Les Cucurbitacées

[1] - Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol 2000;106:379-385

Allergy to zucchini (Cucurbita pepo), a member of the Cucurbitaceae family, has not previously been reported. We examined 4 patients complaining of allergic symptoms, such as oral allergy syndrome, nausea, diarrhea, or pruritus, after the intake of zucchini. OBJECTIVE: After the confirmation of food allergy, we wanted to characterize zucchini allergens and examine possible cross-reactions to pollen and food. METHODS: The patients underwent skin prick and prick-to-prick-testing with different allergens, including zucchini, latex, and birch, ragweed, and grass pollen. Moreover a double-blind, placebo-controlled, food challenge was performed to confirm food allergy. Total and specific serum IgE levels were determined by using CAP-FEIA and the enzyme allergosorbent test method (EAST), respectively. Proteins from zucchini reacting with patient IgE were detected by means of immunoblotting. To characterize cross-reacting IgE antibodies, immunoblot- and EAST-inhibition assays were carried out. RESULTS: All patients in this study had positive reactions to zucchini both in prick-to-prick tests and double-blind, placebo-controlled, food challenges. Specific serum IgE levels to zucchini were found in all cases. In blot- and EAST-inhibition assays IgE from two patients revealed binding to zucchini profilin at about 15 kd. Furthermore, in two cases, including one of the profilin-positive patients, IgE directed against cross-reacting carbohydrate determinants was detected. For one patient, no cross-reacting IgE could be found, but IgE from this patient reacted strongly with a zucchini protein at 17 kd. CONCLUSIONS: We report the first 4 cases of food allergy to zucchini. Zucchini allergens can cause systemic reactions and are at least partially heat stable. We suggest that allergy to zucchini can occur as a result of primary sensitization to zucchini, as well as to cross-reactions to the panallergen profilin and cross-reacting carbohydrate determinants.

↩

[2] - Pereira C, Tavares B, Loureiro G, Lundberg M, Chieira C. Turnip and zucchini: new foods in the latex-fruit syndrome. Allergy 2007;62:452-453

↩

[3] - Zapatero L, González LA, González de Pedro A, Martínez MI, Alonso E, Lombardero M. A case of pollinic rhinoconjunctivitis and sensitization to Rosaceae and Cucurbitaceae fruits. Allergy Clin Immunol Int 2005;17(Suppl. 1):337

Background: The association between pollen allergy and food allergy to vegetables is frequent due to the existence of panallergens (e.g. profilins, LTPs, Bet v 1-like proteins) in species with no close taxonomic relationship. Clinical case: A ten-year-old boy with a history of pollinic rhinoconjunctivitis and oral allergy syndrome to peach, banana, melon and watermelon, who, after ingestion of pickles, presented lip edema, oropharingeal itching and swelling of the throat that required intravenous pharmacological treatment at the hospital emergency room. Methods: Skin prick tests were carried out with a standard battery of pneumoallergens. Prick-by-prick test was performed with the relevant vegetables. Lip exposure test was done with crude cucumber. Specific IgE was determined against several extracts (Pharmacia CAP System) and rPru p 3 (peach LTP), rMal d 4 (apple profilin) and nBet v 1 (Bayer Centaur platform). Immunoblotting experiments were carried out after SDS-PAGE of cucumber pulp extract using patient's serum and polyclonal antibodies against pear profilin and peach LTP. Results: The patient had a positive test against all the pollens studied. The prick-by-prick test was positive to pickle, cucumber, melon, pumpkin and zucchini (all members of the family Cucurbita), and to peach and banana. Lip exposure test to crude cucumber was positive with a local micropapular rash. The specific IgE was 20.3 kU/L to cucumber, 5.0 to melon, 6.1 to watermelon, 3.9 to peach, 5.3 to banana, 7.8 to Pru p 3, 121.7 to Mal d 4 and 0.7 to Bet v 1. IgE-immunoblotting showed the presence in the cucumber extract of a double band, close to the 15 kDa marker, clearly recognized by patient serum IgE. A similar pattern was obtained when the immunoblotting on the cucumber extract was performed with the anti-profilin antibody, but the anti-LTP antibody did not recognize any cucumber band. Conclusion: The presence of a profilin homologue in the cucumber extract and the sensitization of the patient to profilin can explain his allergic symptoms to different pollens and to pickles and Cucurbitaceae vegetables. In addition, the patient is sensitized to peach LTP, which explains his allergic symptoms with Rosaceae fruits, but no LTP homologue was detected in the cucumber extract.

↩

[4] - Figueredo E, Cuesta-Herranz J, Minguez A, Vidarte L, Pastor C, de las Heras M, et al. Allergy to pumpkin and cross-reactivity to other Cucurbitaceae fruits. J Allergy Clin Immunol 2000;106:402-403

↩

[5] - Hagendorens MM, Carrette M, Bridts CH, Stevens WJ, Ebo DG. Allergy from giant pumpkin (Cucurbita maxima) is not a fairy tale. Allergy 2009;64:1694-1696

↩

[6] - Zapatero L, González LA, González de Pedro A, Martínez MI, Alonso E, Lombardero M. A case of pollinic rhinoconjunctivitis and sensitization to Rosaceae and Cucurbitaceae fruits. Allergy Clin Immunol Int 2005;17(Suppl. 1):337

Background: The association between pollen allergy and food allergy to vegetables is frequent due to the existence of panallergens (e.g. profilins, LTPs, Bet v 1-like proteins) in species with no close taxonomic relationship. Clinical case: A ten-year-old boy with a history of pollinic rhinoconjunctivitis and oral allergy syndrome to peach, banana, melon and watermelon, who, after ingestion of pickles, presented lip edema, oropharingeal itching and swelling of the throat that required intravenous pharmacological treatment at the hospital emergency room. Methods: Skin prick tests were carried out with a standard battery of pneumoallergens. Prick-by-prick test was performed with the relevant vegetables. Lip exposure test was done with crude cucumber. Specific IgE was determined against several extracts (Pharmacia CAP System) and rPru p 3 (peach LTP), rMal d 4 (apple profilin) and nBet v 1 (Bayer Centaur platform). Immunoblotting experiments were carried out after SDS-PAGE of cucumber pulp extract using patient's serum and polyclonal antibodies against pear profilin and peach LTP. Results: The patient had a positive test against all the pollens studied. The prick-by-prick test was positive to pickle, cucumber, melon, pumpkin and zucchini (all members of the family Cucurbita), and to peach and banana. Lip exposure test to crude cucumber was positive with a local micropapular rash. The specific IgE was 20.3 kU/L to cucumber, 5.0 to melon, 6.1 to watermelon, 3.9 to peach, 5.3 to banana, 7.8 to Pru p 3, 121.7 to Mal d 4 and 0.7 to Bet v 1. IgE-immunoblotting showed the presence in the cucumber extract of a double band, close to the 15 kDa marker, clearly recognized by patient serum IgE. A similar pattern was obtained when the immunoblotting on the cucumber extract was performed with the anti-profilin antibody, but the anti-LTP antibody did not recognize any cucumber band. Conclusion: The presence of a profilin homologue in the cucumber extract and the sensitization of the patient to profilin can explain his allergic symptoms to different pollens and to pickles and Cucurbitaceae vegetables. In addition, the patient is sensitized to peach LTP, which explains his allergic symptoms with Rosaceae fruits, but no LTP homologue was detected in the cucumber extract.

↩

[7] - Figueredo E, Cuesta-Herranz J, Minguez A, Vidarte L, Pastor C, de las Heras M, et al. Allergy to pumpkin and cross-reactivity to other Cucurbitaceae fruits. J Allergy Clin Immunol 2000;106:402-403

↩

[8] - Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: A poor predictive value for profilins cross-reactivity. Clin Mol Allergy 2005;3:13

BACKGROUND: Profilins are highly cross-reactive allergens which bind IgE antibodies of almost 20% of plant-allergic patients. This study is aimed at investigating cross-reactivity of melon profilin with other plant profilins and the role of the linear and conformational epitopes in human IgE cross-reactivity . METHODS: Seventeen patients with melon allergy were selected based on clinical history and a positive skin prick test to melon extract. Melon profilin has been cloned and expressed in E. coli. The IgE binding and cross-reactivity of the recombinant profilin were measured by ELISA and inhibition ELISA. The amino acid sequence of melon profilin was compared with other profilin sequences. A combination of chemical cleavage and immunoblotting techniques were used to define the role of conformational and linear epitopes in IgE binding. Comparative modeling was used to construct three-dimensional models of profilins and to assess theoretical impact of amino acid differences on conformational structure . RESULTS: Profilin was identified as a major IgE-binding component of melon. Alignment of amino acid sequences of melon profilin with other profilins showed the most identity with watermelon profilin. This melon profilin showed substantial cross-reactivity with the tomato, peach, grape and Cynodon dactylon (Bermuda grass) pollen profilins. Cantaloupe, watermelon, banana and Poa pratensis (Kentucky blue grass) displayed no notable inhibition. Our experiments also indicated human IgE only react with complete melon profilin. Immunoblotting analysis with rabbit polyclonal antibody shows the reaction of the antibody to the fragmented and complete melon profilin. Although, the well-known linear epitope of profilins were identical in melon and watermelon, comparison of three-dimensional models of watermelon and melon profilins indicated amino acid differences influence the electric potential and accessibility of the solvent-accessible surface of profilins that may markedly affect conformational epitopes . CONCLUSION: Human IgE reactivity to melon profilin strongly depends on the highly conserved conformational structure, rather than a high degree of amino acid sequence identity or even linear epitopes identity.

