Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens

BACKGROUND: Food IgE-mediated allergy to members of the Brassicaceae family has been increasingly reported. OBJECTIVE: To characterize cabbage-Brassica oleracea var capitata-allergy and its major allergens. METHODS: A prospective study was performed, recruiting 17 patients allergic to cabbage, and control subjects. Skin prick tests and double-blind placebo-controlled food challenges were performed. A major allergen was isolated from cabbage by RP-HPLC and characterized by N-terminal amino acid sequencing and matrix-assisted laser desorption/ionization mass spectrometry analysis. Specific IgE determinations, IgE immunoblots, and CAP-inhibition assays were also performed. RESULTS: Skin prick test and specific IgE were positive to cabbage in all patients. Five of them referred anaphylactic reactions when eating cabbage, and in another 5 patients, cabbage allergy was further confirmed by double-blind placebo-controlled food challenge. Most of them showed associated sensitizations to mugwort pollen, mustard, and peach. A 9-kd cabbage IgE-binding protein, Bra o 3, was identified as a lipid transfer protein (LTP) with 50% of identity to peach LTP Pru p 3. Skin prick test with Bra o 3 showed positive results in 12 of 14 cases (86%). On CAP inhibition assays, Bra o 3 managed to inhibit significantly the IgE binding to cabbage, mugwort pollen, and peach. Both Bra o 3 and Pru p 3 were recognized by IgE from the patients' sera. CONCLUSION: Bra o 3, a cabbage LTP, is a major allergen in this food, cross-reacting with mugwort pollen and with other plant foods, such as peach. CLINICAL IMPLICATIONS: Cabbage IgE-mediated allergy is a potentially severe condition that can present with other plant food and pollen allergies.     

Two different profiles of peach allergy in the north of Spain

BACKGROUND: Peach allergy has two different patterns: central Europe with oral allergy syndrome (OAS) related to a primary sensitization to birch pollen Bet v 1 and profilins and southern Europe with mostly systemic symptoms, in many cases due to sensitization to lipid-transfer proteins. METHODS: Thirty peach-allergic patients with positive skin and food challenge tests and 29 control subjects were included. Skin prick tests (SPT) with inhalant allergens, commercial peach and apple extracts and native Pru p 3 were performed. In vitro specific immunoglobulin (Ig) E to grass pollen, birch pollen, peach, apple, rBet v 1, rBet v 2 and rPhl p 12 was determined by CAP, and rBet v 1, rMal d 1, rMal d 4, rMal d 3 and rPru p 3 using the ADVIA-Centaur platform. Basophil activation test (BAT) with commercial peach extract, commercial apple extract, nPru p 3, rMal d 3, rMal d 1 and rMal d 4 was also performed. RESULTS: Pru p 3 was the major allergen in the patient group from northern Spain. Sensitization to this allergen was found in 100% of the patients with systemic symptoms or contact urticaria. Only 60% of OAS patients were sensitized to Pru p 3, being all of them sensitized to profilins and 60% of them to allergens of the Bet v 1 family. Specific IgE determination and BAT using recombinant allergens (rPru p 3) show specificity and sensitivity values close to 100%. CONCLUSIONS: Most peach-allergic patients coming from the north of Spain present systemic symptoms after ingestion of peach, Pru p 3 being the main allergen. Patients with OAS present profilin-Bet v 1-related sensitization. Thus, in the north of Spain our patients show a mixed central-south Europe pattern with LTP-profilin-Bet v 1 sensitization depending on the symptoms presented. The use of natural and recombinant plant allergens, allows establishing the sensitization patterns to the different allergens studied.     

Occupational rhinoconjunctivitis and food allergy because of aniseed sensitization.

