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R van Ree

Publications and source records attributed to R van Ree.

At least 19 recordsLinked to original sources
PubMed2006

Allergenicity assessment of apple cultivars: hurdles in quantifying labile fruit allergens.

BACKGROUND: Assessment of allergenicity of foods is important for allergic consumers and regulators. Immunoassays to measure major food allergens are widely applied, often giving variable results. Using the major apple allergen Mal d 1 as a model, we aimed to establish at the molecular level why different immunoassays for assessing allergenicity of apple cultivars produce conflicting outcomes. METHODS: Mal d 1 was measured in 53 cultivars from Italy and 35 from The Netherlands, using four different immunoassays. Purified Mal d 1 standards were molecularly characterized by size-exclusion chromatography (SEC) and mass spectrometry (MS). RESULTS: Three immunoassays using an identical standard gave similar results. Minor differences in sample preparation already resulted in significant loss of allergenicity. The fourth assay, using a different Mal d 1 standard, gave 10- to 100-fold lower outcomes. By SEC, this standard was shown to be almost fully aggregated. This aggregation was accompanied by a decrease of the mass of the Mal d 1 molecule by approximately 1 kDa as analyzed by MS. The deviating immunoassay was shown to selectively recognize this aggregated form of Mal d 1, whereas the other three assays, including the one based on IgE antibody recognition, preferentially bound non-aggregated allergen. CONCLUSIONS: Variable and poorly controllable major allergen modification in both extracts and standards hamper accurate allergenicity assessments of fruits.

Allergens↗
PubMed2006

Profiling preparations of recombinant birch pollen allergen Bet v 1a with capillary zone electrophoresis in pentamine modified fused-silica capillaries.

Three preparation batches of the recombinant birch pollen allergen Bet v 1a have been analyzed by capillary zone electrophoresis (CZE) using a separation electrolyte consisting of 100 mmol L(-1) phosphate at pH 6.50 with 2.0 mmol L(-1) tetraethylenepentamine (TEPA) added. TEPA improved the resolution by wall shielding and selective attachment to allergens, but reduced migration repeatability at concentrations >2.0 mmol L(-1). Heterogeneity of preparations determined by CZE and electrospray ionization-quadrupole-time-of flight-MS were in accordance and revealed chemically modified (carbamylated) allergens in one of the preparations. The method was validated according to the ICH-guidelines. Repeatability of effective electrophoretic mobility (mu(eff)) was <0.55% R.S.D. (n = 5). Migration time corrected peak areas were used for quantification. Limit of quantification (LOQ) was 25 microg mL(-1) for the major isoform Bet v 1a, based on a signal-to-noise ratio of 10, and detector response was linear between LOQ and 0.90 mg mL(-1). Purity of the different rBet v 1a preparations was determined to be between 40 and 92% depending on the manufacturing protocol.

Allergens↗
PubMed2006

The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area.

BACKGROUND: In contrast to other Rosaceae fruit, only few cases of patients with adverse reactions to strawberry are listed in literature. OBJECTIVE To identify allergenic proteins in strawberry and to express and characterize recombinant strawberry lipid transfer protein (LTP; rFra a 3). METHODS: Established apple-allergic patients were recruited on the basis of a reported allergic reaction to strawberry (n=28, confirmed by double-blind placebo-controlled food challenge in four patients) or on the basis of IgE reactivity to LTP (n=34). Sensitization to purified natural and recombinant allergens was assessed by RAST, immunoblot (inhibition) and basophil histamine release (BHR). A strawberry cDNA library was screened for genes homologous to known fruit allergens. Fra a 3 was cloned and expressed in the yeast Pichia pastoris and compared with peach and apple LTP by RAST, immunoblot-inhibition and BHR tests. RESULTS: Genes homologous to Bet v 1, Bet v 6, profilin and LTP were identified in a strawberry cDNA library. In BHR the rFra a 3 induced histamine release at a 100-fold higher concentration than peach LTP. RAST inhibition showed high cross-reactivity to peach and apple LTP, although IgE reactivity was lower by a factor 5. On strawberry immunoblot, patients' IgE showed reactivity to a Bet v 1 homologue, profilin, LTP and high-molecular weight bands. CONCLUSION: In addition to a Bet v 1 homologue, strawberry also contains IgE-binding profilin and LTP. The rFra a 3 has less allergenic potency than peach and apple LTP, and therefore is an interesting tool for future immunotherapy. Fra a 3 does not seem to be clinically relevant.