↩

[9] - Miralles JC, Negro JM, Sanchez Gascon F, Garcia M, Pascual A. Occupational rhinitis/asthma to courgette. Allergy 2000;55:407-408

↩

[10] - Hofmann B, Guilloux L, Guérin L, Leduc V. Allergie au melon (Cucumis melo): implication de la cucumisine. Rev Fr Allergol Immunol Clin 2005;45:274-275

↩

[11] - Varasteh AR, Sankian M, Esmail N, Moghadam M, Pishnamaz R, Mahmoudi M. Persian melon allergy and its allergenic cross reactivity with other allergens. EAACI 23th Congress, Amsterdam, 12-16 June, 2004, Poster n°988

Allergenic reaction to melon, Cucumis melo (belongs to Cucurbitaceae family), has been reported in some allergic patients. Oral allergy syndrome was the most common clinical features associated with melon allergy. This study was aimed to confirm allergenicity of Persian melon (Mashadi melon), identify allergenic protein(s) of melon and its allergenic cross reactivity with other allergens. Prick test was preformed with the extract of different part of melon (Peel, pulp and loose layer on pulp) on the 35 patients who suffer from allergic symptoms after the ingestion of melon. Total IgE and specific IgE to melon were measured in 21 sera from patients with positive skin prick test and 15 healthy controls' sera by means of ELISA. The IgE reactive protein of melon extract was detected by western blotting, using the 12 patient's sera (with high levels of IgE). ELISA inhibition carried out in order to detect cross-reactivity between melon and kiwi, banana, Cynodon dactylon and Poa pratensis. Clinical reactions to melon were oral allergy syndrome 61% (immediate oral itching with or without angioedema of the lips and oral mucosa), rhinitis 38%, itching 19% and gastrointestinal symptoms 4.8%. Twenty one of the 35 patients showed positive skin prick test (SPT) to loose layer on pulp. Three patients also showed reaction to pulp and loose layer. Increased specific IgE levels to melon were observed in 18 patients with positive SPT to melon extract. Inhibition experiments showed a strong cross-reactivity of melon specific IgE with two species of ragweed pollen, especially with Cynodon doctylon, but banana and kiwi extract did not inhibit melon specific IgE in Inhibition ELISA method. Immunoblot analyses of aqueous protein extract from melon were showed an IgE-binding protein of ~ 14.4 kDa with 8 of 12 melon-allergic patients' sera. In conclusion, we confirmed IgE-mediated hypersensitivity to melon with common clinical feature of oral allergy syndrome (OAS) and presence of an IgE-binding protein of ~ 14.4 kDa in melon extract. These findings suggest that main allergen of melon could be profilin.

↩

[12] - Costa Dominguez C, Parra Arrondo A, Lopez-Rico R, Bartolomé B, Diaz Roman T. Selective melon allergy. Allergy 2009;64(Suppl. 90):243-244

Introduction: Melon (Cucumis melon) is a fruit belonging to the Cucurbitaceae family. In Spain it is the second most frequent fruit implicated in allergic reactions. Case: A 44-year-old woman has been suffering from itch, edema and erythema in the skin for the last two years when she handles melon peel. Symptoms begin a few minutes after the contact, lasting 4 hours without treatment. She also refers parestesias on her lips when she eats melon. She denies problems with latex or because of the ingestion or contact with other fruits and vegetables, including other Cucurbitaceas species. She does not present pollen allergy symptoms. Allergy Study: Skin prick test with extracts from a standard allergen panel including mites, fungi, mammal epitheliums, latex, egg, milk, shellfish, peanut, fish, Anisakis simplex and the most important allergenic pollens in our geographical area including grasses, trees and weeds: Negative Skin prick test with commercial fruit extracts (pineapple, cherry, coconut, fig, lemon, apple, peach, melon, orange, banana, watermelon, grape, strawberry, kiwi, pear): negative. Skin prick by prick test with melon Positive to melon peel (21x15 mm wheal; 50 mm erythema) and negative to melon pulp. Skin prick by prick test with other vegetables of Cucurbitaceae family (cucumber, pumpkin and watermelon): Positive to pumpkin peel (10x6 mm wheal; 30x40 mm erythema) Total IgE: 6.23 kU/l. Serum specific IgE: negative against latex, pumkin, rBetv1, rBetv2, watermelon, melon (CAP system Pharmacía); microarray assay showed specific IgE levels below 0.35 kU/ L against a panel of 40 allergens including profilin (rBetv2) and LTP (Pru p3). IgE-immunoblotting with extracts from peel of two varieties of melon, revealed an IgE binding band of 11 kDa. No IgE binding band appeared in melon pulp. Diagnosis: Oral Allergy syndrome and contact urticaria due to melon peel allergy. Discussion: Patients with melon allergy usually have concomitant sensitization to pollen, latex or another fruits, mainly peach, and present symptoms like oral allergy syndrome, respiratory and skin problems. We present a case of melon allergy in which this fruit is the unique cause of allergy. The patient is only sensitized to melon and cucumber. An IgE-binding band of 11 kDa was detected in melon peel.

↩

[13] - Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol 2000;106:379-385

Allergy to zucchini (Cucurbita pepo), a member of the Cucurbitaceae family, has not previously been reported. We examined 4 patients complaining of allergic symptoms, such as oral allergy syndrome, nausea, diarrhea, or pruritus, after the intake of zucchini. OBJECTIVE: After the confirmation of food allergy, we wanted to characterize zucchini allergens and examine possible cross-reactions to pollen and food. METHODS: The patients underwent skin prick and prick-to-prick-testing with different allergens, including zucchini, latex, and birch, ragweed, and grass pollen. Moreover a double-blind, placebo-controlled, food challenge was performed to confirm food allergy. Total and specific serum IgE levels were determined by using CAP-FEIA and the enzyme allergosorbent test method (EAST), respectively. Proteins from zucchini reacting with patient IgE were detected by means of immunoblotting. To characterize cross-reacting IgE antibodies, immunoblot- and EAST-inhibition assays were carried out. RESULTS: All patients in this study had positive reactions to zucchini both in prick-to-prick tests and double-blind, placebo-controlled, food challenges. Specific serum IgE levels to zucchini were found in all cases. In blot- and EAST-inhibition assays IgE from two patients revealed binding to zucchini profilin at about 15 kd. Furthermore, in two cases, including one of the profilin-positive patients, IgE directed against cross-reacting carbohydrate determinants was detected. For one patient, no cross-reacting IgE could be found, but IgE from this patient reacted strongly with a zucchini protein at 17 kd. CONCLUSIONS: We report the first 4 cases of food allergy to zucchini. Zucchini allergens can cause systemic reactions and are at least partially heat stable. We suggest that allergy to zucchini can occur as a result of primary sensitization to zucchini, as well as to cross-reactions to the panallergen profilin and cross-reacting carbohydrate determinants.

↩

[14] - Pereira C, Tavares B, Loureiro G, Lundberg M, Chieira C. Turnip and zucchini: new foods in the latex-fruit syndrome. Allergy 2007;62:452-453

↩

[15] - Caubet JC, Hofer MF, Eigenmann PA, Wassenberg J. Snack seeds allergy in children. Allergy 2010;65:136-137

↩

[16] - Torres J, Ibáñez M, Bartolomé B, Escudero C. Anaphylaxis due to pumpkin seed and Brazil nut: cosensitisation or cross-reactivity ?. Allergy 2009;64(Suppl. 90):249

Background: A 9-year-old boy developed a facial urticaria, lips and eyelids swelling, and dysnea after the ingestion of one roasted pumpkin seed. Since then he does not eat neither pumpkin nor its seeds. He also referred a similar reaction after the ingestion of a Brazil nut five years ago. He tolerates other different nuts and some Cucurbitaceous vegetables and fruits. METHODS: Skin prick-to-prick tests (SPPT) with different nuts (Brazil nut, walnut, hazelnut, and almond) and with Cucurbitaceous family seeds: pumpkin (raw and roasted), cucumber, watermelon, melon and zucchini, and a skin prick test (SPT) with profilin (ALK-Abelló®) were performed. Specific IgE against the mentioned nuts and Cucurbitaceous seeds was measured by means of Enzyme AllergoSorbent Test (EAST). SDS-PAGE and IgE-Immunoblotting in non reducing conditions were carried out using extracts from Brazil nut and raw pumpkin seed. Brazil nut IgE-immunoblotting inhibition analysis was performed using Brazil nut, zucchini, cucumber, and raw pumpkin seeds extracts as inhibitors. RESULTS: SPPT (mm) resulted positive to Brazil nut 12 but negative to the other nuts. Also was positive to pumpkin (raw 9, roasted 11), melon 4, zucchini 5, and watermelon 6. SPT (mm) resulted negative to profilin. Levels of specific IgE: raw pumpkin seed: 1.7 kU/L, roasted pumpkin seed: 1.3 kU/L, melon: 0.8 kU/L, zucchini: 2.1 kU/L, watermelon: 0.8 kU/L, cucumber: 2.3 kU/L, and to Brazil nut: 2.5kU/L. Specific IgE for the other nuts resulted negative (<0.35 kU/L). IgE-Immunoblotting with raw pumpkin seed extract revealed several IgE-binding bands with molecular weights ranging from 14-97 kDa. Six IgE-binding bands of about 14, 26, 40, 50, 67, and 80 kDa were shown in the Brazil nut extract. The Brazil nut IgE-binding bands found were completely inhibited by preadsorption of the patient‚s serum with Brazil nut, zucchini, cucumber, and raw pumpkin seeds extracts. CONCLUSIONS: We present a case of IgE-mediated anaphylaxis due to pumpkin seed and Brazil nut. The IgE-inmmunoblotting inhibition results demonstrated the presence of cross-reactivity between pumpkin seed and Brazil nut.

↩

[17] - Rodríguez-Jiménez B, Domínguez-Ortega J, Ledesma A, González-García JM, Kindelan-Recarte C. Food allergy to pumpkin seed. Allergol Immunopathol (Madr) 2010;38:50-51

↩

[18] - Paradis J, Paradis L, des Roches A, Bui LK, Bougeard H, et al. Anaphylactic reaction to Sechium edule (chayote). Allergy 1997;52(suppl. 37):115

The Sechium edule, commonly named chayote, is classified in the Cucurbitaceae family. This vegetable originates from Latin America, where it is commonly used since pre-Columbian time. It is now produced in many sub-tropical countries. rcpoa: We report 2 cases of anaphylactic reaction to chayote. A 30 year-old woman presented 30 minutes after eating a mixed salad with various exotic vegetables containing chayote, oral itching, angioedema, throat tightness, shortness of breath and an urticarian rash on the upper part of the body. The second patient was a 40 year-old woman. She reported oral itching and throat tightness 15 minutes after eating a similar salad containing chayote. Both patients ate the salad in a Californian style restaurant. We tested all the foods eaten before the reaction and the only positive skin tests was the chayote. We used fresh foods to perform the skin prick tests. In the same time, we performed an extensive battery of skin prick tests to inhalant allergens. Both were polysensitized to birch, grass, artemesia species and ragweed pollens. Conclusion: The apparition on the accidental food market of various fruits and vegetables from foreign countries has led to the apparition of new allergic reaction. In our knowledge, it is the first report of anaphylactic reaction to the chayote. A cross-reactivity with ragweed pollen, known to react with other cucurbitaceae family members as melon, could be possible. Other cases of chayote allergy are susceptible to be reported in the future.