BACKGROUND: Aniseed is a spice frequently used in Mediterranean cooking and, as with other Umbelliferae, it has been involved in clinical allergy. OBJECTIVE: This investigation was undertaken to study the allergens implicated in a case of occupational allergy to aniseed associated with rhinoconjunctivitis and gastrointestinal symptoms. METHODS: Skin prick tests were performed to inhalant allergens, spices used in the patient's workplace (aniseed and cinnamon), and 12 other Umbelliferae spices, birch, and mugwort. A nasal challenge test to aniseed and cinnamon and a double-blind placebo-controlled oral food challenge test to aniseed were also performed. The molecular weights of the allergens were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting and cross-reactivity among Umbelliferae species by enzyme immunoassay inhibition. RESULTS: Skin prick tests showed a positive immediate response to aniseed, asparagus, caraway, coriander, cumin, dill, and fennel extracts, and an intense late response to aniseed. Skin prick tests to celery, carrot, birch pollen, and mugwort pollen extracts were negative. Results of a nasal challenge test were positive to aniseed and negative to cinnamon; an aniseed oral food challenge test yielded a positive response. The molecular weights of the main immunoglobulin (Ig)E-binding proteins in aniseed extracts were approximately 48, 42, 39, 37, 34, 33, and 20 kD. Caraway, fennel, cumin, and coriander extracts showed similar IgE-binding patterns. Enzyme immunoassay inhibition studies with the patient's serum revealed cross-reactivity among the IgE components from aniseed, caraway, coriander, fennel, and dill extracts. CONCLUSIONS: We demonstrate the presence of aniseed allergens in a case of occupational rhinoconjunctivitis and food allergy, with molecular weights for this spice that differed from those previously reported.     

Carrot allergy: double-blinded, placebo-controlled food challenge and identification of allergens

BACKGROUND: Allergic reactions to carrot affect up to 25% of food-allergic subjects. Clinical manifestations of carrot allergy and IgE responses to carrot proteins, however, have never been studied in subjects with carrot allergy confirmed by means of double-blinded, placebo-controlled food challenge (DBPCFC). OBJECTIVE: The purposes of this investigation were to confirm clinically relevant sensitizations to carrot by means of DBPCFC, to validate current diagnostic methods, and to identify IgE-reactive carrot proteins in patients with true allergy. METHODS: DBPCFCs were performed in 26 subjects with histories of allergic reactions to carrot. Patients underwent skin prick tests with carrot extract, fresh carrot, and various pollen extracts. Specific IgE to carrot, celery, birch, and mugwort pollen and to rBet v 1, rBet v 2, and rBet v 6 were measured through use of the CAP method. Carrot allergens were identified by means of immunoblotting and blotting inhibition. RESULTS: Twenty of 26 patients had positive DBPCFC results. The sensitivity of the determination of carrot-specific IgE antibodies through use of the CAP method (> or =0.7 kU/L) was 90%, the sensitivity for skin prick testing with commercial extracts was 26%, and the sensitivity for prick-to-prick tests with raw carrot was 100%. The Bet v 1--related major carrot allergen Dau c 1 was recognized by IgE from 85% of patients; 45% were sensitized to cross-reactive carbohydrate determinants and 20% to carrot profilin. In 1 subject, a Bet v 6--related carrot allergen was recognized. In 4 patients, IgE binding to Dau c 1 was not inhibited or was weakly inhibited by rBet v 1 or birch pollen extract. CONCLUSION: This study confirmed the allergenicity of carrot by means of DBPCFC. DBPCFC-positive patients had exclusively specific IgE antibodies to birch pollen--related carrot allergens, Dau c 1 being the major allergen. The lack of inhibition of IgE binding to Dau c 1 by birch allergens in a subgroup of patients might indicate an secondary immune response to new epitopes on the food allergen that are not cross-reactive with Bet v 1.     

IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance

BACKGROUND: Individuals with pollen allergy often have IgE against plant-derived foods. This can be due to cross-reactive IgE against Bet v 1 and homologues, profilins, and/or cross-reactive carbohydrate determinants. OBJECTIVE: The aim of this study was to correlate sensitization to Bet v 1 and profilin with individual recognition patterns to plant foods and clinical relevance. METHODS: Fifty-two patients with pollen allergy and IgE against at least one plant-derived food were included in the study. Adverse reactions to plant-derived foods were documented by using standardized interviews. Skin prick tests were performed for pollen (grass, birch, and mugwort) and 14 plant-derived foods. In addition, recombinant (r) Bet v 1 and rBet v 2 (profilin) were tested intracutaneously. Specific IgE against the abovementioned allergens were determined by means of RAST. Cross-reactivity was studied by means of RAST inhibition. RESULTS: Eighty-five percent of patients were sensitized to Bet v 1, and 71% were sensitized to profilin. Profilin was associated with a higher number of positive RAST results to plant-derived foods than Bet v 1. In contrast, Bet v 1 was associated with more positive skin prick test responses and more food-related symptoms. Sensitization to Bet v 1 was associated with IgE against apple, hazelnut, and peach, whereas sensitization to profilin was associated with positive RAST results to all investigated plant-derived foods except apple, peach, and melon. CONCLUSIONS: IgE antibodies against Bet v 1 have a more limited spectrum of cross-reactivity than those against profilin, but they frequently give rise to clinically relevant cross-reactivities to food. In analogy to anticarbohydrate IgE, cross-reactive IgE against food profilins have no or very limited clinical relevance.     