Allergens↗
PubMed2006

Characterization of recombinant Mal d 4 and its application for component-resolved diagnosis of apple allergy.

BACKGROUND: Profilins are ubiquitous panallergens that have been extensively characterized; yet, their clinical relevance is still unclear. OBJECTIVE: The aim of the present study was to produce recombinant apple profilin (rMal d 4) and to evaluate its allergenic activity and its potency for component-resolved allergy diagnosis. METHODS: Complementary DNA-derived Mal d 4 was cloned, expressed in Escherichia coli and subsequently purified via poly (l-proline) sepharose. A total of 28 sera from apple-allergic patients were used for IgE-ELISA, immunoblot, RAST and basophil histamine release (BHR) test. In addition, skin prick tests (SPTs) were performed in five patients. RESULTS: Four different complementary DNA coding for apple profilin, Mal d 4, each with an open reading frame of 393 nucleotides, were identified. One isoform Mal d 4.0101 was expressed in Escherichia coli and subsequently purified. Mass spectroscopy revealed the expected mass of 13.826 for rMal d 4.0101, and circular dichroism analysis data were typical for a folded protein and small-angle X-ray scattering measurement identified the protein as a monomer. All the serum samples displayed IgE binding to rMal d 4.0101 in IgE ELISA, immunoblot and RAST. In immunoblotting, IgE binding to natural Mal d 4 was partially/completely inhibited by preincubation with rMal d 4.0101, and RAST values to apple extract were significantly reduced upon serum pretreatment with rMal d 4.0101. SPTs and BHR assays using purified rMal d 4.0101 were positive. Purified rMal d 4.0101 was destroyed within seconds when subjected to pepsin digestion. CONCLUSIONS: Apple profilin complementary DNAs were identified. The physicochemical and allergenic properties of purified recombinant Mal d 4.0101 were evaluated showing that the recombinant protein was equal to the natural protein as shown by inhibition assays. Thus, Mal d 4 represents another example suitable for component-resolved diagnosis of food allergy.

Antigens, Plant↗
PubMed2006

Brassica oleracea pollen, a new source of occupational allergens.

BACKGROUND: Vegetable pollen is a rare source of occupational allergens. Occupational allergy has only been described in the case of paprika pollen and tomato pollen. We describe a new source of occupational pollen allergy. AIM: To study the incidence and the impact of broccoli and cauliflower pollen allergy in employees involved in classical plant breeding. METHODS: Fifty-four employees of five companies working with cauliflower (Brassica oleracea botrytis) and broccoli (B. oleracea italica/cymosa) pollen were eligible for complete evaluation. Allergy to cauliflower and broccoli pollen was evaluated by questionnaire and determination of sensitization by radioallergosorbent test (RAST) and skin-prick tests (SPT). SPT and RAST were performed with a panel of commercial and homemade extracts from cauliflower and broccoli pollen. RESULTS: Work-related symptoms such as rhinitis, conjunctivitis, asthma and urticaria caused by B. oleracea pollen were reported by 44% of the participants (24/54), of whom all but one had positive SPT for cauliflower- and/or broccoli-pollen/flower extracts and 58% (14/24) had positive RAST results. Symptoms had developed within the first 2 years in 33% of the patients. Six patients had to stop or change work. CONCLUSIONS: Brassica oleracea pollen is a new source of occupational allergen with strong allergenic potential leading to symptoms in almost half of the exposed employees.

Adult↗
PubMed2005

Component-resolved in vitro diagnosis in carrot allergy: does the use of recombinant carrot allergens improve the reliability of the diagnostic procedure?