↩

[19] - Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: A poor predictive value for profilins cross-reactivity. Clin Mol Allergy 2005;3:13

BACKGROUND: Profilins are highly cross-reactive allergens which bind IgE antibodies of almost 20% of plant-allergic patients. This study is aimed at investigating cross-reactivity of melon profilin with other plant profilins and the role of the linear and conformational epitopes in human IgE cross-reactivity . METHODS: Seventeen patients with melon allergy were selected based on clinical history and a positive skin prick test to melon extract. Melon profilin has been cloned and expressed in E. coli. The IgE binding and cross-reactivity of the recombinant profilin were measured by ELISA and inhibition ELISA. The amino acid sequence of melon profilin was compared with other profilin sequences. A combination of chemical cleavage and immunoblotting techniques were used to define the role of conformational and linear epitopes in IgE binding. Comparative modeling was used to construct three-dimensional models of profilins and to assess theoretical impact of amino acid differences on conformational structure . RESULTS: Profilin was identified as a major IgE-binding component of melon. Alignment of amino acid sequences of melon profilin with other profilins showed the most identity with watermelon profilin. This melon profilin showed substantial cross-reactivity with the tomato, peach, grape and Cynodon dactylon (Bermuda grass) pollen profilins. Cantaloupe, watermelon, banana and Poa pratensis (Kentucky blue grass) displayed no notable inhibition. Our experiments also indicated human IgE only react with complete melon profilin. Immunoblotting analysis with rabbit polyclonal antibody shows the reaction of the antibody to the fragmented and complete melon profilin. Although, the well-known linear epitope of profilins were identical in melon and watermelon, comparison of three-dimensional models of watermelon and melon profilins indicated amino acid differences influence the electric potential and accessibility of the solvent-accessible surface of profilins that may markedly affect conformational epitopes . CONCLUSION: Human IgE reactivity to melon profilin strongly depends on the highly conserved conformational structure, rather than a high degree of amino acid sequence identity or even linear epitopes identity.

↩

[20] - Lopez-Torrejon G, Crespo JF, Sanchez-Monge R, Sanchez-Jimenez M, Alvarez J, Rodriguez J, et al. Allergenic reactivity of the melon profilin Cuc m 2 and its identification as major allergen. Clin Exp Allergy 2005;35:1065-1072

BACKGROUND: Melon allergy is commonly associated with oral allergy syndrome (OAS) and with hypersensitivity to pollens and other plant foods. No melon allergen responsible for these clinical characteristics has yet been isolated, although profilin has been proposed as a potential target . OBJECTIVE: To isolate natural and recombinant melon profilin, to evaluate its in vivo and in vitro reactivity, and to analyse its behaviour in simulated gastric fluid (SGF) and heat treatments . METHODS: A pool or individual sera from 23 patients, and an additional group of 10 patients, all of them with melon allergy, were analysed by in vitro and in vivo tests, respectively. Natural melon profilin (nCuc m 2) and its recombinant counterpart (rCuc m 2) were isolated by poly-l-proline affinity chromatography, and characterized by N-terminal amino acid sequencing, matrix-assisted laser desorption/ionization analysis, DNA sequencing of cDNAs encoding rCuc m 2, and immunodetection with anti-profilin antibodies. In vitro analysis included IgE immunodetection, specific IgE determination, ELISA-inhibition assays, and histamine release (HR) tests. In vivo activity of nCuc m 2 was established by skin prick testing (SPT). The effect of SGF and heat treatment on rCuc m 2 was followed by immunodetection, ELISA inhibition, and HR assays . RESULTS: Both purified forms of melon profilin were recognized by rabbit anti-profilin antibodies and IgE of sera from allergic patients, and showed molecular sizes typical of the profilin family. nCuc m 2 had a blocked N-terminus, whereas rCuc m 2 rendered the expected N-terminal amino acid sequence, its full protein sequence being highly similar (98--71% identity) to those of profilins from plant foods and pollens. The natural allergen displayed a slightly higher IgE-binding capacity than its recombinant counterpart. Specific IgE to nCuc m 2 and rCuc m 2 was found in 100% and 78% of the 23 individual sera analysed, respectively. nCuc m 2 evoked positive SPT responses in all (10/10) patients tested, and rCuc m 2 induced HR in two out of three sera assayed. SGF treatment readily inactivated rCuc m 2, as shown by its loss of recognition by anti-profilin antibodies, lack of IgE binding, and inability to induce HR. In contrast, heat treatment did not affect the IgE-binding capacity of rCuc m 2 . CONCLUSIONS: Profilin is highly prevalent in melon-allergic patients, and promptly inactivated by SGF, as expected for an allergen mainly linked to OAS.

↩

[21] - Rodriguez-Perez R, Crespo JF, Rodríguez J, Salcedo G. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. J Allergy Clin Immunol 2003;111:634-639

BACKGROUND: Melon allergy has been documented by means of double-blind, placebo-controlled food challenges. The most common clinical feature associated with melon allergy is oral allergy syndrome (OAS). However, no relevant allergens of melon have been identified to date . OBJECTIVE: We sought to identify melon allergens and analyze their digestibility in human saliva and simulated gastric fluid (SGF) to provide a rationale for the OAS . METHODS: Melon, zucchini, cucumber, and watermelon allergens were identified by means of IgE immunoblotting of sera from 21 patients with OAS after melon ingestion confirmed by means of double-blind, placebo-controlled food challenge. Further characterization was performed with rabbit antisera against sunflower pollen profilin and anticomplex glycans. Lability of allergens was assayed by incubation of melon extract in human saliva and SGF . RESULTS: Several IgE-binding components between 15 and 60 kd and a main reactive band of 13 kd were detected in melon extract with the pooled sera from patients with melon allergy. As in melon, 13-kd components of zucchini, cucumber, and watermelon extracts were strongly recognized by the IgE antibodies of the patients with melon allergy and were identified as profilins. Putative cross-reacting carbohydrate determinants were also detected. Sera from 71% of patients recognized the melon profilin, and therefore profilin is considered a major allergen. Melon allergens were unaffected by crude human saliva. In contrast, most melon proteins, predominantly the 13-kd component (profilin), were quickly digested in the SGF . CONCLUSION: In patients with OAS, a 13-kd protein identified as a profilin is a major melon allergen highly susceptible to pepsin digestion.

↩

[22] - Vieths S, Lüttkopf D, Reindl J, Anliker MD, Wüthrich B, Ballmer-Weber BK. Allergens in celery and zucchini. Allergy 2002;57(Suppl. 72):100-105

The aim of this study was to confirm allergy to celery tuber and to zucchini, for the first time, by DBPCFC, and to identify the allergens recognized by IgE from DBPCFC-positive patients. Therefore, raw vegetables were hidden in a broccoli drink, and a DBPCFC-procedure was developed that consisted of a spit and swallow protocol, making sure that the procedure was safe for the patients and that reactions strictly localized to the oral cavity as well as systemic reactions could be reproduced by DBPCFC. The allergens in celery and zucchini extract were identified by immunoblot inhibition using allergen extracts, recombinant allergens and purified N-glycans as inhibitors. Celery allergy was confirmed in 69% (22/32) of subjects with a positive case history. Four subjects with a history of allergic reactions to zucchini had a positive DBPCFC to this vegetable. During DBPCFC, systemic reactions were provoked in 50% (11/22) of the patients to celery, and in 3/4 of the zucchini-allergic patients. The Bet v 1-related major celery allergen was detected by IgE of 59% (13/22) of the patients. Cross-reactive carbohydrate epitopes (CCD) bound IgE of 55% (12/22) of the celery-allergic patients and in 2/4 of the subjects with zucchini allergy. Profilin was a food allergen in celery in 23% (5/22) and in zucchini in 2/4 of the cases. A zucchini-specific allergen was detected by IgE from one patient. We conclude that ubiquitous cross-reactive structures are important in allergy to both, celery and zucchini, and that a specific association to birch pollen allergy exists in allergy to celery (mediated by Api g 1), but not in zucchini allergy.

↩

[23] - Rodriguez-Perez R, Crespo JF, Rodríguez J, Salcedo G. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. J Allergy Clin Immunol 2003;111:634-639

BACKGROUND: Melon allergy has been documented by means of double-blind, placebo-controlled food challenges. The most common clinical feature associated with melon allergy is oral allergy syndrome (OAS). However, no relevant allergens of melon have been identified to date . OBJECTIVE: We sought to identify melon allergens and analyze their digestibility in human saliva and simulated gastric fluid (SGF) to provide a rationale for the OAS . METHODS: Melon, zucchini, cucumber, and watermelon allergens were identified by means of IgE immunoblotting of sera from 21 patients with OAS after melon ingestion confirmed by means of double-blind, placebo-controlled food challenge. Further characterization was performed with rabbit antisera against sunflower pollen profilin and anticomplex glycans. Lability of allergens was assayed by incubation of melon extract in human saliva and SGF . RESULTS: Several IgE-binding components between 15 and 60 kd and a main reactive band of 13 kd were detected in melon extract with the pooled sera from patients with melon allergy. As in melon, 13-kd components of zucchini, cucumber, and watermelon extracts were strongly recognized by the IgE antibodies of the patients with melon allergy and were identified as profilins. Putative cross-reacting carbohydrate determinants were also detected. Sera from 71% of patients recognized the melon profilin, and therefore profilin is considered a major allergen. Melon allergens were unaffected by crude human saliva. In contrast, most melon proteins, predominantly the 13-kd component (profilin), were quickly digested in the SGF . CONCLUSION: In patients with OAS, a 13-kd protein identified as a profilin is a major melon allergen highly susceptible to pepsin digestion.

↩

[24] - Cuesta-Herranz J, Pastor C, Figueredo E, Vidarte L, de las Heras M, Duran C, et al. Identification of cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as the major allergen of melon fruit. Clin Exp Allergy 2003;33:827-833

BACKGROUND: Allergenic components in melon extracts have not been described in spite of the fact that melon (Cucumis melo) is a frequent allergy-eliciting fruit. The aim of this study was to evaluate allergenic components in melon extract and to report the identification of cucumisin as a major melon allergen. MATERIALS AND METHODS: Sera from 35 patients allergic to melon were selected on the basis of clinical symptoms, skin prick tests and oral challenge test. Allergenic components were detected by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing . RESULTS: More than 10 IgE-binding bands, between 10 and 80 kDa, were identified in melon extract. Out of them, four IgE-binding bands were major allergens: 14 kDa, 36 kDa, 54 kDa and 67 kDa. These major allergens, except 14 kDa band, showed the same N-terminal sequence: T-T-R-S-W-D-F-L. Research conducted with protein databases identified this N-terminal sequence as cucumisin, an alkaline serine protease, which shares structural homology with microbial subtilisin. The molecular mass of the identified bands corresponds with different molecular forms of cucumisin produced during the processing or degradation of the enzyme: 67 kDa native cucumisin, 54 kDa mature cucumisin and 36 kDa NH2-terminal cucumisin fragment . CONCLUSION: Cucumisin (Cuc m 1) and several N-terminal cucumisin fragments are the major allergens of melon. The ubiquitous distribution of this protein family (cucumisin-like proteases) in many plant species and its high structural similarity suggest its potential role as a new panallergen in plant foods.