Skin test diagnosis of grass pollen allergy with a recombinant hybrid molecule

BACKGROUND: A recombinant hybrid molecule (HM) consisting of 4 major allergens from timothy grass (Phl p 1, 2, 5, and 6) was expressed in Escherichia coli, purified, and characterized regarding its immunologic properties. OBJECTIVE: We sought to determine whether the recombinant HM can be used for the diagnosis of grass pollen allergy by means of skin testing. METHODS: Skin prick testing was performed in 32 patients with grass pollen allergy and in 9 control individuals by using increasing concentrations (4, 12, 36, and 108 mug/mL) of the HM and using commercial grass pollen extract. Specific IgE reactivities against the HM, grass pollen extract, and a panel of purified grass pollen allergens (recombinant Phl p 1, 2, 5, 6, 7, 12, and 13 and natural Phl p 4) were measured by means of ELISA, and timothy grass pollen-specific IgE levels were determined by using ImmunoCAP. RESULTS: Grass pollen allergy was diagnosed in all patients by means of skin testing with the HM. No false-positive skin test responses were obtained in the control individuals. There was an excellent correlation between IgE levels obtained with the HM and natural grass pollen extract measured by means of ELISA (r = 0.98, P < .0001) and by means of ImmunoCAP (r = 0.98, P < .0001). CONCLUSIONS: The recombinant HM permitted accurate and specific in vivo diagnosis of grass pollen allergy in all tested patients. It can be considered a well-defined tool for the diagnosis and perhaps for immunotherapy of grass pollen allergy. CLINICAL IMPLICATIONS: A recombinant HM can replace traditional allergen extracts for skin test-based diagnosis of grass pollen allergy.     

Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome

BACKGROUND: Chestnut allergy has been almost exclusively considered in the context of the latex-fruit syndrome. Chestnut allergens not linked to latex hypersensitivity have not been studied. OBJECTIVE: We sought to explore whether differences in sensitization patterns between chestnut allergy with or without associated latex-fruit syndrome can be detected. METHODS: Twelve patients sensitized to chestnut but not to latex and 3 control patients with latex-chestnut allergy were analyzed. A major chestnut allergen was purified and characterized. IgE immunoblotting, specific IgE determination, and skin prick tests with 5 isolated allergens involved in food allergy or latex-fruit syndrome were also performed. RESULTS: A major 9-kd allergen was detected in chestnut extract, isolated, and identified as lipid transfer protein (LTP) Cas s 8. Specific IgE to this allergen was found in 91% (by means of IgE immunoblotting) and 58% (by means of ELISA) of sera from patients with chestnut but not latex allergy. Moreover, 66% of these patients had positive skin prick test responses to Cas s 8. Additionally, allergenic LTPs from peach fruit and Artemisia vulgaris pollen were also reactive. In contrast, avocado class I chitinase and latex hevein, allergens associated with the latex-fruit syndrome, showed no reaction. The opposite situation was exhibited by patients with latex-chestnut allergy. CONCLUSIONS: Patients with chestnut allergy with or without associated latex hypersensitivity present different patterns of major allergens (LTPs and class I chitinases, respectively). CLINICAL IMPLICATIONS: LTPs and class I chitinases can be used as diagnostic tools in patients with chestnut allergy to predict whether an associated latex sensitization and a risk of potential cross-reactivity with other plant foods and pollens exist.     

Detection and clinical characterization of patients with oral allergy syndrome caused by stable allergens in Rosaceae and nuts.

