Shrimp Allergic Patients Research Articles

Is mealworm or shrimp allergy indicative for food allergy to insects?

The growing world population is a key driver for the exploration of sustainable protein sources to ensure food security. Mealworm and other insects are promising candidates. Previously we found that shrimp allergic patients are at risk for mealworm allergy, and that mealworm can induce a primary allergy . This study set out to investigate the allergenic potential of edible insects, suggested for human consumption by agencies such as WHO/FAO, in both the shrimp (potentially cross-reactive) and primary mealworm allergic population. The following insects were studied: mealworm, house cricket, giant mealworm, lesser mealworm, African grasshopper, large wax moth, and black soldier fly. Fifteen shrimp (mealworm sensitized or allergic) patients and four primary mealworm allergic subjects, who participated in previous studies, were included. All shrimp allergic patients were sensitized to multiple insects with similar response profiles for all insects tested. Primary mealworm allergic patients, showed IgE binding to proteins from only a few insects on immunoblot, although basophil activation test was positive for all tested insects. Shrimp allergic patients are most likely at risk of food allergy to mealworm and other insects. Primary mealworm allergy does not mean subjects are likely to react to all insects.

Shrimp Allergy: Analysis of Commercially Available Extracts for In Vivo Diagnosis.

Skin prick testing (SPT) with commercial extracts is the first step in the diagnosis of shrimp allergy, although its clinical efficiency is unknown. Objective: To analyze the clinical usefulness of all commercial crustacean extracts available for SPT in Italy. We performed a multicenter study of 157 shrimp-allergic patients who underwent SPT with 5 commercial crustacean extracts and with house dust mite (HDM) extract. Commercial extracts were analyzed using SDS-PAGE and compared with a freshly prepared in-house shrimp extract. IgE to Pen a 1/Pen m 1, Pen m 2, and Pen m 4 was determined, and immunoblot analysis was performed on a large number of sera. The skin reactions caused by commercial crustacean extracts were extremely heterogeneous, resulting in 32 clinical profiles, with marked differences in protein content and missing proteins at molecular weights corresponding to those of major shrimp allergens. Only strong Pen a 1/Pen m 1 reactors reacted to both HDM and all 5 commercial extracts in SPT. Most patients, including those who were tropomyosin-negative, reacted to HDM. Patients reacted to a large and variable array of proteins, and IgE reactivity was common at high molecular weights (>50 kDa). The in vivo diagnosis of shrimp allergy must continue to be based on SPT with fresh material. Shrimp-allergic patients frequently react to a number of ill-defined high-molecular-weight allergens, thus leaving currently available materials for component-resolved diagnosis largely insufficient. Mites and crustaceans probably share several allergens other than tropomyosin.

High rate of house dust mite sensitization in a shrimp allergic southern Ontario population

BackgroundShrimp and house dust mite (HDM) allergies are common in Canadians. Often, both of these allergies occur in the same patient. This may be due to homology of tropomyosin or other potentially shared proteins. The aim of our study was to assess the frequency of house dust mite sensitization in a shrimp allergic Canadian population.MethodsWe undertook a retrospective chart review of shrimp allergic patients at an outpatient allergy clinic in Kitchener, Ontario, Canada. Our primary endpoint was to assess for presence of HDM sensitization in this population. Patients were categorized into approximate quartiles. We assessed the severity of the shrimp reactions, correlated shrimp skin test size to HDM skin test size, and measured the proportion of patients with atopic symptoms.ResultsWe identified 95 shrimp allergic patients who were tested for house dust mite. 86 (90.5%) of these patients had a positive skin test to HDM. Patients with a shrimp skin test ≥5 mm were 5.31 times (95% CI, 1.55–18.14; p = 0.008) more likely to exhibit a dust mite skin test ≥5 mm than patients with a shrimp skin test <5 mm. The odds of a patient with a shrimp skin test between 10 and 18 mm having a larger HDM skin test were 3.93 times (95% CI 1.03–14.98, p = 0.045) the odds for a patient with a shrimp skin test size between 3 and 4 mm. We did not find a correlation between shrimp skin test size and shrimp reaction symptom grade (p = 0.301).ConclusionIn our Canadian patients, we found a large majority of shrimp allergic patients to be sensitized to HDM. We found that patients with a large skin test to shrimp were more likely to have a large skin test to HDM compared to those patients with a small skin test to shrimp. We did not find a correlation between shrimp skin test size and shrimp reaction symptom severity. Most of these patients had symptoms of rhinitis and/or asthma that may have been caused by house dust mite allergy.