↩

[25] - Asensio T, Crespo JF, Sanchez-Monge R, Lopez-Torrejon G, Somoza ML, Rodriguez J, et al. Novel plant pathogenesis-related protein family involved in food allergy. J Allergy Clin Immunol 2004;114:896-899

Background Members belonging to 9 different families of plant pathogenesis-related (PR) proteins have been identified as pollen and food allergens. However, no PR-1 protein, a family widely distributed throughout the plant kingdom, has been involved so far in allergic reactions. On the other hand, melon ranges among the most relevant fruits causing food allergy in some countries, but the majority of its allergens remain still unidentified. Objective We sought to identify melon allergens related to plant PR proteins. Methods A serum pool or individual sera from 17 patients with allergy to melon confirmed by means of double-blind, placebo-controlled food challenge were used to detect IgE binding proteins of extracts from melon pulp and juice. Cuc m 3 was isolated from melon juice by reverse-phase HPLC and characterized by means of N-terminal amino acid sequencing of internal peptides, matrix-assisted laser desorption/ionization mass spectrometry analysis, direct and inhibition ELISA assays, and skin prick tests. Results Cuc m 3 was a minor component of the melon juice, with a molecular weight of 16,097 d and a blocked N-terminus. N-terminal amino acid sequences of 3 different peptides derived from endo-Lys C digestion (overall 41 residues) showed more than 60% of sequence identity with PR-1 proteins from grape and cucumber. Cuc m 3 bound IgE from 12 of 17 sera from patients allergic to melon and inhibited approximately 40% and 70% of the IgE binding to melon pulp and juice extracts, respectively. Positive skin prick test responses to purified Cuc m 3 were found in 2 of 14 allergic patients. Conclusion A new melon allergen belonging to the PR-1 protein family has been isolated and characterized. It is the first evidence of the involvement of this plant protein family in food allergy.

↩

[26] - Asturias J, Arilla C, Ibarrola I, Daza J, Puente Y, Martinez A. Cloning and Characterization of Art v 2 from Artemisia Vulgaris Pollen. AAAAI 62nd Annual Meeting, Miami, 3-7 March 2006, Poster n°461

RATIONALE: Artemisia vulgaris (mugwort) belongs to the same family than ragweed, the Compositae or Asteracea family, and is one of the main causes of allergy in late summer and autumn. The aim of the study was to characterize the allergen Art v 2 from mugwort pollen METHODS: Skin prick tests were performed in twelve patients allergic to mugwort and 10 control patients. Art v 2 was purified by standard chromatography and binding to Concanavalin A column. Art v 2-encoding cDNA was amplified by PCR using degenerate primers based on reported partial amino acid sequences. Expression of Art v 2 was achieved using vector pKN172 and E. coli BL21 (DE3) RESULTS: Skin prick tests showed Art v 2 prevalences of 58% at 200 µg/ml or 33% at 50 µg/ml, whereas none false positives were detected among control patients. Purified nArt v 2 had 33 kDa and 20 kDa, calculated by gel permeation and SDS-PAGE under denaturing conditions, respectively, showing that the allergen is composed of two identical subunits Cloned cDNA encoding Art v 2 contains 140 bp that codify for a polypeptide of 15.8 kDa, with a predicted pI value of 5.2, and one potential N-glycosylation site. Protein homology search using BLAST software demonstrated that Art v 2 share 55-42% identical residues with pathogenesis related protein PR-1 of tomate, potato, rape, wheat, and rice Homology was also found to Ves v 5 (41% identical residues) CONCLUSIONS: Art v 2 from mugwort is the first pollen allergen that belongs to the pathogenesis related protein PR-1.

↩

[27] - Karamloo F, Wangorsch A, Kasahara H, Davin LB, Haustein D, Lewis NG, et al. Phenylcoumaran benzylic ether and isoflavonoid reductases are a new class of cross-reactive allergens in birch pollen, fruits and vegetables. Eur J Biochem 2001;268:5310-5320

We investigated the biochemical function of the birch pollen allergen Bet v 6 and its role in the IgE-cross-reactivity between birch pollen and plant foods, and characterized Pyr c 5, a Bet v 6-related food allergen, from pear; the proteins were expressed as His-Tag fusion proteins in Eschershia coli and purified by Ni-chelate affinity chromatography under native conditions. Nonfusion proteins were obtained by factor Xa protease treatment. The highest degree of amino-acid sequence identity of Pyr c 5 and Bet v 6 was found with a plant protein related to a defense mechanism, which we have named phenylcoumaran benzylic ether reductase (PCBER) based on its ability to catalyze the NADPH-dependent reduction of 8-5' linked lignans such as dehydrodiconiferyl alcohol to give isodihydrodehydrodiconiferyl alcohol. Enzymatic assays with recombinant Pyr c 5 and Bet v 6 showed PCBER catalytic activity for both recombinant allergens. Both Pyr c 5 and Bet v 6 allergens had similar IgE binding characteristics in immunoblotting and enzyme allergosorbent tests (EAST), and bound IgE from 10 sera of birch-pollen-allergic patients including six pear-allergic subjects. EAST inhibition experiments with Pyr c 5 as the solid phase antigen suggested that homologous allergens may be present in many vegetable foods such as apple, peach, orange, lychee fruit, strawberry, persimmon, zucchini (courgette), and carrot. In extracts of pear, apple, orange, and persimmon, the presence of proteins of approximately 30-35 kDa containing Bet v 6 cross-reactive epitopes was demonstrated with two Bet v 6-specific monoclonal antibodies. Recombinant Pyr c 5 triggered a strong, dose-dependent mediator release from basophils of a pear-allergic subject, suggesting that Pyr c 5 has the potential to elicit type I allergic reactions.

↩

[28] - Pereira C, Tavares B, Loureiro G, Lundberg M, Chieira C. Turnip and zucchini: new foods in the latex-fruit syndrome. Allergy 2007;62:452-453

↩

[29] - Hadfield KA, Dang T, Guis M, Pech JC, Bouzayen M, Bennet AB. Characterization of Ripening-Regulated cDNAs and Their Expression in Ethylene-Suppressed Charentais Melon Fruit. Plant Physiol 2000;122:977-983

Charentais melons (Cucumis melo cv Reticulatus) are climacteric and undergo extremely rapid ripening. Sixteen cDNAs corresponding to mRNAs whose abundance is ripening regulated were isolated to characterize the changes in gene expression that accompany this very rapid ripening process. Sequence comparisons indicated that eight of these cDNA clones encoded proteins that have been previously characterized, with one corresponding to ACC (1-aminocyclopropane-1-carboxylic acid) oxidase, three to proteins associated with pathogen responses, two to proteins involved in sulfur amino acid biosynthesis, and two having significant homology to a seed storage protein or a yeast secretory protein. The remaining eight cDNA sequences did not reveal significant sequence similarities to previously characterized proteins. The majority of the 16 ripening-regulated cDNAs corresponded to mRNAs that were fruit specific, although three were expressed at low levels in vegetative tissues. When examined in transgenic antisense ACC oxidase melon fruit, three distinct patterns of mRNA accumulation were observed. One group of cDNAs corresponded to mRNAs whose abundance was reduced in transgenic fruit but inducible by ethylene treatment, indicating that these genes are directly regulated by ethylene. A second group of mRNAs was not significantly altered in the transgenic fruit and was unaffected by treatment with ethylene, indicating that these genes are regulated by ethylene-independent developmental cues. The third and largest group of cDNAs showed an unexpected pattern of expression, with levels of mRNA reduced in transgenic fruit and remaining low after exposure to ethylene. Regulation of this third group of genes thus appears to ethylene independent, but may be regulated by developmental cues that require ethylene at a certain stage in fruit development. The results confirm that both ethylene-dependent and ethylene-independent pathways of gene regulation coexist in climacteric fruit.

↩

[30] - Ruperti B, Bonghi C, Ziliotto F, Pagni S, Rasori A, Varotto S, et al. Characterization of a major latex protein (MLP) gene down-regulated by ethylene during peach fruitlet abscission. Plant Sci 2002;163:265-272

We report the isolation of a new peach gene, Pp-MLP1, that shows significant similarity to a family of fruit- and flower-specific genes, designated as major latex protein (MLP) homologues. Transcript of Pp-MLP1 highly accumulated in cells of fruit pedicel, similar to lacticifers, adjacent to the abscission zone (non-abscission zone) and, to a lesser extent, in epicotyls, stems and roots, while no accumulation was detected in leaves. In contrast to the MLP homologues isolated so far, the Pp-MLP1 transcript was detected during fruit cells expansion, though its expression appeared unrelated to fruit ripening. Propylene treatment caused a decrease in mRNA accumulation of Pp-MLP1 in all tested tissues. The function of Pp-MLP1, as with all previously described MLP homologues, is unknown. MLPs are associated with fruit and flower development in addition to plant pathogenesis responses. Expression in tissues associated with abscission would be consistent with a role in implementing this aspect of floral development or possibly protective responses to plant pathogens which may infect post-abscission wounds. In addition, the high similarity between proteins encoding by Pp-MLP1 and Csf2, an MLP gene associated with the early development of cucumber fruit, could suggest an alternative developmental role such as cell and tissue expansion.

↩

[31] - Iyer LM, Koonin EV, Aravind L. Adaptations of the helix-grip fold for ligand binding and catalysis in the START domain superfamily. Proteins 2001;43:134-144

With a protein structure comparison, an iterative database search with sequence profiles, and a multiple-alignment analysis, we show that two domains with the helix-grip fold, the star-related lipid-transfer (START) domain of the MLN64 protein and the birch allergen, are homologous. They define a large, previously underappreciated superfamily that we call the START superfamily. In addition to the classical START domains that are primarily involved in eukaryotic signaling mediated by lipid binding and the birch antigen family that consists of plant proteins implicated in stress/pathogen response, the START superfamily includes bacterial polyketide cyclases/aromatases (e.g., TcmN and WhiE VI) and two families of previously uncharacterized proteins. The identification of this domain provides a structural prediction of an important class of enzymes involved in polyketide antibiotic synthesis and allows the prediction of their active site. It is predicted that all START domains contain a similar ligand-binding pocket. Modifications of this pocket determine the ligand-binding specificity and may also be the basis for at least two distinct enzymatic activities, those of a cyclase/aromatase and an RNase. Thus, the START domain superfamily is a rare case of the adaptation of a protein fold with a conserved ligand-binding mode for both a broad variety of catalytic activities and noncatalytic regulatory functions

↩

[32] - Elbez M, Kevers C, Hamdi S, Rideau M, Petit-Paly G. Les protéines de pathogénèse PR-10 des végétaux. Acta Bot Gallica 2002;149:415-444

The PR-10 protein family contains proteins related to pathogenesis and also allergenic proteins. They are acidic proteins with an intracellular localization, usually members of a multigene family and ubiquitous among the plant kingdom. They contain a highly conserved motif, identified as a phosphate-binding site. Even if the biological function of these proteins is still unknown, many indicators seem to favour the hypothesis of RNAse [ribonuclease] activity. Moreover, one of them seems to be a cytokinin-specific binding protein. Besides, the induction of PR-10 protein expression under cytokinin treatment was observed with the Catharanthus roseus CrPR-10a protein. Here, we present evidence of a significant increase in endogenous cytokinin content in leaves of transgenic tobacco plants over-expressing the CrPR10-a protein.

