Cross-Reacting Allergens in Tree Pollen and Pollen-Related Food Allergy: Implications for Diagnosis of Specific IgE

Scheiner, Otto; Aberer, Werner; Ebner, Christof; Ferreira, Fatima; Hoffmann‐Sommergruber, Karin; Hsieh, Li-Shan; Kraft, Dietrich; Sowka, Slawomir; Vanek-Krebitz, M; Breiteneder, Heimo

doi:10.1159/000237519

Cited by 24 publications

(17 citation statements)

References 14 publications

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“…Recombinant allergens were used to sensitize animals in order to examine the activity eliciting the production of antigen-specific IgE antibodies [23,24]. In humans, immunotherapy by T-cell-reactive peptides derived from a cat allergen, Fel d I [25], and diagnosis of hypersensitivity using recombinant allergens, Phl p 1 in timothy grass pollen and Bet v 1 in birch pollen, have been reported [26,27]. Among the major house-dust mite allergens, genes for Der f 1, 2, 3 found in D. farinae, and Der p 1, 2, 3, 5 in Dermatophagoides pteronyssinus have been cloned [28][29][30][31].…”

Section: Discussionmentioning

confidence: 99%

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Yasue

Yokota²,

Yuasa³

et al. 1998

Eur Respir J

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Recombinant Der f2 (rDer f2) has recently been developed as a promising allergen for the diagnosis and immunotherapy of house-dust mite allergy, and studies in immunology. The aim of the present study was to evaluate whether oral administration of rDer f2 could suppress an immediate allergic reaction in mice sensitized with mite allergen. We developed a murine allergic model that showed bronchoconstriction after inhalation of rDer f2, and studied the effect of oral administration of rDer f2 on the reaction.Seven week old male A/J mice were intranasally immunized with rDer f2 12 times. Sensitized mice showed anti-rDer f2 immunoglobulin (Ig)E production and immediate airway constriction after inhalation of 10 mg·mL -1 of rDer f2, as determined by the Konzett-Rössler method. Immunized animals were divided into three groups, and fed phosphate-buffered saline (PBS), 0.1 mg·day -1 , or 1 mg·day -1 of rDer f2 for 4 weeks, respectively. Seven days after the last feeding, the mice were examined for their immediate response.Animals fed with 1 mg·day -1 rDer f2 showed significantly reduced bronchoconstriction after inhalation of both 2 mg·mL -1 and 10 mg·mL -1 of rDer f2 compared with PBS-fed mice. Similar results were obtained when we examined mice 10 weeks after the last feeding. Reactions in the 0.1 mg·day -1 rDer f2-fed group also tended to decrease in comparison with PBS-fed animals. Plasma anti-rDer f2 IgE, IgG1, IgG2a, and IgG2b levels were not changed by feeding with rDer f2.We conclude that recombinant Der f2 exhibits both sensitizing and hyposensitizing activities in mice. rDer f2 may be useful in immunotherapy and diagnosis of housedust mite allergy. Eur Respir J 1998; 11: 144-150 To date, several clinically important allergens such as Der 1 and Der 2 have been identified in crude mite extract [1][2][3][4]. Among others, the structural gene of Der f2, one of the major mite allergens found in Dermatophagoides farinae was cloned, and the product (recombinant Der f2 (rDer f2)) shown to exhibit allergic activity in humans comparable with native Der f2 prepared from crude mite extract [5,6]. Since Der f2 has been shown to sensitize over 80% of patients with house-dust mite allergy, rDer f2 should prove useful in the diagnosis and immunotherapy of allergic asthma and rhinitis caused by house-dust mites. It should also provide a basis for research into allergies and immunology.In the present study, with special reference to the therapeutic application of rDer f2, we established a murine allergic model by intranasal or intraperitoneal injection of rDer f2 to A/J mice, which are highly responsive to Der f2 [7]. We examined the effect of oral-hyposensitization therapy with rDer f2 against the immediate bronchoconstriction in the intranasally sensitized animals because their reaction after rDer f2 inhalation was more intense than that of intraperitoneally immunized mice. Materials and methodsAntigen rDer f2, clone 1 [5], was kindly supplied by the Nikka Whisky Distilling Co., Ltd. (Chiba, Japan), and dissolved in...

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Section: Discussionmentioning

confidence: 99%

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Yasue

Yokota²,

Yuasa³

et al. 1998

Eur Respir J

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“…This is particularly the case of asthma attacks occurring during thunderstorms (401)(402)(403)(404)(405). Cross-reactivities between pollens are now better understood using molecular biology techniques (406)(407)(408)(409). However, it is unclear as to whether all in vitro cross-reactivities observed between pollens are clinically relevant (410).…”

Section: Other Mitesmentioning

confidence: 99%

Allergic Rhinitis and its Impact on Asthma (ARIA) 2008*

Bousquet¹,

Khaltaev²,

Cruz³

et al. 2008

Allergy

3,754

1,761

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“…Sensitization to profilin was observed in about 20% of patients allergic to birch pollen in different studies as assessed by IgE immunoblot [19], IgE immuno-adsorption [22], skin prick testing (SPT) [23] or ImmunoCAP [24] with rBet v 2. Of note, different profiles of sensitization to rBet v 2 have been described in diverse geographical locations [25], with 5–7% of birch pollen-allergic patients from Scandinavian centers recognizing rBet v 2 as opposed to 20–38% of birch pollen-allergic patients from Central and Southern European centers.…”

Section: Profilin: Prevalence Of Sensitizationmentioning

confidence: 99%

Profilins: Mimickers of Allergy or Relevant Allergens?

Santos

Ree

2011

Int Arch Allergy Immunol

139

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Profilins are ubiquitous proteins, present in all eukaryotic cells and identified as allergens in pollen, latex and plant foods. The highly conserved structure justifies the cross-reactive nature of IgE antibodies against plant profilins and their designation as pan-allergens. Primary sensitization to profilin seems to arise from pollen sensitization with later development of cross-reactive IgE antibodies against plant food (and possibly latex) profilins. The role of profilin in inducing allergic symptoms needs to be evaluated and raises important issues in allergy diagnosis due to cross-reactivity. IgE cross-reactivity among profilins is associated with multiple pollen sensitization and with various pollen-food syndromes. In respiratory allergy, sensitization to pollen to which the patient has virtually no environmental exposure has been identified as a manifestation of profilin sensitization. As a food allergen, profilin usually elicits mild reactions, such as oral allergy syndrome, is not modified by processing and is especially important in allergy to some fruits, such as melon, watermelon, banana, tomato, citrus fruit and persimmon. Purified natural and recombinant profilins for in vitro and in vivo allergy tests are helpful in the diagnostic work-up. Herein we review the current state of knowledge about the allergen profilin and its implications in the diagnosis and treatment of allergic diseases. We conclude that, although its role in triggering allergic symptoms is still controversial, profilin is undoubtedly a relevant allergen. As a pan-allergen, profilin is associated with multiple pollen sensitization and pollen-food-latex syndromes that the allergist has to be aware of in order to accomplish an accurate diagnosis and successful treatment of allergic diseases.

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Cross-Reacting Allergens in Tree Pollen and Pollen-Related Food Allergy: Implications for Diagnosis of Specific IgE

Cited by 24 publications

References 14 publications

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Effects of oral hyposensitization with recombinant Der f2 on immediate airway constriction in a murine allergic model

Allergic Rhinitis and its Impact on Asthma (ARIA) 2008*

Profilins: Mimickers of Allergy or Relevant Allergens?

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