Safety of chitosan processed wine in shrimp allergic patients

Safety of chitosan processed wine in shrimp allergic patients

Majority of shrimp-allergic patients are allergic to mealworm

Majority of shrimp-allergic patients are allergic to mealworm

Shellfish and House Dust Mite Allergies: Is the Link Tropomyosin?

Crustacean shellfish allergy is an important cause of food allergy and anaphylaxis in Asia. The major allergen in shellfish allergy is tropomyosin, a pan-allergen that is also found in house dust mites and cockroaches. Tropomyosins from house dust mites (HDMs) have a high sequence homology to shellfish tropomyosins, and cross-reactivity between HDM and shrimp tropomyosins has been demonstrated. Exposure to inhaled tropomyosins from house dust mites has been postulated to be the primary sensitizer for shellfish allergy, in a reaction analogous to the oral allergy (inhalant-food) syndrome. This notion is supported by indirect data from the effects of HDM immunotherapy on shellfish allergy, and strong correlations of shellfish and HDM sensitization. HDM immunotherapy has been reported to induce both shrimp allergy in non-allergic patients and shrimp tolerance in shrimp-allergic patients. Epidemiological surveys have also demonstrated a strong correlation between shellfish and HDM sensitization in both hospital-based and community-based studies. Unexposed populations have also been shown to develop sensitization-shellfish sensitization in orthodox Jews with no history of shellfish consumption was associated with HDM sensitization. Reciprocally, HDM sensitization in an Icelandic population living in a HDM-free environment was associated with shrimp sensitization. In vitro IgE inhibition studies on sera in shrimp-allergic Spanish patients indicate that mites are the primary sensitizer in shrimp-allergic patients living in humid and warm climates. Current data supports the hypothesis that tropomyosin is the link between HDM and shellfish allergies. The role of tropomyosin in HDM and shellfish allergies is a fertile field for investigation as it may provide novel immunotherapeutic strategies for shellfish allergy.

Effect of thermal processing on mealworm allergenicity.

The growing world population requires the exploration of new sustainable protein sources to ensure food security. Insects such as mealworm are promising candidates. For safety reasons, a risk assessment, including allergy risks, is needed. Since allergenicity can be influenced by thermal processing, it is highly important to take this into account. Fresh mealworm was heat processed and extracted by a sequential extraction method using in succession Tris, urea, and a combined SDS/DTT buffer. Extracts were tested using immunoblot, basophil activation test and skin prick test in 15 shrimp allergic patients, previously indicated as population at risk for mealworm allergy. Immunoblots showed a difference in IgE binding between processed and unprocessed mealworm extracts. However, this was due to change in solubility. Some allergens were soluble in urea buffer, but became more soluble in Tris buffer and vice versa. IgE binding was seen for all extracts in blot and basophil activation test. The results from 13 skin prick tests showed a skin reaction similar between processed and unprocessed mealworm. Thermal processing did not lower allergenicity but clearly changed solubility of mealworm allergens. A sequential extraction method allowed for assessment of a broader protein panel.

Digestibility and Immunoreactivity of Shrimp Extracts Using an In Vitro Digestibility Model with Pepsin and Pancreatin.