BACKGROUND: A minority of patients with oral allergy syndrome (OAS) induced by Rosaceae or nuts are positive on skin prick tests with commercial food extracts. This suggests reactivity against distinct stable allergens. OBJECTIVES: (1) To define the prevalence of subjects positive on skin prick tests with commercial extracts among patients with OAS caused by Rosaceae and/or nuts and (2) To investigate whether commercial extracts-positive subjects show some peculiar clinical feature and may represent a specific subset with food allergy. METHODS: Skin prick tests were carried out with a large panel of commercial extracts of airborne allergens (Allergopharma) and of vegetable foods (Dome/Hollister-Stier) in 298 adults with OAS caused by Rosaceae (n = 237) and or nuts (n = 161), positive on skin prick tests with fresh offending foods. RESULTS: 25/237 (11%) patients were positive on prick tests with commercial plum extract. This subgroup showed a higher incidence of systemic symptoms (64% versus 6%; P < .001) and a lower incidence of birch pollen allergy (12% versus 99%; P < .001) than commercial extract-negative patients; moreover, 36% versus 0%, respectively, did not have respiratory allergy (P < .001). Apple and peach were the main offending foods among commercial extract-negative and commercial extract-positive patients, respectively (87% versus 44% for apple, P < .001; and 52% versus 88% for peach, P < .005). Eight of one hundred sixty-one (5%) nuts-sensitive patients were positive on prick test with commercial walnut extract. This subgroup showed a higher proportion of patients who experienced systemic symptoms (63% versus 6%, P < .001), a lower prevalence of birch pollen allergy (13% versus 97%, P < .001), and a higher prevalence of grass pollen allergy (88% versus 41%, P < .05) than commercial extract-negative subjects. Further, reactivity against commercial walnut extract was associated with skin reactivity against commercial extracts of peanut (88% versus 37%, P < .005), tomato (75% versus 5%, P < .001), and plum (63% versus 8%, P < .001), and inversely related with skin reactivity against fresh apple (P < .001). In most cases, high levels of IgE specific for peach, apple, and hazelnut were associated with peanut reactivity rather than with clinical sensitivity to specific foods. In a preliminary investigation, most commercial extract-positive patients reacted against a 10-kDa protein characterized as a lipid transfer protein (LTP). CONCLUSIONS: Skin prick tests with commercial extracts of plum and walnut may be usefully employed to detect patients with OAS reacting against stable allergens. The high prevalence of systemic symptoms in these patients suggests that allergens' stability is associated with a higher resistance to the gastrointestinal environment and strongly influences the clinical expression of vegetable food allergy. At least some stable allergens, namely lipid transfer protein might be shared by botanically unrelated fruits such as nuts, peanuts, legumes, tomato, and Prunoideae.     

Platanus acerifolia pollinosis and food allergy

BACKGROUND: In Mediterranean areas, oral allergy syndrome (OAS) occurs independently of an associated birch pollinosis; moreover, on occasions it presents with no other associated pollinosis. The aim of this study was to assess the possible association of OAS with Platanus acerifolia pollinosis. METHODS: We evaluated consecutive patients seen for pollinosis in an allergy department. Seven hundred and twenty patients were selected on the basis of seasonal or perennial rhinitis, or asthma, or both. Respiratory and food allergies were studied in all patients. Clinical history was recorded and examinations and skin prick tests were performed with a battery of available common inhalant allergens and plant-derived food allergens. Specific IgE levels to P. acerifolia pollen extract and food allergens tested were measured. Molecular masses of the IgE-binding proteins and cross-reactivity among the P. acerifolia pollen and different food extracts were also determined. RESULTS: Of the 720 patients evaluated, 61 (8.48%) were sensitized to P. acerifolia pollen. Food allergy was observed in 32 (52.45%) of the 61 patients sensitized to P. acerifolia pollen. Food allergens most frequently implicated were hazelnuts, peach, apple, peanuts, maize, chickpea and lettuce. Enzyme allergosorbent (EAST)-inhibition showed high inhibition values when P. acerifolia pollen extract was used as free phase. On the contrary low inhibition was observed when plant-derived food allergens were used as free phase and P. acerifolia pollen extract as solid phase. CONCLUSIONS: Cross-reactivity was observed among P. acerifolia pollen and plant-derived foods. OAS in these patients may have been caused by primary respiratory sensitization.     