↩

[33] - Pastor C, Cuesta-Herranz J, Cases B, Pérez-Gordo M, Figueredo E, de las Heras M et al. Identification of Major Allergens in Watermelon. Int Arch Allergy Immunol 2009;149:291-298

BACKGROUND: Watermelon is a worldwide consumed Cucurbitaceae fruit that can elicit allergic reactions. However, the major allergens of watermelon are not known. The aim of this study is to identify and characterize major allergens in watermelon . METHODS: Twenty-three patients allergic to watermelon took part in the study. The diagnosis was based on a history of symptoms and positive skin prick-prick tests to watermelon, confirmed by positive open oral challenge testing to watermelon pulp. Allergenic components were detected by SDS-PAGE and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing and mass spectrometry. Allergens were purified combining several chromatographic steps . RESULTS: Several IgE binding bands (8-120 kDa) were detected in watermelon extract. Three major allergens were identified as malate dehydrogenase (36 kDa), triose phosphate isomerase (28 kDa) and profilin (13 kDa). Purified allergens individually inhibited IgE binding to the whole watermelon extract . CONCLUSIONS: All in all these results indicate that malate dehydrogenase, triose phosphate isomerase and profilin are major allergens involved in watermelon allergy.

↩

[34] - Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol 2000;106:379-385

Allergy to zucchini (Cucurbita pepo), a member of the Cucurbitaceae family, has not previously been reported. We examined 4 patients complaining of allergic symptoms, such as oral allergy syndrome, nausea, diarrhea, or pruritus, after the intake of zucchini. OBJECTIVE: After the confirmation of food allergy, we wanted to characterize zucchini allergens and examine possible cross-reactions to pollen and food. METHODS: The patients underwent skin prick and prick-to-prick-testing with different allergens, including zucchini, latex, and birch, ragweed, and grass pollen. Moreover a double-blind, placebo-controlled, food challenge was performed to confirm food allergy. Total and specific serum IgE levels were determined by using CAP-FEIA and the enzyme allergosorbent test method (EAST), respectively. Proteins from zucchini reacting with patient IgE were detected by means of immunoblotting. To characterize cross-reacting IgE antibodies, immunoblot- and EAST-inhibition assays were carried out. RESULTS: All patients in this study had positive reactions to zucchini both in prick-to-prick tests and double-blind, placebo-controlled, food challenges. Specific serum IgE levels to zucchini were found in all cases. In blot- and EAST-inhibition assays IgE from two patients revealed binding to zucchini profilin at about 15 kd. Furthermore, in two cases, including one of the profilin-positive patients, IgE directed against cross-reacting carbohydrate determinants was detected. For one patient, no cross-reacting IgE could be found, but IgE from this patient reacted strongly with a zucchini protein at 17 kd. CONCLUSIONS: We report the first 4 cases of food allergy to zucchini. Zucchini allergens can cause systemic reactions and are at least partially heat stable. We suggest that allergy to zucchini can occur as a result of primary sensitization to zucchini, as well as to cross-reactions to the panallergen profilin and cross-reacting carbohydrate determinants.

↩

[35] - Brehler R, Theissen U, Mohr C, Luger T. 'Latex-fruit syndrome': frequency of cross-reacting IgE antibodies. Allergy 1997;52:404-410

An association between allergies to latex proteins and to various foods has been reported and confirmed by RAST and immunoblotting inhibition. However, no significant data had been collected on the frequency of specific IgE antibodies to fruits in these patients and the frequency of a history of fruit intolerance. Serum samples of 136 patients with well-documented, clinically relevant, immediate-type hypersensitivity against latex proteins were analyzed for IgE antibodies against a panel of different fruits. Patient history of food intolerance was documented by a standardized questionnaire. Fruit-specific IgE antibodies were detected in 69.1% of serum samples. Cross-reacting IgE antibodies recognizing latex and fruit allergens (papaya. avocado, banana, chestnut, passion fruit, fig. melon, mango, kiwi, pineapple, peach, and tomato) were demonstrated by RAST-inhibition tests. Of our patients 42.6% reported allergic symptoms after ingestion of these fruits and a total of 112 intolerance reactions were recorded. However, fruit-specific IgE antibodies were detected only in serum samples from 32.1% of the patients who perceived symptoms due to these fruits. Thus, serologic tests seem to be of low significance for prediction of food allergy in latex-allergic patients.

↩

[36] - Beaudouin E, Renaudin JM, Jacquenet S, Moneret-Vautrin DA. Intérêt diagnostique des IgE spécifiques aux allergènes recombinants du latex. Alim'Inter 2007;12:219-225

↩

[37] - Rodriguez J, Crespo JF, Burks W, Rivas-Plata C, Fernández-Anaya S, Vives R, et al. Randomized, double-blind, crossover challenge study in 53 subjects reporting adverse reactions to melon (Cucumis melo). J Allergy Clin Immunol 2000;106:968-972

BACKGROUND: Few studies have evaluated IgE-mediated hypersensitivity to melon with details of clinical reactions confirmed by double-blind, placebo-controlled, food challenges (DBPCFCs). OBJECTIVE: We sought to investigate clinical features (type and severity of reactions, age at onset, results of skin prick and in vitro tests, and incidence of other allergic diseases and associated food allergies) of acute allergic reactions to melon confirmed by DBPCFCs. METHODS: Fifty-three consecutive adult patients complaining of adverse reactions to melon were included in the study. Skin prick tests and detection of specific IgE were performed in all patients with melon, avocado, kiwi, banana, chestnut, latex, pollen, and other offending foods. Patients first underwent an open food challenge, unless they had a convincing history of severe anaphylaxis. Positive open food challenge reactions were subsequently evaluated by DBPCFCs. RESULTS: Actual clinical reactivity was confirmed in 19 (36%) of 53 patients. The most frequent symptom was oral allergy syndrome (n = 14), but two patients experienced life-threatening reactions, including respiratory symptoms and hypotension. The positive predictive value for a skin prick test was 42%, and that for specific IgE measurement was 44%. Forty-five reactions to 15 other foods were confirmed in 18 patients. The most common foods associated with melon allergy were avocado (n = 7), banana (n = 7), kiwi (n = 6), watermelon (n = 6), and peach (n = 5). Onset of melon-induced allergic symptoms occurred from 6 to 45 years (median, 20 years), preceded by seasonal rhinitis, asthma, or both in 88% (15/17). CONCLUSION: About one third of reported reactions to melon are confirmed by means of DBPCFC, which has been proven to be the most reliable procedure in the diagnosis of clinical fruit allergy. Isolated melon allergy is rare, with most patients either having allergic rhinitis, asthma, or both and associated food allergies.

↩

[38] - Figueredo E, Cuesta-Herranz J, De-Miguel J, Lazaro M, Sastre J, Quirce S, et al. Clinical characteristics of melon (Cucumis melo) allergy. Ann Allergy Asthma Immunol 2003;91:303-308

BACKGROUND: Although melon is a frequent allergy-eliciting fruit, allergic reactions to melon have rarely been reported. OBJECTIVE: To evaluate and describe the clinical characteristics of melon allergy in melon-allergic patients. MATERIALS AND METHODS: We evaluated patients allergic to melon and a control group of patients allergic to pollen. The diagnosis of melon allergy was based on a convincing clinical history, positive skin test results (prick-by-prick test), and positive results on oral challenge tests to melon. RESULTS: A total of 161 patients were included in the study: 66 in the melon allergy group and 95 in the pollen control group. The melon allergy group included 35 female and 31 male patients with a mean age of 26.6 +/- 2.7 years (range, 5-61 years). Although all patients had oral symptoms, 13 (19.7%) of the patients had extraoral symptoms and none experienced generalized urticaria or anaphylaxis. Excluding other Cucurbitaceae fruits, peach, fig, and kiwi most frequently elicited positive skin test results and symptoms. Up to 23% of melon-allergic patients had a concomitant latex sensitization. Melon allergy was especially linked to pollen allergy, since all the melon-allergic patients were also allergic to pollen. Some differential features with respect to the pollen allergy control group were a higher prevalence of asthma (odds ratio [OR], 2.13; P < 0.05) and a statistical increase in the frequency of sensitization to several tree and weed pollens, including Ulmus (OR, 42.8) and Ambrosia (OR, 22.4). CONCLUSION: The most important conditions linked to melon allergy are pollen allergy (100%), allergy to other nonrelated fruits, mainly peach (up to 62%), and latex sensitivity (up to 23%). Some differential features of the pollinosis in melon allergy were a higher prevalence of asthma and a higher frequency of sensitization to several weed and tree pollens.

↩

[39] - Rodriguez J, Crespo JF, Burks W, Rivas-Plata C, Fernández-Anaya S, Vives R, et al. Randomized, double-blind, crossover challenge study in 53 subjects reporting adverse reactions to melon (Cucumis melo). J Allergy Clin Immunol 2000;106:968-972

BACKGROUND: Few studies have evaluated IgE-mediated hypersensitivity to melon with details of clinical reactions confirmed by double-blind, placebo-controlled, food challenges (DBPCFCs). OBJECTIVE: We sought to investigate clinical features (type and severity of reactions, age at onset, results of skin prick and in vitro tests, and incidence of other allergic diseases and associated food allergies) of acute allergic reactions to melon confirmed by DBPCFCs. METHODS: Fifty-three consecutive adult patients complaining of adverse reactions to melon were included in the study. Skin prick tests and detection of specific IgE were performed in all patients with melon, avocado, kiwi, banana, chestnut, latex, pollen, and other offending foods. Patients first underwent an open food challenge, unless they had a convincing history of severe anaphylaxis. Positive open food challenge reactions were subsequently evaluated by DBPCFCs. RESULTS: Actual clinical reactivity was confirmed in 19 (36%) of 53 patients. The most frequent symptom was oral allergy syndrome (n = 14), but two patients experienced life-threatening reactions, including respiratory symptoms and hypotension. The positive predictive value for a skin prick test was 42%, and that for specific IgE measurement was 44%. Forty-five reactions to 15 other foods were confirmed in 18 patients. The most common foods associated with melon allergy were avocado (n = 7), banana (n = 7), kiwi (n = 6), watermelon (n = 6), and peach (n = 5). Onset of melon-induced allergic symptoms occurred from 6 to 45 years (median, 20 years), preceded by seasonal rhinitis, asthma, or both in 88% (15/17). CONCLUSION: About one third of reported reactions to melon are confirmed by means of DBPCFC, which has been proven to be the most reliable procedure in the diagnosis of clinical fruit allergy. Isolated melon allergy is rare, with most patients either having allergic rhinitis, asthma, or both and associated food allergies.