Shellfish allergy affects 2% of the adult population in the United States. Identification of allergenic shrimp proteins is needed for improved management and assessment of shrimp allergy. We determined the temporal pepsin and pancreatin stability of total shrimp proteins using simulated physiological digestive conditions in vitro. Gel electrophoresis was used to determine protein stability, whereas immunoreactivity of protease stable proteins was determined using rabbit antigen-specific antibodies. Potential allergenicity of protease stable proteins was determined utilizing human sera from shrimp allergic patients. Total shrimp myofibrillar proteins were pepsin- and pancreatin-stable for up to 1 h after initiating digestion, whereas only pancreatin-stable total shrimp proteins were Immunoglobulin G (IgG) immunoreactive. However, shrimp proteins of 32 and 25 kDa were pepsin and/or pancreatin stable and Immunoglobulin E (IgE) reactive, denoting the stability and potential allergenicity. These findings suggest that this in vitro digestibility model may be useful for the identification of shrimp allergenic proteins that are more resistant to physiologic digestive conditions and may elicit an immunologic response in vivo. Unlike other food allergies, shellfish allergy is typically life-long and predominantly affects the adult population. A major difficulty in managing shellfish allergy is the lack of reliable diagnostic assays due to limited knowledge of clinically relevant shellfish allergens. Therefore, the identification and characterization of digestive-stable and immunoreactive food proteins is fundamental to the development of new polyclonal antibodies for improved food allergen detection methods within the food industry.

Shrimp allergic patients are at risk when eating mealworm proteins

Due to the imminent growth of the world population, shortage of protein sources for human consumption will arise in the near future. Alternative and sustainable protein sources like insects, such as mealworm, are now being explored for the production of food and feed. Before novel products can be launched on the market the assessment of food safety is vital. One of the key aspects of food safety is the risk of the development of food allergy. Food allergies specifically have a significant impact on the quality of life of allergic patients and their daily functioning, and they may even be life-threatening. TNO together with the University Medical Center Utrecht (UMCU) developed a risk assessment strategy to assess the allergenicity of novel proteins, in accordance to the European Food Safety Authority (EFSA) guidelines to assess the safety of Genetic modified organisms. Using this strategy the safety of mealworm (Tenebrio molitor L.) proteins for use in human consumption was assessed. In this study, 15 shrimp allergic patients were tested on their allergic reaction to mealworm proteins. For this purpose different in vivo (skin prick tests) and in vitro tests (immune blot and basophil activation) were used. In all tests a positive reaction to mealworm extracts was seen. This indicates that shrimp allergic patients are at risk for developing allergic reactions when consuming food containing mealworm proteins. Double blind placebo controlled food challenge will have to confirm this in the coming months.

A Sensitive Immunoassay for Invertebrate Tropomyosin Allergens in Foods, Inhalants, Ticks and Worms