Oral allergy syndrome to jackfruit (Artocarpus integrifolia)

A 30-year-old man from the Philippines with pollen allergy noted the appearance of oral allergy syndrome (OAS) after eating raw apple, raw peach, raw celery, and, recently, jackfruit ( Artocarpus integrifolia ), a tropical fruit which belongs to the Moraceae family (mulberry) and to the genus Artocarpus (breadfruit tree). Despite the patient's multiple sensitization in skin prick tests and in the Pharmacia CAP System to birch, grass, mugwort pollen, related fruits and vegetables, and jackfruit, in RAST-inhibition studies neither rBet v 1 nor rBet v 2 (profilin), the well-known cross-reacting allergenic components in OAS, could inhibit the specific IgE response to jackfruit. Whether the reaction to jackfruit is specific or whether other pollen-related, cross-reacting allergenic components exist should be investigated further.     

Primary sensitization to sweet bell pepper pollen in greenhouse workers with occupational allergy

BACKGROUND: In a previous investigation, a high prevalence of allergy to sweet bell pepper pollen was found among exposed horticulture workers. Allergy to plant-derived food is often the consequence of primary sensitization to common pollen allergens. OBJECTIVE: We therefore investigated the cross-reactivity between sweet bell pepper pollen and pollen from grass, birch or mugwort. METHOD: We selected 10 sera from greenhouse workers who had, besides specific IgE against sweet bell pepper pollen, also IgE to grass, birch or mugwort pollen. Cross-reactivity was tested by the inhibition of IgE binding to solid-phase coupled sweet bell pepper pollen extract. The 10 sera were also analysed for IgE binding to sweet bell pepper pollen by immunoblotting. RESULTS: With these sera, no or small inhibition of IgE binding to sweet bell pepper pollen extract was observed with grass, birch and mugwort pollen. With immunoblotting, major IgE-binding structures were seen at 14, 29 and 69 kDa in sweet bell pepper pollen extract. CONCLUSION: The results of our study demonstrate that sweet bell pepper pollen contains allergens that have no or limited cross-reactivity with common pollen allergens. With sera from the 10 patients tested, sensitization to sweet bell pepper pollen was not the consequence of primary sensitization to common pollen allergens.     

Tobacco allergy: demonstration of cross-reactivity with other members of Solanaceae family and mugwort pollen.

BACKGROUND: Tobacco is a plant belonging to the Solanaceae family. This plant is usually used as a contact insecticide for several infestations in some areas, such as the Canary Islands. Allergy induced by inhalation of this plant is unusual. Identification of the potential allergen in growing areas is essential. OBJECTIVE: We report a patient with occupational sensitivity to an aqueous solution of cut tobacco whose clinical manifestations were rhinoconjunctivitis and urticaria. Past medical history was significant for seasonal allergic rhinoconjunctivitis to mugwort pollen and oral allergy syndrome with avocado. METHODS: Green tobacco and cured tobacco leaf extracts were prepared, skin prick tests were performed with green tobacco, cured tobacco leaf extracts, and certain aeroallergens. Conjunctival challenge test was carried out with green tobacco and cured tobacco leaf extract. Serum-specific IgE against tobacco leaf was performed by commercial CAP. CAP inhibition experiments were carried out with tobacco and Artemisia vulgaris. RESULTS: Skin prick tests and conjunctival challenge tests with green tobacco and cured tobacco leaf extracts were positive, as well as serum-specific IgE by CAP, indicating an IgE-mediated sensitization. CAP inhibition experiments were carried out and it was found that tobacco, mugwort pollen, and tomato extracts inhibited the binding of the patient's serum to solid-phase tobacco leaf. No inhibition was observed when Alternaria, D. pteronyssinus, and potato were used as control inhibitors. Inhibition of immunoCAP to mugwort was obtained with mugwort and tobacco extracts and no cross-reactivity to D. pteronyssinus was shown. CONCLUSION: The results suggest that tobacco can induce IgE-mediated reactions that are mediated by the existence of common antigenic epitopes between tobacco and mugwort pollen. This allergy can be a hazard of employment in the agricultural areas.     

