Allergy caused by ingestion of persimmon (Diospyros kaki) : Detection of specific IgE and cross-reactivity to profilin and carbohydrate determinants

Background: Allergy to sharon fruit (persimmon) has been only rarely reported. Cross-reactivity with pollen (profilin and Bet v 6) appeared to be involved, but Bet v 1 has not been implicated previously. Objective: It is our aim to identify whether Bet v 1 sensitization is linked to sharon fruit allergy. Methods: Two patients with a reaction upon first exposure to sharon fruit were included in the study, as well as 7 patients with birch-pollen-related apple allergy. Sensitivity was assessed by skin prick testing (SPT), a radio-allergosorbent test (RAST) and immunoblotting. RAST analysis was performed for Bet v 1, Bet v 2 and Bet v 6. Cross-reactivity was evaluated by RAST and immunoblot inhibitions. Biological activity of IgE was measured by basophil histamine release. Sharon fruit allergy was evaluated by double-blind placebo-controlled food challenge (DBPCFC) or open challenge (OC). Results: Both sharon-fruit-allergic patients demonstrated positive reactions in the RAST (8.6 and 6.2 IU/ml, respectively) and SPT (wheal area 37 and 36 mm²). Sharon fruit allergy was confirmed by DBPCFC in 1 patient. The second patient refused a challenge because of the severe initial reaction. Sera from both patients were reactive to Bet v 1 and Bet v 6, which was cross-reactive with sharon fruit by inhibition assays. The patient with the severest reactions was reactive to profilin on immunoblotting. However, profilin did not induce significant histamine release, nor did Bet v 6. Bet v 1 induce approximately 60% histamine release. An OC with sharon fruit in 7 patients allergic to birch pollen and apple, who had not eaten sharon fruit previously, was positive in 6/7 cases. Conclusions: Birch-pollen-related allergy to sharon fruit is mediated by the known cross-reactive pollen allergens including Bet v 1 and may become more of a problem should sharon fruit consumption increase.

Section: Discussionsupporting

confidence: 82%

“…The study of Anliker et al [4]suggested a role for primary sensitization by grass pollen. They implicated profilin and CCD as the main allergens in sharon fruit.…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Severe Allergy to Sharon Fruit Caused by Birch Pollen

Bolhaar

Ree

et al. 2005

“…Protein extracts of fresh bananas and pineapples were prepared by a low-temperature method as described [16]with the following minor modifications. To improve the extraction of protein from banana acetone powder, we applied a food grade pectinase enzyme mixture (Rohapect ® B5L, Röhm, Darmstadt, Germany) at a dilution of 1:10,000 in PBS.…”

Section: Methodsmentioning

confidence: 99%

IgE Reactivity to Profilin in Pollen-Sensitized Subjects with Adverse Reactions to Banana and Pineapple

Reindl¹,

Rihs²,

Scheurer³

et al. 2002

Background: The so-called ‘latex-fruit syndrome’ is a well-documented phenomenon in cross-reactive allergies. By contrast, there is a lack of information about allergy to exotic fruits in patients with a predominant pollen sensitization. Since the ubiquitous protein profilin has been identified as an allergen in natural rubber latex as well as in pollen-related foods, the aim of this study was to investigate the role of profilin in allergy to certain exotic fruits. Methods: Recombinant profilins from banana and pineapple were cloned by a PCR technique after isolation of total RNA using degenerated profilin-specific primers. The unknown 5′ ends of copy DNA (cDNA) were identified by rapid amplification of 5′cDNA ends (5′-RACE) and expression in Escherichia coli BL21(DE3) cells. The recombinant profilins were purified by affinity chromatography using poly-(L)-proline as the solid phase. IgE-binding capabilities were characterized by means of immunoblot and Enzyme Allergosorbent Test (EAST). The cross-reactivity to birch pollen profilin and latex profilin was studied by EAST as well as by immunoblot inhibition experiments. Results: Both banana and pineapple profilin were found to consist of 131 amino acid residues with high amino acid sequence identity to known allergenic pollen and food profilins (71–84%). IgE binding to the recombinant profilins was observed in 7/16 sera from subjects with suspected banana allergy (44%) and in 8/19 sera from subjects with suspected pineapple allergy (42%). Inhibition experiments indicated similar IgE reactivity of natural and recombinant allergens. In addition, high cross-reactivity to birch pollen profilin Bet v 2 and latex profilin Hev b 8 was demonstrated by immunoblot inhibition as well as EAST inhibition experiments. Conclusions: Since a high IgE-binding prevalence of about 40% was obtained in both banana and pineapple allergy, we conclude that profilin is an important mediator of IgE cross-reactivity between pollen and exotic fruits.

“…In one study, the few patients monosensitized to profilin did not report any relevant symptom following the ingestion of plant-derived foods [41], and another one concluded that IgE cross-reactive against food profilins has no or very little clinical relevance [43]; on the other hand, profilin has been involved in the so-called ‘birch-mugwort-celery-spice’ syndrome and in adverse reactions to Apiaceae [44,45,46,47], hazelnut [11], Rosaceae [14, 48], tomato [49], pumpkin seed [50], zucchini [51], lychee [52], pineapple and banana [53], persimmon [54] and melon [55]. Altogether, these studies suggest that probably only a limited proportion of subjects sensitized to profilin develop clinical allergy.…”

Section: Allergy To Profilinmentioning

confidence: 99%

Plant Food Allergies: A Suggested Approach to Allergen-Resolved Diagnosis in the Clinical Practice by Identifying Easily Available Sensitization Markers

Asero¹

2005

Background: Molecular biology techniques have led to the identification of a number of allergens in vegetable foods, but due to the lack of purified food proteins for routine diagnostic use, the detection of sensitizing allergens remains a nearly impossible task in most clinical settings. The allergen-resolved diagnosis of food allergy is essential because each plant-derived food may contain a number of different allergens showing different physical/chemical characteristics that strongly influence the clinical expression of allergy; moreover, many allergens may cross-react with homologue proteins present in botanically unrelated vegetable foods. Objective: Through a review of the available literature, this study aimed to detect ‘markers’ of sensitization to specific plant food allergens that are easily accessible in the clinical practice. Results: There are several ‘markers’ of sensitization to different allergenic proteins in vegetable foods that can be helpful in the clinical practice. Specific algorithms for patients allergic to Rosaceae and to tree nuts were built. Conclusion: Clinical allergologists lacking the assistance of an advanced molecular biology lab may take advantage of some specific clinical data as well as of some ‘markers’ in the difficult task of correctly diagnosing patients with plant food allergy and to provide them the best preventive advice.