T U E S D A Y 802 Predicting Shrimp Allergy Using Skin Prick Test, Specific IgE to Shrimp and Rpen a1 in Area with High Prevalence of House Dust Mite Sensitization Jaichat Mekaroonkamol, MD, Pantipa Chatchatee, MD, Jarungchit Ngamphaiboon, MD, Piyawadee Lertchanaruengrith, MD, Narissara Suratannon, MD; King Chulalongkorn Memorial Hospital, Bangkok, Thailand, Division of Allergy and Immunology, Department of Pediatrics, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand. RATIONALE: In areas with high HDM exposure and high shrimp consumption, diagnosis of shrimp allergy is a clinical challenge since sensitization to both allergens frequently occurs. The aim of this study was to evaluate role of skin prick test(SPT), specific IgE(sIgE) to shrimp and rPena1 in the diagnosis of shrimp allergy in area with high prevalence of HDM sensitization. METHODS: Fifty-one participants with sensitization to both shrimp and Dermatophagoides pteronyssinus(Derp) as demonstrated by SPT were enrolled. Clinical reactions to shrimp were determined. SIgE to Der p, shrimp and rPen a1 were analyzed. RESULTS: Patients were divided into 2 groups; shrimp allergy(n522) and shrimp tolerance(n529). About half (54%) of shrimp allergic patients had anaphylaxis while 30 % had only oral allergy syndrome. Compared to shrimp tolerant subjects, shrimp allergic subjects had significant larger SPT wheal size(7vs4.5 mm,p50.003) and higher sIgE levels to shrimp(2.36vs0.21 kUA/l,p 3.5 mm or positive shrimp sIgE(>0.35 kUA/) provided 90% sensitivity and negative predictive value of 0.86. SIgE to rPen a1 had low sensitivity(45%) but high specificity(85%) and positive predictive value of 0.71 with the cut-off level of 0.35 kUA/L. Size of SPT, levels of shrimp sIgE and sIgE to rPena1 did not differ between anaphylactic and non-anaphylactic patients. CONCLUSIONS: In double sensitized patients with unclear clinical reaction to shrimp, SPT and sIgE to shrimp can be used as screening tests while sIgE to rPen a1 adds diagnostic value for predicting clinical reaction. SIgE to rPen a1 is not a severity marker of shrimp allergy in our population.

Identification of a novel allergen from muscle and various organs in banana shrimp (Fenneropenaeus merguiensis)

BackgroundThe increasing consumption of shellfish can cause an increase in allergic symptoms. Shrimp allergy can be species specific, but specific allergies in different organs have not been studied. Identification of allergens in muscle and others organs of banana shrimp is necessary for improved diagnostics of allergies for shrimp and food safety control. ObjectiveTo identify the IgE-binding proteins in various organs of Fenneropenaeus merguiensis by immunoblotting and tandem mass spectrometry. MethodsProteomic methods were used to investigate the allergenic proteins from banana shrimp. Proteins from muscle and various organs were separated by denaturing polyacrylamide gel electrophoresis. Allergens were analyzed by immunoblotting with pooled sera from shrimp allergic patients (n = 21) and tandem mass spectrometry. ResultsThe important allergens in banana shrimp are arginine kinase, sarcoplasmic calcium-binding protein, myosin heavy chain, hemocyanin, enolase, and glyceraldehyde-3-phosphate dehydrogenase, which can be demonstrated by immunoblotting in muscle and shell. Moreover, vitellogenin, ovarian peritrophin 1 precursor, β-actin, and 14-3-3 protein were suggested as allergens in the ovary at different stages of ovarian development. ConclusionTen allergens were identified as allergens in various organs, and they are suggested as novel allergens in banana shrimp. The major allergen in muscle and shell from this shrimp is arginine kinase, whereas the major allergen in the ovary is vitellogenin.

Identification and validation of shrimp-tropomyosin specific CD4 T cell epitopes

BackgroundShellfish allergy is an immune-mediated adverse reaction to allergenic shellfish and is responsible for significant morbidity and mortality. CD4 T cell responses play an important role in the pathophysiological mechanisms of sensitization and in production of IgE. ObjectiveWe sought to identify and validate CD4 T cell shrimp tropomyosin-derived epitopes and characterize CD4 T cell responses in subjects with a clinical history of shellfish allergy. MethodUsing an in vitro MHC-peptide binding assay, we screened 91 overlapping peptides and identified 28 epitopes with moderate and strong binding capacities; 3 additional peptides were included based on MHC binding prediction score. These peptides were then examined in proliferation and cytokine release assays with T cells from allergic subjects. Result17 epitopes restricted to DRB∗01:01, DRB1∗03:01, DRB1∗04:01, DRB1∗09:01, DQB1∗02:01, DQB1∗03:02 and DQB1∗05:01 alleles were identified and validated by both the MHC binding and the functional assays. Two peptides showed specificities to more than one MHC class II allele. We demonstrated that these peptides exert functional responses in an epitope specific manner, eliciting predominantly IL-6 and IL-13. ConclusionThe identified epitopes are specific to common MHC class II alleles in the general population. Our study provides important data for the design of peptide-based immunotherapy of shrimp-allergic patients.