Allergy to Rosaceae fruits without related pollinosis

Background: Rosaceae fruit allergy is frequently associated with birch pollinosis in Central and Northern Europe and with grass pollen allergy in Central Spain. The main cross-reactive structures involved for birch pollinosis are Bet v 1 and profilin, and for grass pollinosis they are profilin and carbohydrate determinants. Rosaceae fruit allergy can occasionally be observed in patients without pollinosis. Objective: We investigated the clinical presentation and the allergens involved in allergy to Rosaceae fruit without pollinosis. Methods: Eleven patients from Central Spain allergic to apples, peaches, and/or pears but not to pollens were compared with 22 control subjects with combined grass pollen and fruit allergy. Skin prick tests and RASTs to apple, peach, and pear were performed. Cross-allergenicity was studied by RAST inhibition. Bet v 1 was tested with an indirect RAST, and profilin was tested in skin prick tests, histamine release, and RAST. Results: Rosaceae fruit allergy without pollinosis is severe with 82% of patients reporting systemic symptoms, mainly anaphylaxis (73%), whereas oral symptoms are less frequent (64%). Anaphylactic shock was observed in 36% of patients. The fruit allergens involved showed cross-reactivity among Rosaceae species but were not related to profilin or Bet v 1. Ninety-one percent of patients with combined grass pollinosis and fruit allergy reported oral allergy, 45% reported systemic symptoms, 18% reported anaphylaxis, and 9% reported anaphylactic shock. Conclusion: Allergy to Rosaceae fruits in patients without a related pollen allergy is a severe clinical entity. Profilin- and Bet v 1-related structures are not involved in Rosaceae fruit allergy without pollinosis.(J Allergy Clin Immunol 97;100;728-33)     

Lipid transfer proteins and allergy to oranges

BACKGROUND: Lipid transfer proteins (LTPs) are relevant fruit allergens, recently proposed as model plant food allergens. No citrus fruit allergen has been characterized to date. We sought to identify and isolate citrus fruit LTPs and to explore their relevance in orange allergy. METHODS: Twenty-seven patients, showing mainly oral allergy syndrome after orange ingestion, as well as positive prick responses and serum-specific IgE levels to orange, were selected. Natural orange and lemon LTPs, as well as a recombinant orange LTP isoform expressed in Pichia pastoris, were isolated by chromatographic methods and characterized by N-terminal amino acid sequencing and matrix-assisted laser desorption/ionizaion mass spectrometry, and DNA sequencing of the corresponding cDNA in the case of the recombinant allergen. Specific IgE determination, immunodetection, ELISA-inhibition assays and in vivo skin prick tests (SPTs) were performed with all three purified allergens and with the major peach LTP allergen, Pru p 3. RESULTS: The natural allergens purified from orange (nCit s 3) and lemon (nCit l 3) showed very similar N-terminal amino acid sequences (18 out of 20 identical residues), typical of LTPs, and molecular masses of 9,610 and 9,618 Da, respectively. The recombinant orange isoform (rCit s 3) expressed in P. pastoris (16 out of 20 residues identical to its natural counterpart in the N-terminal region) presented 92 amino acid residues and 9,463 Da, and 67% sequence identity with rPru p 3. Of the 27 sera analyzed, specific IgE to the purified allergens was found in 54% for nCit l 3, 48% for nCit s 3, 46% for rCit s 3 and 37% for rPru p 3. Positive SPT responses were obtained in 7 out of 26 patients tested for nCit s 3, 3 out of 8 for nCit l 3 and 10 out of 26 for nPru p 3. ELISA-inhibition assays showed an equivalent IgE-binding pattern for the natural and recombinant orange LTPs, and IgE cross-reactivity among the purified orange, lemon and peach LTP allergens. CONCLUSIONS: Members of the LTP allergen family are involved in allergy to oranges, displaying positive in vitro and in vivo reactions in 30-50% of the patients studied. Both orange and lemon allergens show cross-reactivity with the major peach allergen Pru p 3.     