BACKGROUND: In Europe, pollen-related food allergy is the most frequent form of food allergy in adults. Reliability of current diagnostic procedures, however, is poor and therapeutic options are not available. OBJECTIVES: In the present study, we created a panel of recombinant allergens from carrot and evaluated its potential in component-resolved in vitro diagnosis of carrot allergy. METHODS: Recombinant (r) Dau c 1.0104, Dau c 1.0201 and Dau c 4 were cloned by a polymerase chain reaction strategy, expressed in Escherichia coli and purified. Carrot lipid transfer protein (LTP) was expressed in the yeast Pichia pastoris. Sera from 40 carrot-allergic patients were investigated. Twenty-one birch pollen-allergic subjects with negative open provocation to carrot and 20 non-allergic subjects were included as controls. IgE binding to recombinant allergens as well as to cross-reactive carbohydrate determinants (CCD) was measured by ELISA. Cross-reactivity between Dau c 1 isoforms and Bet v 1 was assayed by ELISA inhibition. Biological activity of the recombinant carrot allergens was assessed by histamine release assay and peripheral blood mononuclear cells stimulation. RESULTS: Ninety-eight percent of the carrot-allergic patients were positive to at least one recombinant allergen; 98% reacted to rDau c 1.0104, 65% to rDau c 1.0201, 38% to rDau c 4 and 20% had IgE against CCD. Specificity using the recombinant allergens was high when compared with non-allergic controls, but low compared with birch-sensitized subjects without carrot allergy. Sensitization to Dau c 1.0201, however, proved to be highly specific for clinically relevant sensitization. Inhibition assays indicated the absence of LTP in carrot root extract, and epitope diversity between Dau c 1.0104, Dau c 1.0201 and Bet v 1. CONCLUSIONS: Our panel of recombinant allergens from carrot can provide a standardized tool for in vitro diagnosis of carrot allergy, and for epitope studies.

Adult↗
PubMed2005

A mutant of the major apple allergen, Mal d 1, demonstrating hypo-allergenicity in the target organ by double-blind placebo-controlled food challenge.

BACKGROUND: Allergen-specific immunotherapy for food allergy has been hindered by severe side-effects in the past. Well-characterized hypo-allergenic recombinant food allergens potentially offer a safe solution. OBJECTIVE: To demonstrate hypo-allergenicity of a mutated major food allergen from apple, Mal d 1, in vitro and in vivo. METHODS: A mutant of the major apple allergen, Mal d 1, was obtained by site-directed mutagenesis exchanging five amino acid residues. Fourteen patients with combined birch pollen-related apple allergy were included in the study. Hypo-allergenicity of the mutant rMal d 1 (rMal d 1mut) compared with rMal d 1 was assessed by in vitro methods, i.e. RAST (inhibition), immunoblotting and basophil histamine release (BHR) and in vivo by skin prick test and double-blind placebo-controlled food challenge (DBPCFC). RESULTS: RAST analysis (n = 14) revealed that IgE reactivity to rMal d 1mut was twofold lower than that of the wild-type molecule (95% confidence interval (CI): 1.7-2.4). RAST inhibition (n = 6) showed a 7.8-fold decrease in IgE-binding potency (95% CI: 3.0-12.6). In contrast to this moderate decrease in IgE-binding potency, the biological activity of rMal d 1mut assessed by SPT and BHR decreased 10-200-fold. Hypo-allergenicity was confirmed by DBPCFC (n = 2) with both recombinant molecules. CONCLUSION: A moderate decrease in IgE-binding potency translates into a potent inhibition of biological activity. This is the first study that confirms by DBPCFC that a mutated recombinant major food allergen is clinically hypo-allergenic. This paves the way towards safer immunotherapy for the treatment of food-allergic patients.

Adolescent↗
PubMed2005

The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3.

