 protein family.
 
Mw
Approximately 17 kDa. 
 
Allergen description:
Ara h 8 is a Bet v 1-homologous panallergen. Ara h 8 appears to have a low stability to roasting and no stability to gastric digestion (14). A study was done of 9 Swiss and 11 Dutch patients with Peanut and Birch pollen allergy, and with positive double-blind, placebo-controlled food challenges to Peanut. All patients experienced symptoms of the oral cavity on exposure to Peanut; these progressed to more-severe symptoms in 40% of patients; serum IgE to recombinant Ara h 8 was detected in 85%. The study concluded that Peanut allergy may be mediated in a subgroup of patients by means of cross-reaction of Bet v 1 induced antibodies with the homologous Peanut allergen Ara h 8 (14).
 
Ara h 8 belongs to the PR-10 potein family. It has also been designated a Group 1 Fagales-related potein. Pathogenesis-related (PR) proteins of class 10 are abundant in higher plants. Some of these proteins are induced under stress conditions as part of the plant’s defence mechanism. Other homologues are developmentally regulated, and their expression varies in different plant organs. The PR-10 proteins are encoded by multigene families, have a weight of about 17 kDa and are found in the cytosol (28). They are common panallergens in Fagales pollens (Alder, Hornbeam, Beech, Chestnut) and may be present in a number of vegetables and fruits, e.g., Apple and Hazelnut. Pyr c 1, the major allergen from Pear (Pyrus communis), along with Lupine (Lupinus albus), is a homologous Bet v 1 allergen(29,30). Patients suffering from Birch pollen allergy can also exhibit allergic symptoms on exposure to the pollen of trees from the Fagales (Alder, Hazel, Hornbeam) and Oak and Chestnut, because all contain this panallergen. Recombinant marker allergens are therefore of value for more-accurate diagnoses and subsequent immunotherapy (31).
 
Due to cross-reactivity between Bet v 1 and Ara h 8, sensitisation to other PR-10 proteins might be evaluated to some extent by using rAra h 8. For example, in a study that evaluated whether Fagales sensitisation occurred within a population not exposed to Birch pollen, reactivity to Bet v 1 was recorded in 84% of the Birch/Hazel/Oak co-reactivity group. Bet v 1 prevalence ranged between 48% and 21% among subgroups of patients coming from different areas (32).
 
Lupine is an emerging cause of food allergy, as a result of recent large-scale introduction into processed foods and frequent cross-reactions with other members of the legume family. Significant sequence homology and molecular similarity were found between the allergen Ara h 8 of Peanut and the pathogenesis-related protein PR-10 of White lupine (33).
 
Ara h 8 is also cross-reactive with Gly m 4 from Soya bean and Pru av 1 from Cherry. Nonetheless, although common binding epitopes do occur for this panallergen, patient-specific IgE epitope patterns also occur (29).
 
In a study evaluating severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in Soya bean, Gly m 4/SAM22, immediate-type allergic symptoms in patients with Birch pollen allergy after ingestion of Soy protein-containing food items were reported to occur from cross-reactivity of Bet v 1-specific IgE to homologous pathogenesis-related proteins, particularly the PR-10 protein Gly m 4/SAM22 (34). Similar cross-reactions can also be expected to Ara h 8.

References:

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2006



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