IgE to food allergens are highly prevalent in patients allergic to pollens, with and without symptoms of food allergy

Serum samples from 274 patients allergic to one or more of three pollens (birch, grass, mugwort), from 36 patients allergic to cat and/or Dermatophagoides pteronyssinus but not to pollen and from 55 non-allergic controls, as well as 20 cord blood samples, were examined for specific IgE to six ‘pollen-associated’ food allergens In uiing a new sensitive assay (CAP). A questionnaire asking for reactions to food was also sent to all patients. In the pollen group, 111 patients (47%) were positive (≥0.71 kU/l) fora food allergen (392 positive tests). Of these, 92 were sensitive to apple, 68 to potato, 64 to carrot, 63 to celery, 61 to peach and 44 to melon. In the non-allergic group, no IgE to any of the food allergens tested was found, whereas in the group allergic to non-pollen allergens, only one individual had such an IgE. The CAP assay was found to he more sensitive than RAST for the allergens studied. A history of clinical reactions (oral symptoms in 67, rhinoconjunctivitis in 65, asthma in 42 and urticaria in 39) to the corresponding food allergen was reported mainly by patients with positive CAP. In conclusion, we found a high prevalence of IgE to some food allergens in patients allergic to pollen and Ihe absence of such antibodies in the control groups. The new in vitro assay, being moresensitue than previous ones, indicated a high prevalence of food specific IgE in pollen allergic patients, which in many cases did not correspond to clinical symptoms of food allergy.     

Evaluation of a capsulated hydrophilic carrier polymer (the ImmunoCAP) for measurement of specific IgE antibodies

The Pharmacia CAP System is a new assay for serum specific IgE, utilising a solid phase capable of binding more antigen than conventional systems. The CAP System has been evaluated in 69 consecutive patients referred to one allergy clinic in relation to skin prick test (SPT), radioallergosorbent test (Phadebas RAST) and specific allergy diagnosis for five inhalant allergens, D.pteronyssinus, timothy grass pollen, cat epithelium/dander, Cladosporium and Alternaria. Good correlation was obtained between RAST and CAP for all allergens, e.g. r = 0.974 for D.pteronyssinus and r = 0.964 for grass pollen. When sensitivity and specificity were examined for both CAP and RAST versus SPT, CAP was usually found to be of greater sensitivity than RAST, and of similar or slightly lower specificity. SPT gave more positive reactions than either in vitro test, but CAP gave more positives than RAST. Twenty-two of 336 (6.6%) tests were CAP positive/RAST negative, whereas a negative CAP with a positive RAST occurred in only 2/336 (0.6%) tests. Of patients with any test (SPT or RAST or CAP) for specific IgE positive, up to 20-30% did not have clinical allergy, confirming the importance of the history in interpreting these tests. Our results suggest that, for the allergens tested, the Pharmacia CAP System is more sensitive than the RAST, identifying more positive tests and approximating more closely to the SPT. It offers the additional advantages of speed and efficiency.     

Oral allergy syndrome to fig

BACKGROUND: The few cases of food allergy to fig reported to date, whose main manifestations were anaphylactic reactions, have been related to a cross-sensitisation to weeping fig (Ficus benjamina) or to the 'latex-fruit syndrome'. Here we report on two cases of the oral allergy syndrome (OAS) to fig in patients whose main allergic manifestations were related to sensitisation to grass and birch pollens. METHODS: The patients were characterised by clinical history, skin prick tests (SPT) with commercial and in-house extracts, prick-by-prick test, specific IgE measurements and challenge tests. PBS-soluble and insoluble extracts of both fig skin and pulp were examined for the presence of potential allergens by IgE immunoblotting. RESULTS: Both patients showed OAS followed by respiratory symptoms when challenged with fig. They were negative in both specific IgE detection and SPT with commercial extracts of fig and many other plant materials, including F. benjamina and Hevea Brasiliensis, while grass and birch pollens gave positive results. Prick-by-prick tests and SPT with in-house extracts indicated that the fig skin had a much higher allergenicity than the pulp. Despite negative IgE detection by the CAP assay, immunoblotting experiments showed that potential fig allergens were PBS-soluble and present only in the skin of the fruit. CONCLUSIONS: OAS to fig followed by respiratory symptoms can be present in patients not sensitised to weeping fig or having the latex-fruit syndrome. Different parts of the fig can have different allergenicities, the most important allergens being proteins related to the skin of the fruit. Improved commercial fig extracts to be used for the diagnosis of this type of allergy have to be developed.     