BACKGROUND: Non-specific lipid transfer proteins (LTPs) are involved in allergy to fresh and processed fruits. We have investigated the effect of thermal treatment and glycation on the physico-chemical and IgE-binding properties of the LTP from apple (Mal d 3). METHODS: Mal d 3 was purified from apple peel and the effect of heating in the absence and presence of glucose investigated by CD spectroscopy, electrospray and MALDI-TOF mass spectrometry. IgE reactivity was determined by RAST and immunoblot inhibition, SPT and basophil histamine release test. RESULTS: The identity and IgE reactivity of purified Mal d 3 was confirmed. Mild heat treatment (90 degrees C, 20 min) in the absence or presence of glucose did not alter its IgE reactivity. More severe heat treatment (100 degrees C, 2 h) induced minor changes in protein structure, but a significant decrease in IgE-binding (30-fold) and biological activity (100- to 1000-fold). Addition of glucose resulted in up to four glucose residues attached to Mal d 3 and only a 2- and 10-fold decrease of IgE-binding and biological activity, respectively. CONCLUSIONS: Only severe heat treatment caused a significant decrease in the allergenicity of Mal d 3 but glycation had a protective effect. The presence of sugars in fruits may contribute to the thermostability of the allergenic activity of LTP in heat-processed foods.

Allergens↗
PubMed2005

Allergy vaccines: a need for standardisation in mass units of major allergen.

Treatment of respiratory allergies can be performed with allergen-specific immunotherapy using allergen extracts. These products are biologicals with an extremely complex and variable composition. Only a few components are of major importance for the disease, the so-called major allergens. At present, standardisation of allergen extracts is dominated by techniques that aim at establishing their overall IgE-binding potencies using pooled sera of allergic patients. Each company in the market uses its own type of units to express potencies, thus hampering comparability. Another disadvantage is that the major allergen composition is not determined. Most companies have introduced assays for the measurement of major allergens in their quality control systems, but these data are not yet used for labelling purposes. The need to include major allergen content in standardisation protocols is now widely accepted. To support future labelling on the basis of major allergen content the European Union has funded the multidisciplinary multicentre project CREATE. This project aims at developing international certified references for the most important major respiratory allergens and at evaluating the performance of available ELISA for their measurement. The project will facilitate expression of potencies by active ingredient (major allergen) content and will allow direct comparison of competitor products.

Allergens↗
PubMed2004

Severe allergy to sharon fruit caused by birch pollen.

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

Adult↗
PubMed2004

Efficacy of birch-pollen immunotherapy on cross-reactive food allergy confirmed by skin tests and double-blind food challenges.

BACKGROUND: The effect of birch-pollen immunotherapy (IT) on cross-reactive food allergies is controversial. OBJECTIVE: The aim of this study was to investigate the effect of birch-pollen IT on apple allergy and to evaluate recombinant allergens and double-blind placebo-controlled food challenges (DBPCFCs) as monitoring tools. METHODS: Twenty-five adult birch-pollen- and apple-allergic patients were randomly divided into two groups, either receiving birch-pollen IT or symptomatic drugs only. IgE and IgG4 antibodies against birch pollen, apple, natural Bet v 1 and Mal d 1 were measured. In addition, skin prick tests (SPT) were performed using recombinant Bet v 1 (rBet v 1) and Mal d 1 (rMal d 1). Clinical outcome was evaluated by DBPCFC. CD4(+)CD25(+) regulatory T cells (Tregs) were isolated from peripheral blood and tested in functional assays. RESULTS: Birch-pollen IT resulted in a significant decrease of SPT reactivity for rBet v 1 (30-fold) and rMal d 1 (10-fold) already after 3 months. IgG4 antibodies were potently induced against Bet v 1, displaying cross-reactivity to Mal d 1. Visual analogue scale scores decreased >10-fold in 9/13 patients of the IT group, with three patients converting to negative. In the control group, no decrease was observed. Birch-pollen IT did not lead to detectable changes in the number or function of the CD4(+)CD25(+) Tregs. CONCLUSIONS: This trial supports the claims that birch-pollen IT also decreases allergy to foods containing Bet v 1-homologous allergens. Recombinant allergens and DBPCFCs have proven to be useful tools for monitoring the effect of birch-pollen IT on linked food allergies.