↩

[40] - Figueredo E, Cuesta-Herranz J, De-Miguel J, Lazaro M, Sastre J, Quirce S, et al. Clinical characteristics of melon (Cucumis melo) allergy. Ann Allergy Asthma Immunol 2003;91:303-308

BACKGROUND: Although melon is a frequent allergy-eliciting fruit, allergic reactions to melon have rarely been reported. OBJECTIVE: To evaluate and describe the clinical characteristics of melon allergy in melon-allergic patients. MATERIALS AND METHODS: We evaluated patients allergic to melon and a control group of patients allergic to pollen. The diagnosis of melon allergy was based on a convincing clinical history, positive skin test results (prick-by-prick test), and positive results on oral challenge tests to melon. RESULTS: A total of 161 patients were included in the study: 66 in the melon allergy group and 95 in the pollen control group. The melon allergy group included 35 female and 31 male patients with a mean age of 26.6 +/- 2.7 years (range, 5-61 years). Although all patients had oral symptoms, 13 (19.7%) of the patients had extraoral symptoms and none experienced generalized urticaria or anaphylaxis. Excluding other Cucurbitaceae fruits, peach, fig, and kiwi most frequently elicited positive skin test results and symptoms. Up to 23% of melon-allergic patients had a concomitant latex sensitization. Melon allergy was especially linked to pollen allergy, since all the melon-allergic patients were also allergic to pollen. Some differential features with respect to the pollen allergy control group were a higher prevalence of asthma (odds ratio [OR], 2.13; P < 0.05) and a statistical increase in the frequency of sensitization to several tree and weed pollens, including Ulmus (OR, 42.8) and Ambrosia (OR, 22.4). CONCLUSION: The most important conditions linked to melon allergy are pollen allergy (100%), allergy to other nonrelated fruits, mainly peach (up to 62%), and latex sensitivity (up to 23%). Some differential features of the pollinosis in melon allergy were a higher prevalence of asthma and a higher frequency of sensitization to several weed and tree pollens.

↩

[41] - Vieths S, Lüttkopf D, Reindl J, Anliker MD, Wüthrich B, Ballmer-Weber BK. Allergens in celery and zucchini. Allergy 2002;57(Suppl. 72):100-105

The aim of this study was to confirm allergy to celery tuber and to zucchini, for the first time, by DBPCFC, and to identify the allergens recognized by IgE from DBPCFC-positive patients. Therefore, raw vegetables were hidden in a broccoli drink, and a DBPCFC-procedure was developed that consisted of a spit and swallow protocol, making sure that the procedure was safe for the patients and that reactions strictly localized to the oral cavity as well as systemic reactions could be reproduced by DBPCFC. The allergens in celery and zucchini extract were identified by immunoblot inhibition using allergen extracts, recombinant allergens and purified N-glycans as inhibitors. Celery allergy was confirmed in 69% (22/32) of subjects with a positive case history. Four subjects with a history of allergic reactions to zucchini had a positive DBPCFC to this vegetable. During DBPCFC, systemic reactions were provoked in 50% (11/22) of the patients to celery, and in 3/4 of the zucchini-allergic patients. The Bet v 1-related major celery allergen was detected by IgE of 59% (13/22) of the patients. Cross-reactive carbohydrate epitopes (CCD) bound IgE of 55% (12/22) of the celery-allergic patients and in 2/4 of the subjects with zucchini allergy. Profilin was a food allergen in celery in 23% (5/22) and in zucchini in 2/4 of the cases. A zucchini-specific allergen was detected by IgE from one patient. We conclude that ubiquitous cross-reactive structures are important in allergy to both, celery and zucchini, and that a specific association to birch pollen allergy exists in allergy to celery (mediated by Api g 1), but not in zucchini allergy.

↩

[42] - Asero R, Mistrello G, Roncarolo D, Amato S, Zanoni D, Barocci F, et al. Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods. J Allergy Clin Immunol 2003;112:427-432

BACKGROUND: A proper classification of patients allergic to plant-derived foods is of pivotal importance because the clinical features of allergic reactions to fruits and vegetables depend on the nature and characteristics of proteins responsible for sensitization. However, in normal clinical settings this is presently impossible . OBJECTIVE: We sought to detect clinical markers of sensitization to profilin . METHODS: Seventy-one patients allergic to fruits and vegetables but not sensitized to lipid transfer protein or natural rubber latex were studied. Food allergy was ascertained on the basis of clinical history and positive skin prick test responses with fresh foods, commercial extracts, or both. Allergies to foods that had caused less than 2 adverse reactions were confirmed by means of open oral challenge. IgE reactivity to rBet v 1/rBet v 2 and to natural Phleum species profilin were detected. Moreover, IgE to the 30- to 40-kd and 60- to 90-kd birch pollen-enriched fractions, which also can be involved in cross-reactivity phenomena, were measured in sera from 52 patients by means of ELISA . RESULTS: On the basis of in vitro tests, 24, 18, and 25 patients turned out to be sensitized to Bet v 1, Bet v 2, or both, respectively. Four patients had negative test results for both allergens. Hypersensitivity to Bet v 2 was strongly associated with clinical allergy to citrus fruits (39% in patients monosensitized to Bet v 2 vs 4% in patients monosensitized to Bet v 1, P <.025), melon or watermelon (67% vs 0%, P <.001), banana (66% vs 8%, P <.001), and tomato (33% vs 0%, P <.05), whereas Bet v 1 sensitivity was associated with clinical allergy to apple (100% vs 39%, P <.001) and hazelnut (56% vs 0%, P <.001). The sensitivity of a history of allergy to gourd fruits, citrus fruits, tomato, banana, or a combination thereof as a means to detect profilin-hypersensitive patients was 85% (41/48). The specificity of an allergy to any of these fruits exceeded 85%, with positive predictive values ranging between 68% and 91% . CONCLUSION: In clinical settings in which laboratory investigations are not easily accessible, allergy to melon, watermelon, citrus fruits, tomato, and banana can be used as a marker of profilin hypersensitivity once a sensitization to natural rubber latex and lipid transfer protein is ruled out.

↩

[43] - Pereira C, Tavares B, Loureiro G, Lundberg M, Chieira C. Turnip and zucchini: new foods in the latex-fruit syndrome. Allergy 2007;62:452-453

↩

[44] - Vlaicu P, Rusu L, Ledesma A, Zamorano M, Antolin-Amerigo D, Alvarez-Cuesta E et al. Cucumber allergy: a new plant-derived food with cross-reactivity to latex. Allergy 2009;64(Suppl. 90):481

Background: The allergy to plants-derived food is a frequent cause of food allergy and represents a growing clinical problem. The cucumber (Cucumis sativus) is a fruit belonging to Cucurbitaceas family. Methods: We report the case of a 76-years-old woman who experienced dizziness, malaise, vomiting, difficulty breathing, submammary erythema and pruritus, vaginal itching, within 5 min of eating half peeled cucumber. The patient presented approx 3 months before an episode of acute urticaria after eating papaya, and she was diagnosed as having latex allergy. The patient had no history of allergic rhinitis, asthma or atopic eczema. She reported only one previous knee surgical intervention as a risk factor to latex sensitization. Skin prick tests with commercial battery of inhalant and food allergens, including cucumber, watermelon, melon, papaya and profilin were performed. The investigation comprised quantification of total IgE and specific IgE (ImmunoCAP, Phadia) for cucumber and latex. We also performed, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting with cucumber, papaya, melon and latex extracts, in order to analyze the protein bands and their molecular weights, and identify IgE- binding bands. Immunoblot inhibition was performed with latex in order to investigate cross-reactivity. Results: Skin prick tests for cucumber, watermelon, papaya and latex extracts were positive, and negative for melon and profilin extracts. ImmunoCAP for latex specific serum IgE was positive. Specific serum IgE for latex allergens were positive for rubber elongation factor (Hev b1), rubber acidic protein (Hev b5), prohevein (Hev b6), and negative for rubber profilin (Hev b8), avocado and chestnut chitinase (Prs a 1 and Cas s 5), apple profilin (Mal d 4) and peach LTP (Pru p 3). Cucumber specific serum IgE was negative. Immunoblot analysis using patient serum detected a 30-32-kD protein band in the cucumber and papaya extract. Immunoblot inhibition with latex extract demonstrated inhibition of the band in each of the two vegetable extract. Conclusion: We present a case of allergy IgE mediated to cucumber (anaphylaxis) and papaya (urticaria). Our results strongly suggest that the allergen/s implicated are associated with latex sensitization. In our knowledge is the first report of the association between cucumber and latex allergy, and our results confirm cucumber as another food with clinical cross-reactivity in latex allergy patients.

↩

[45] - Cuesta-Herranz J, Pastor C, Figueredo E, Vidarte L, de las Heras M, Duran C, et al. Identification of cucumisin (Cuc m 1), a subtilisin-like endopeptidase, as the major allergen of melon fruit. Clin Exp Allergy 2003;33:827-833

BACKGROUND: Allergenic components in melon extracts have not been described in spite of the fact that melon (Cucumis melo) is a frequent allergy-eliciting fruit. The aim of this study was to evaluate allergenic components in melon extract and to report the identification of cucumisin as a major melon allergen. MATERIALS AND METHODS: Sera from 35 patients allergic to melon were selected on the basis of clinical symptoms, skin prick tests and oral challenge test. Allergenic components were detected by sodium dodecyl sulphate polyacrylamide gel electrophoresis and immunoblotting. Molecular characterization of IgE-binding bands was performed by N-terminal amino acid sequencing . RESULTS: More than 10 IgE-binding bands, between 10 and 80 kDa, were identified in melon extract. Out of them, four IgE-binding bands were major allergens: 14 kDa, 36 kDa, 54 kDa and 67 kDa. These major allergens, except 14 kDa band, showed the same N-terminal sequence: T-T-R-S-W-D-F-L. Research conducted with protein databases identified this N-terminal sequence as cucumisin, an alkaline serine protease, which shares structural homology with microbial subtilisin. The molecular mass of the identified bands corresponds with different molecular forms of cucumisin produced during the processing or degradation of the enzyme: 67 kDa native cucumisin, 54 kDa mature cucumisin and 36 kDa NH2-terminal cucumisin fragment . CONCLUSION: Cucumisin (Cuc m 1) and several N-terminal cucumisin fragments are the major allergens of melon. The ubiquitous distribution of this protein family (cucumisin-like proteases) in many plant species and its high structural similarity suggest its potential role as a new panallergen in plant foods.

↩

[46] - Parker JE. Plant recognition of microbial patterns. Trends Plant Sci 2003;8:245-247

Animals express an innate immune system against pathogens through receptor-mediated recognition of conserved microbial structures called pathogen-associated molecular patterns (PAMPs). In plants, resistance to invading microorganisms is often governed by specific recognition between plant and pathogen proteins. Perception of more broadly conserved 'general' pathogen elicitors constitutes another layer of plant resistance and prompts questions of where, mechanistically and evolutionarily, this mode of non-self discrimination fits within known systems of microbial surveillance in animals and plants.