Lupine allergy: not simply cross-reactivity with peanut or soy

BACKGROUND: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized. OBJECTIVES: We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges. METHODS: Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were also allergic to peanut. Lupine allergens were characterized by means of IgE immunoblotting and peptide sequencing. RESULTS: In all 6 patients the ED for lupine flour was 3 mg or less for subjective symptoms and 300 mg or more for objective symptoms. The low ED and moderate-to-severe historical symptoms indicate significant allergenicity of lupine flour. Two patients allergic to lupine but not to peanut displayed IgE binding predominantly to approximately 66-kd proteins and weak binding to 14- and 24-kd proteins, whereas patients with peanut allergy and lupine allergy showed weak binding to lupine proteins of about 14 to 21 or 66 kd. Inhibition of binding was primarily species specific. CONCLUSION: Lupine allergy can occur either separately or together with peanut allergy, as demonstrated by 3 patients who are cosensitized to peanut and lupine. CLINICAL IMPLICATIONS: Lupine flour is allergenic and potentially cross-reactive with peanut allergen, thus posing some risk if used as a replacement for soy flour.     

Respiratory allergy to peach leaves and lipid-transfer proteins

BACKGROUND: Several lipid-transfer proteins (LTPs) have been identified as important food allergens, especially in fruits of the Rosaceae family. The major peach (Prunus persica) allergen has been identified, sequenced and designated Pru p 3. OBJECTIVE: To present Pru p 3 as an aeroallergen able to induce occupational asthma. METHODS: A thorough investigation was performed in a fruit grower with occupational asthma. Skin prick-prick tests with peach leaves and prick tests with perennial respiratory allergens and pollens, fruits and peach leaf extracts were done. Serum-specific IgE was tested for peach leaf, peach fruit, peach skin and respiratory allergens that were positive in skin prick tests. Specific bronchial provocation tests (BPTs) with extracts of peach leaf were also done. Before and 24 h after the BPT, BPTs with methacholine and sputum induction were done. The IgE reactivity pattern to peach leaf and fruit extracts and to Pru p 3 was identified by using SDS-PAGE and immunoblotting. Blotting inhibition of peach leaf extract by Pru p 3 was also performed. The putative allergen was quantified in leaf and fruit skin extracts with ELISA based on an anti-Pru p 3 antibody. RESULTS: Skin tests were positive for peach leaf and fruit. The BPT was positive, with immediate and delayed response. This test induced a decrease in PD20 (dose of agonist that induces a 20% fall in FEV1) methacholine and an increase in eosinophils and eosinophil cationic protein in sputum. Peach leaf extract contained concentrations of Pru p 3 similar to those found in peach skin. Specific IgE immunodetection showed that patient's sera reacted with Pru p 3, and with a single major band from the peach leaf extract fully inhibited by Pru p 3. CONCLUSION: Pru p 3 from peach leaves can act as a respiratory allergen and cause occupational rhinoconjunctivitis and asthma.     

Tobacco as an allergen in bronchial disease.

BACKGROUND: Skin testing and sera measurements have verified the existence of tobacco specific IgE. However, the few published studies on this matter report conflicting results concerning their clinical significance. OBJECTIVE: To verify if a specific clinical allergenic response against tobacco might be possible in allergenic and nonallergenic bronchial diseases. METHODS: We performed a cross-sectional observational case-control analysis on 180 patients with asthma, chronic obstructive pulmonary disease (COPD), and bronchial carcinoma and controls who were randomly chosen. Skin prick tests and serum specific IgE to tobacco and related allergens, bronchial challenge with cigarettes and tobacco extract, patch tests with tobacco and nicotine, sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoblotting, and Enzyme AllergoSorbent Test (EAST) inhibition were performed. RESULTS: Twenty-eight patients had positive tobacco skin prick test results. The association among positive skin prick test results, IgE, and bronchial challenge was strong (P < .001). Tobacco sensitivity was higher in patients with pollen asthma than in patients with COPD and carcinoma and negative in patients with intrinsic asthma and controls. A positive bronchial challenge result was related to the length of habit (P < .001) and the tobacco index in patients who had stopped smoking (P < .001). Delayed bronchial and patch response was more common in patients with COPD (P < .001). Tobacco IgE response (EAST) was related to sensitivity to Lolium perenne (rye grass) pollen (P < .001) but not to other vegetables that belong to the Solanaceae family. EAST inhibition showed cross-reactivity between tobacco and Lolium pollen. CONCLUSIONS: Tobacco may be responsible for a specific IgE response. Patients with pollen asthma were those with more positive responses to tobacco due to cross-reactivity between Lolium and tobacco allergens.