Adult↗
PubMed2003

Oral allergy syndrome to chicory associated with birch pollen allergy.

BACKGROUND: A few cases of IgE-mediated chicory allergy with oral, cutaneous, and/or respiratory symptoms are reported. We present 4 patients with inhalant birch pollen allergy and oral allergy syndrome to chicory. IgE-binding proteins in chicory and cross-reactivity with birch pollen were studied. METHODS: Chicory extract was prepared and immunoblotting was used to study IgE reactivity and cross-reactions with birch pollen. RESULTS: The pattern of IgE binding to chicory was variable among the patients, with protein bands recognized at 18, 21, 40, 52 and 71 kD. Bet v 1-like proteins were detected in chicory by monoclonal antibody binding. Chicory-birch pollen cross-reactivity, as studied in 2 patients from whom enough serum was available, could be demonstrated but did not involve the Bet v 1 protein family. In one of these cases, a 51-kD protein of birch pollen was found to be responsible for cross-reactivity. CONCLUSIONS: Chicory should be added to the list of foods that can cross-react with birch pollen and cause the birch pollen-associated oral allergy syndrome.

Adult↗
PubMed2002

Immunological cross-reactivity between lipid transfer proteins from botanically unrelated plant-derived foods: a clinical study.

BACKGROUND: Lipid transfer proteins (LTP) are highly conserved and widely distributed throughout the plant kingdom. Recent studies demonstrated immunological cross-reactivity between LTP from many botanically unrelated fruits and vegetables and concluded that LTP are pan-allergens. This study aimed to evaluate the clinical relevance of such cross-reactivity in a group of subjects monosensitized to LTP. METHODS: Twenty LTP-hypersensitive patients were selected from a population of about 600 subjects with history of Rosaceae allergy by means of: 1) negative skin prick test (SPT) with a commercial birch pollen extract; 2) positive SPT with a commercial plum extract, rich in LTP but virtually lacking both Bet v 1-like proteins and profilin; 3) in-vitro IgE reactivity to the 9-10 kDa fraction of peach peel or immunoblot with peach peel showing a single band at 10 kDa; and 4) total inhibition of reactivity to whole peach extract (containing Bet v 1-related allergen, profilin, and LTP) by purified peach LTP on enzyme-linked immunoassay (ELISA). Allergy to foods other than Rosaceae was ascertained by careful interview and analysis of medical recordings. SPT with a large series of plant-derived foods were carried out as well. The cross reactivity between LTPs from botanically unrelated plant-derived foods was assessed by ELISA inhibition tests using walnut and peanut extracts as substrate, and peach LTP as inhibitor. RESULTS: All patients reported allergic reactions after the ingestion of at least one from a large number of vegetable foods other than Rosaceae, and in several cases clinical reactions were very severe (anaphylaxis, asthma, urticaria/angioedema). Nuts and peanuts were the most frequently reported causes of allergic reactions (80% and 40% of patients, respectively). All patients showed positive SPT to several non-Rosaceae food extracts. SPT with nuts, peanut, legumes, celery, rice, and corn were positive in the majority of patients. In ELISA inhibition studies, absorption of sera with peach LTP caused complete inhibition of IgE reactivity to walnut and peanut in all cases. CONCLUSION: LTP is a clinically relevant pan-allergen. Most Rosaceae-allergic, LTP-hypersensitive patients experience adverse reactions after ingestion of botanically unrelated plant-derived foods as well. In view of the high prevalence and severity of the allergic reactions induced, hazelnut, walnut, and peanut should be regarded as potentially hazardous for these patients.

Allergens↗
PubMed2002

Clinical importance of non-specific lipid transfer proteins as food allergens.