↩

[47] - Hofmann B, Guilloux L, Guérin L, Leduc V. Allergie au melon (Cucumis melo): implication de la cucumisine. Rev Fr Allergol Immunol Clin 2005;45:274-275

↩

[48] - Miralles JC, Negro JM, Sanchez Gascon F, Garcia M, Pascual A. Occupational rhinitis/asthma to courgette. Allergy 2000;55:407-408

↩

[49] - Zapatero L, González LA, González de Pedro A, Martínez MI, Alonso E, Lombardero M. A case of pollinic rhinoconjunctivitis and sensitization to Rosaceae and Cucurbitaceae fruits. Allergy Clin Immunol Int 2005;17(Suppl. 1):337

Background: The association between pollen allergy and food allergy to vegetables is frequent due to the existence of panallergens (e.g. profilins, LTPs, Bet v 1-like proteins) in species with no close taxonomic relationship. Clinical case: A ten-year-old boy with a history of pollinic rhinoconjunctivitis and oral allergy syndrome to peach, banana, melon and watermelon, who, after ingestion of pickles, presented lip edema, oropharingeal itching and swelling of the throat that required intravenous pharmacological treatment at the hospital emergency room. Methods: Skin prick tests were carried out with a standard battery of pneumoallergens. Prick-by-prick test was performed with the relevant vegetables. Lip exposure test was done with crude cucumber. Specific IgE was determined against several extracts (Pharmacia CAP System) and rPru p 3 (peach LTP), rMal d 4 (apple profilin) and nBet v 1 (Bayer Centaur platform). Immunoblotting experiments were carried out after SDS-PAGE of cucumber pulp extract using patient's serum and polyclonal antibodies against pear profilin and peach LTP. Results: The patient had a positive test against all the pollens studied. The prick-by-prick test was positive to pickle, cucumber, melon, pumpkin and zucchini (all members of the family Cucurbita), and to peach and banana. Lip exposure test to crude cucumber was positive with a local micropapular rash. The specific IgE was 20.3 kU/L to cucumber, 5.0 to melon, 6.1 to watermelon, 3.9 to peach, 5.3 to banana, 7.8 to Pru p 3, 121.7 to Mal d 4 and 0.7 to Bet v 1. IgE-immunoblotting showed the presence in the cucumber extract of a double band, close to the 15 kDa marker, clearly recognized by patient serum IgE. A similar pattern was obtained when the immunoblotting on the cucumber extract was performed with the anti-profilin antibody, but the anti-LTP antibody did not recognize any cucumber band. Conclusion: The presence of a profilin homologue in the cucumber extract and the sensitization of the patient to profilin can explain his allergic symptoms to different pollens and to pickles and Cucurbitaceae vegetables. In addition, the patient is sensitized to peach LTP, which explains his allergic symptoms with Rosaceae fruits, but no LTP homologue was detected in the cucumber extract.

↩

[50] - Rodriguez J, Crespo JF, Burks W, Rivas-Plata C, Fernández-Anaya S, Vives R, et al. Randomized, double-blind, crossover challenge study in 53 subjects reporting adverse reactions to melon (Cucumis melo). J Allergy Clin Immunol 2000;106:968-972

BACKGROUND: Few studies have evaluated IgE-mediated hypersensitivity to melon with details of clinical reactions confirmed by double-blind, placebo-controlled, food challenges (DBPCFCs). OBJECTIVE: We sought to investigate clinical features (type and severity of reactions, age at onset, results of skin prick and in vitro tests, and incidence of other allergic diseases and associated food allergies) of acute allergic reactions to melon confirmed by DBPCFCs. METHODS: Fifty-three consecutive adult patients complaining of adverse reactions to melon were included in the study. Skin prick tests and detection of specific IgE were performed in all patients with melon, avocado, kiwi, banana, chestnut, latex, pollen, and other offending foods. Patients first underwent an open food challenge, unless they had a convincing history of severe anaphylaxis. Positive open food challenge reactions were subsequently evaluated by DBPCFCs. RESULTS: Actual clinical reactivity was confirmed in 19 (36%) of 53 patients. The most frequent symptom was oral allergy syndrome (n = 14), but two patients experienced life-threatening reactions, including respiratory symptoms and hypotension. The positive predictive value for a skin prick test was 42%, and that for specific IgE measurement was 44%. Forty-five reactions to 15 other foods were confirmed in 18 patients. The most common foods associated with melon allergy were avocado (n = 7), banana (n = 7), kiwi (n = 6), watermelon (n = 6), and peach (n = 5). Onset of melon-induced allergic symptoms occurred from 6 to 45 years (median, 20 years), preceded by seasonal rhinitis, asthma, or both in 88% (15/17). CONCLUSION: About one third of reported reactions to melon are confirmed by means of DBPCFC, which has been proven to be the most reliable procedure in the diagnosis of clinical fruit allergy. Isolated melon allergy is rare, with most patients either having allergic rhinitis, asthma, or both and associated food allergies.

↩

[51] - Garcia Ortiz JC, Ventas P, Cosmes Martin P, Lopez-Asunsolo A. An immunoblotting analysis of cross-reactivity between melon, and plantago and grass pollens. J Investig Allergol Clin Immunol 1996;6:378-382

It is known that most patients with type I allergy to pollens also suffer intolerance to fruits. Recently, an epidemiological and CAP-inhibition study has shown a new clustering of allergy between melon and Plantago and grass pollens. The aim of the present study was to confirm these results by immunoblotting analysis and inhibition of immunoblotting. Sera from 3 patients with confirmed allergy to melon, and Dactylis glomerata and Plantago lanceolata pollens were used for the in vitro studies. SDS-PAGE and immunoblotting analysis with a pool of sera revealed that several distinct protein bands were shared by the three extracts at 14, 31, and a spectrum between 40 and 70 kDa, approximately. Immunoblotting inhibition experiments, performed with extracts of melon, Plantago and Dactylis, showed that all allergens of melon blotting were almost completely inhibited by grass and Plantago pollen extracts. Inversely, the melon extract was capable of inhibiting IgE-binding to various allergens of Dactylis at high mol mass and partially to the band at 14 kDa. Moreover, the melon almost totally inhibited the IgE-binding capacity to the proteins of Plantago extract. Taken together, the results support the presence of structurally similar allergens in melon, Plantago and grass pollens, and that all allergenic epitopes of the melon are present in these pollens.

↩

[52] - Garcia Ortiz JC, Cosmes Martin P, Lopez-Asunsolo A. Melon sensitivity shares allergens with Plantago and grass pollens. Allergy 1995;50:269-273

Possible associations between allergy to pollen and that to food allergens were studied in 262 patients sensitized to pollen. Forty-four patients (16.7%) showed some allergic symptoms after testing with fruits and vegetables, melon being the food most frequently involved (24 patients), followed by sunflower seed (12 patients). Skin testing was done by the prick method with natural fruit or vegetable, and also with commercial food extracts. We found in our region that the distribution of sensitivity to pollens in the group of patients with allergy to fruits or vegetables does not coincide with the prevalence in pollen-allergic subjects in general, since in the first group--subjects allergic to food--there was a major prevalence of allergy to Plantago (P < 0.01). In particular, in the group of subjects allergic to melon, the prevalence of sensitivity to grass and especially to Plantago was larger than in pollen-allergic subjects in general (P < 0.05 and P < 0.001, respectively). The use of fresh food produced better results than commercial extracts. A positive skin test to fresh melon closely correlated with positive CAP results. CAP inhibition experiments were carried out, and we found that Dactylis and Plantago extracts inhibited the binding of the melon-positive pool to solid-phase melon. The results suggest the existence of common antigenic epitopes in melon and Plantago pollen, and in melon and grass pollen.

↩

[53] - Enberg RN, Leickly FE, McCullough J, Bailey J, Ownby DR. Watermelon and ragweed share allergens. J Allergy Clin Immunol 1987;79:867-875

A biotin-avidin amplified ELISA was used to measure antigen-specific IgE for ragweed, representative members of the gourd family (watermelon, cantaloupe, honeydew melon, zucchini, and cucumber), and banana in the sera of 192 allergic patients, each with an IgE greater than or equal to 180 microns/ml. Sixty-three percent (120/192) of the sera contained antiragweed IgE, and of these patients, 28% to 50% contained IgE specific for any single gourd family member. In contrast, no greater than 11% of the sera positive for a given gourd or banana were negative for ragweed. Correlations between ragweed and gourd-specific IgE levels were significant (p less than 0.001), and correlation coefficients between any two gourds exceeded 0.79. In an ELISA system, the extracts of watermelon and ragweed inhibited each other in a dose-dependent manner; the resulting nonparallel inhibition curves indicate that some, but not all, of the allergens in the two extracts are cross-reactive. Isoelectric focusing of watermelon and ragweed extracts in narrow range gel (pH 4 to 6) followed by immunoblotting demonstrated six watermelon allergen bands with isoelectric points identical to those of ragweed allergens. Several remaining bands in the two extracts had differing isoelectric points, however. Six of 26 patients interviewed with watermelon-specific IgE reported developing oropharyngeal symptoms (itching and/or swelling of the lips, tongue, or throat) after ingesting at least one of the study foods, whereas only one of 25 patients interviewed without detectable watermelon-specific IgE reported similar symptoms (p = 0.05)

↩

[54] - Anderson LB Jr, Dreyfuss EM, Logan J, Johnstone DE, Glaser J. Melon and banana sensitivity coincident with ragweed pollinosis. J Allergy 1970;45:310-319

↩

[55] - Jordan-Wagner DL, Whisman BA, Goetz DW. Cross-allergenicity among celery, cucumber, carrot, and watermelon. Ann Allergy 1993;71:70-79

Cross-reactive allergens may be responsible for the clustering of food allergies seen in patients hypersensitive to fruits and vegetables. The pooled sera of six individuals were used to investigate cross-antigenicity among freshly prepared extracts of celery (Cy), cucumber (Cc), carrot (Ct), and watermelon (W). Each patient demonstrated clinical allergy to one or more study foods and, with the exception of Ct in two cases, had IgE to all four extracts by skin test or ELISA. In comparisons of each food against itself and the other three antigens, ELISA inhibition assays demonstrated allergenic similarity among Cy, Cc, Ct, and W by their similar slopes and 50% inhibition concentrations (2.0-7.3 micrograms/mL) In contrast, mountain cedar pollen (MC) produced at 50% inhibition of each food which was 10-fold higher (26.9-70.8 micrograms/mL) and had a flatter slope. Immunoblots of individual sera showed a 15-kD protein band common to all four foods. Pooled sera immunoblot inhibitions (100 and 5 micrograms/mL) demonstrated mutual inhibition of all bands in each of the four foods with the exception of a 28-kD protein of W uniquely inhibited by itself. We conclude that Cy, Cc, Ct, and W possess shared antigens that may account for clustering of these food allergies in patients.