Non-specific lipid transfer proteins (nsLTPs) have recently been identified as plant food allergens. They are good examples of true food allergens, in the sense that they are capable of sensitizing, i.e. inducing specific IgE, as well as of eliciting severe symptoms. This is in contrast with most plant food allergens, which are recognized because of primary sensitization to related inhalant allergens (cross-reactivity), i.e. pollen allergens. The basis of the difference between the latter category and strong food allergens such as nsLTPs appears to lie in the sensitivity of the allergens to proteolytic attack and food processing. Stability allows the allergen to reach the gastrointestinal immune system in an immunogenic and allergenic conformation, allowing sensitization and induction of systemic symptoms. Stability also explains the presence of such allergens in processed foods. Together, these characteristics make nsLTPs clinically highly relevant plant food allergens and ideal tools with which to study the mechanisms involved in food allergy.

Allergens↗
PubMed2002

The range of minimum provoking doses in hazelnut-allergic patients as determined by double-blind, placebo-controlled food challenges.

BACKGROUND: The risk for allergic reactions depends on the sensitivity of individuals and the quantities of offending food ingested. The sensitivity varies among allergic individuals, as does the threshold dose of a food allergen capable of inducing an allergic reaction. OBJECTIVE: This study aimed at determining the distribution of minimum provoking doses of hazelnut in a hazelnut-allergic population. METHODS: Thirty-one patients with a history of hazelnut-related allergic symptoms, a positive skin prick test to hazelnut and/or an elevated specific IgE level, were included. Double-blind, placebo-controlled food challenges (DBPCFC) were performed with seven increasing doses of dried hazelnut (1 mg to 1 g hazelnut protein) randomly interspersed with seven placebo doses. RESULTS: Twenty-nine patients had a positive challenge. Itching of the oral cavity and/or lips was the first symptom in all cases. Additional gastrointestinal symptoms were reported in five patients and difficulty in swallowing in one patient. Lip swelling was observed in two patients, followed by generalized urticaria in one of these. Threshold doses for eliciting subjective reactions varied from a dose of 1 mg up to 100 mg hazelnut protein (equivalent to 6.4-640 mg hazelnut meal). Extrapolation of the dose-response curve showed that 50% of our hazelnut-allergic population will suffer from an allergic reaction after ingestion of 6 mg (95% CI, 2-11 mg) of hazelnut protein. Objective symptoms were observed in two patients after 1 and 1,000 mg, respectively. CONCLUSION: DBPCFCs demonstrated threshold doses in half of the hazelnut-allergic patients similar to doses previously described to be hidden in consumer products. This stresses the need for careful labelling and strategies to prevent and detect contamination of food products with hazelnut residues.

Adolescent↗
PubMed2001

A case of allergy to beer showing cross-reactivity between lipid transfer proteins.

BACKGROUND: Lipid transfer proteins (LTPs) are highly conserved proteins present in a broad spectrum of fruits and vegetables that might represent a novel plant panallergen. OBJECTIVE: To demonstrate that LTP is an important allergen in beer and that beer LTP cross-reacts with LTP from botanically unrelated plant-derived foods. METHODS: Serum from a patient with clinical allergy to both beer and Rosaceae was studied for IgE reactivity to LTP to several vegetable foods by RAST, ELISA, immunoblot, and inhibition studies. RESULTS: Patient's serum showed a strong IgE reactivity to LTP purified from peach peel, carrot, and broccoli, and to a 10 kD protein in both apple and peach immunoblots, whereas no reactivity to birch cross-reactive allergens such as Bet v 1, profilin, or carbohydrates was found. In inhibition studies, preabsorption of serum with apple, walnut, hazelnut, peanut, corn, and rice caused a fall of 97%, 20%, 66%, 91%, 94%, and 93%, respectively, of its reactivity to peach LTP. Beer RAST fell from 1.8 IU/mL to <0.1 IU/mL when a patient's serum was preabsorbed with recombinant carrot LTP. CONCLUSIONS: LTP is a relevant allergen in beer. Beer LTP may cross-react with LTP from several other plant-derived foods.

Adult↗