↩

[56] - Asero R, Mistrello G, Roncarolo D, Amato S. Detection of Some Safe Plant-Derived Foods for LTP-Allergic Patients. Int Arch Allergy Immunol 2007;144:57-63

BACKGROUND: Lipid transfer protein (LTP) is a widely cross-reacting plant pan-allergen. Adverse reactions to Rosaceae, tree nuts, peanut, beer, maize, mustard, asparagus, grapes, mulberry, cabbage, dates, orange, fig, kiwi, lupine, fennel, celery, tomato, eggplant, lettuce, chestnut and pineapple have been recorded . OBJECTIVE: To detect vegetable foods to be regarded as safe for LTP-allergic patients . METHODS: Tolerance/intolerance to a large spectrum of vegetable foods other than Rosaceae, tree nuts and peanut was assessed by interview in 49 subjects monosensitized to LTP and in three distinct groups of controls monosensitized to Bet v 1 (n = 24) or Bet v 2 (n = 18), or sensitized to both LTP and birch pollen (n = 16), all with a history of vegetable food allergy. Patients and controls underwent skin prick test (SPT) with a large spectrum of vegetable foods. The absence of IgE reactivity to foods that were negative in both clinical history and SPT was confirmed by immunoblot analysis and their clinical tolerance was finally assessed by open oral challenge (50 g per food) . RESULTS: All patients reported tolerance and showed negative SPT to carrot, potato, banana and melon; these foods scored positive in SPT and elicited clinical symptoms in a significant proportion of patients from all three control groups. All patients tolerated these four foods on oral challenge. Immunoblot analysis confirmed the lack of IgE reactivity to these foods by LTP-allergic patients . CONCLUSION: Carrot, potato, banana and melon seem safe for LTP-allergic patients. This finding may be helpful for a better management of allergy to LTP.

↩

[57] - Asero R, Monsalve R, Barber D. Profilin sensitization detected in the office by skin prick test: a study of prevalence and clinical relevance of profilin as a plant food allergen. Clin Exp Allergy 2008;38:1033-1037

BACKGROUND: Profilin, a pan-allergen present in all eukaryotic cells, is one of the main causes of cross-sensitization between pollen and plant-derived foods, but its clinical relevance as a food allergen is still debated . OBJECTIVE: To investigate the prevalence of profilin sensitization in a pollen-allergic population and its clinical relevance as a food allergen . METHODS: Two hundred consecutive patients with pollen allergy underwent skin prick tests (SPT) with purified natural date palm profilin (Pho d 2; 50 microg/mL; Alk Abello, Madrid, Spain). Those reporting adverse reactions to foods (confirmed by SPT with either commercial food extracts or fresh foods) underwent SPT with an apple extract containing uniquely Mal d 1 (2 microg/mL; ALK-Abello), and with a commercial peach extract containing uniquely lipid transfer protein (LTP 30 microg/mL; ALK-Abello) . RESULTS: Sixty patients (30%) showed skin reactivity to date palm profilin, Pho d 2. All were sensitized to grass pollen, and most of them reacted to birch, mugwort, ragweed and plantain pollen as well. SPT with pellitory and cypress scored negative in a high proportion of profilin reactors [26/60 (43%) and 33/60 (55%), respectively]. More than one half (34/60 [57%]) of profilin reactors had food allergy; 21 of these were monosensitized to profilin, 11 were sensitized to both profilin and Bet v 1 homologous protein, one to both profilin and LTP, and one to all the three allergens. The large majority of profilin-allergic patients reported oral allergy syndrome as the only food-induced symptom and were able to tolerate the offending foods if they were cooked or otherwise processed. Twenty-eight of 34 reported reactivity to two or more plant-derived foods. Rosaceae, tree nuts, melon and watermelon, tomato, pineapple, citrus fruits and banana were the more frequently offending foods . CONCLUSION: Profilin should be considered a clinically relevant food allergen. Allergy to melon, watermelon, tomato, banana, pineapple and orange may be considered as a marker of profilin hypersensitivity. This study underlines the clinical importance of being able to diagnose hypersensitivity to single food allergenic proteins by SPT, particularly when the relevant food allergen sources contain several allergens that show different chemical/physical features and, hence, completely different risk profiles.

↩

[58] - Cuesta J, Blanco C, Fernández-Rivas M, Villalba M. Vegetalia. J Investig Allergol Clin Immunol 2006;16(Suppl. 2):40-44

↩

[59] - Fernández-Rivas M. Alergia a frutas y hortalizas. in "Alergia a alimentos", Sociedad Española de Alergología e Inmunología Clínica (SEAIC) Ed., Euromedice, Badalona 2004, pp.143-67

↩

[60] - Rodriguez-Perez R, Crespo JF, Rodríguez J, Salcedo G. Profilin is a relevant melon allergen susceptible to pepsin digestion in patients with oral allergy syndrome. J Allergy Clin Immunol 2003;111:634-639

BACKGROUND: Melon allergy has been documented by means of double-blind, placebo-controlled food challenges. The most common clinical feature associated with melon allergy is oral allergy syndrome (OAS). However, no relevant allergens of melon have been identified to date . OBJECTIVE: We sought to identify melon allergens and analyze their digestibility in human saliva and simulated gastric fluid (SGF) to provide a rationale for the OAS . METHODS: Melon, zucchini, cucumber, and watermelon allergens were identified by means of IgE immunoblotting of sera from 21 patients with OAS after melon ingestion confirmed by means of double-blind, placebo-controlled food challenge. Further characterization was performed with rabbit antisera against sunflower pollen profilin and anticomplex glycans. Lability of allergens was assayed by incubation of melon extract in human saliva and SGF . RESULTS: Several IgE-binding components between 15 and 60 kd and a main reactive band of 13 kd were detected in melon extract with the pooled sera from patients with melon allergy. As in melon, 13-kd components of zucchini, cucumber, and watermelon extracts were strongly recognized by the IgE antibodies of the patients with melon allergy and were identified as profilins. Putative cross-reacting carbohydrate determinants were also detected. Sera from 71% of patients recognized the melon profilin, and therefore profilin is considered a major allergen. Melon allergens were unaffected by crude human saliva. In contrast, most melon proteins, predominantly the 13-kd component (profilin), were quickly digested in the SGF . CONCLUSION: In patients with OAS, a 13-kd protein identified as a profilin is a major melon allergen highly susceptible to pepsin digestion.

↩

[61] - Reindl J, Anliker MD, Karamloo F, Vieths S, Wüthrich B. Allergy caused by ingestion of zucchini (Cucurbita pepo): characterization of allergens and cross-reactivity to pollen and other foods. J Allergy Clin Immunol 2000;106:379-385

Allergy to zucchini (Cucurbita pepo), a member of the Cucurbitaceae family, has not previously been reported. We examined 4 patients complaining of allergic symptoms, such as oral allergy syndrome, nausea, diarrhea, or pruritus, after the intake of zucchini. OBJECTIVE: After the confirmation of food allergy, we wanted to characterize zucchini allergens and examine possible cross-reactions to pollen and food. METHODS: The patients underwent skin prick and prick-to-prick-testing with different allergens, including zucchini, latex, and birch, ragweed, and grass pollen. Moreover a double-blind, placebo-controlled, food challenge was performed to confirm food allergy. Total and specific serum IgE levels were determined by using CAP-FEIA and the enzyme allergosorbent test method (EAST), respectively. Proteins from zucchini reacting with patient IgE were detected by means of immunoblotting. To characterize cross-reacting IgE antibodies, immunoblot- and EAST-inhibition assays were carried out. RESULTS: All patients in this study had positive reactions to zucchini both in prick-to-prick tests and double-blind, placebo-controlled, food challenges. Specific serum IgE levels to zucchini were found in all cases. In blot- and EAST-inhibition assays IgE from two patients revealed binding to zucchini profilin at about 15 kd. Furthermore, in two cases, including one of the profilin-positive patients, IgE directed against cross-reacting carbohydrate determinants was detected. For one patient, no cross-reacting IgE could be found, but IgE from this patient reacted strongly with a zucchini protein at 17 kd. CONCLUSIONS: We report the first 4 cases of food allergy to zucchini. Zucchini allergens can cause systemic reactions and are at least partially heat stable. We suggest that allergy to zucchini can occur as a result of primary sensitization to zucchini, as well as to cross-reactions to the panallergen profilin and cross-reacting carbohydrate determinants.

↩

[62] - Cuesta J, Blanco C, Fernández-Rivas M, Villalba M. Vegetalia. J Investig Allergol Clin Immunol 2006;16(Suppl. 2):40-44

↩

[63] - Asero R, Jimeno L, Barber D. Component-resolved diagnosis of plant food allergy by SPT. Eur Ann Allergy Clin Immunol 2008;40:115-121

BACKGROUND: Fruits and vegetables may contain both labile and stable allergens. The former induce only OAS, whereas stable allergens may induce systemic reactions. Component-resolved diagnosis (CRD) of allergy to plant foods is therefore essential for the clinical management of allergic patients. METHODS: 80 adults allergic to plant foods underwent SPT with purified natural date palm profilin (Pho d 2), purified Mal d 1, a peach extract containing uniquely LTP, and with a kiwi extract containing uniquely stable allergens. RESULTS: 58 (72%) patients were monosensitized: 24 to Mal d 1, 24 to profilin, 7 to LTP, and 3 to kiwi. 22 patients were multi-sensitised: 14 to Mal d 1 and profilin, 2 to Mal d 1 and kiwi, 1 to LTP and profilin, 3 to LTP and Mal d 1, and 2 to LTP, Mal d 1 and profilin. Mal d 1 and LTP sensitisation were associated with apple and peach allergy, respectively, whereas profilin sensitisation was associated with allergy to melon, watermelon, banana, tomato and citrus fruits. 18/21 kiwi-allergic patients were sensitised to one of the cross-reacting allergens, but 2/18 reacted to kiwi-specific allergens as well. CONCLUSIONS: In patients with allergy to plant-derived foods CRD can be performed by SPT with purified allergen proteins. In the future, the availability of a larger number of purified natural or recombinant allergens for SPT will represent a simple means to classify food-allergic patients properly on the first visit.

↩

Les allergènes des Cucurbitacées

Les réactivités croisées des Cucurbitacées et la question du latex

Pollinose et allergie aux Cucurbitacées

Cucurbitacées et syndrome LTP

Rubriques

Dans la même rubrique

Les agrumes

Les "fruits rouges"

Le raisin (et ses dérivés)

Les Liliacées

Les Astéracées (Lactucées, artichaut...)

Divers aliments végétaux

Les épices, herbes aromatiques et autres condiments