Penaeus monodon tropomyosin induces CD4 T-cell proliferation in shrimp-allergic patients

Shellfish allergy affects approximately 2% of the population and can cause immediate hypersensitivity reactions such as urticaria, swelling, difficulty breathing, and, in some cases, anaphylaxis. Tropomyosin is the major shrimp allergen and binds IgE in two-thirds of patients. A total of 38 shrimp-allergic patients and 20 negative control subjects were recruited and evaluated on the basis of history, skin prick testing, specific immunoglobulin E (IgE) levels, and peripheral blood mononuclear cell proliferation in response to shrimp tropomyosin or shrimp tropomyosin-derived peptides. Of the classically allergic patients by history, 59% tested positive for serum shrimp IgE antibodies. Of patients with shrimp-specific IgE in sera, 70% also had significant IgE levels specific for shrimp tropomyosin. Peripheral blood mononuclear cells from classically shrimp-allergic patients proliferated in a dose-dependent manner in response to to tropomyosin. In addition, a T-cell line derived from a shrimp-allergic patient proliferated specifically in response to tropomyosin-derived peptides. These studies suggest a strategy for immunotherapy using a tropomyosin-derived T-cell epitope vaccination.

Shrimp Allergy in Italian Adults: A Multicenter Study Showing a High Prevalence of Sensitivity to Novel High Molecular Weight Allergens

Background: Shrimp is a frequent cause of food allergy worldwide. Besides tropomyosin, several allergens have been described recently. Objective: We investigated which allergens are involved in Italian shrimp-allergic adults. Methods: Sera from 116 shrimp-allergic patients selected in 14 Italian allergy centers were studied. Skin prick tests with house dust mite (HDM) as well as measurements of IgE to Pen a 1 (shrimp tropomyosin) and whole shrimp extract were performed. All sera underwent shrimp immunoblot analysis, and inhibition experiments using HDM extract as inhibitor were carried out on some Pen a 1-negative sera. Results: Immunoblots showed much variability. IgE reactivity at about 30 kDa (tropomyosin) was found in <50% of cases, and reactivity at about 67 kDa and >90 kDa was frequent. Further reactivities at 14–18, 25, 43–50, about 60 and about 80 kDa were detected. Most subjects had a history of shrimp-induced systemic symptoms irrespective of the relevant allergen protein. IgE to Pen a 1 were detected in sera from 46 (41%) patients. Skin reactivity to HDM was found in 43/61 (70%) Pen 1-negative subjects and inhibition studies showed that pre-adsorption of sera with HDM extract induced a marked weakening of the signal at >67 kDa. Conclusions: Several allergens other than tropomyosin are involved in shrimp allergy in adult Italian patients. Some hitherto not described high molecular weight allergens seem particularly relevant in this population and their cross-reactivity with HDM allergens makes them novel potential panallergens of invertebrates.

Tropomyosin IgE-positive results are a good predictor of shrimp allergy

Shrimp is a common cause of food allergy. Our aims were to determine the value of IgE antibodies in the diagnosis of shrimp allergy and to study red shrimp (Solenocera melantho) tropomyosin both as a new allergen and as a cross-reactive IgE-binding protein. We have studied 45 subjects. Skin prick test (SPT) was carried out in all subjects, and specific IgE (sIgE) to shrimp, recombinant and natural shrimp tropomyosins rPen a 1 and nPen m 1, recombinant Der p 10, and Dermatophagoides pteronyssinus was assessed by fluoroimmunoassay and/or immunoblotting. Double-blind, placebo-controlled food challenges were carried out to confirm diagnosis of shrimp allergy. Also, in vitro inhibition tests were performed to evaluate cross-reactivity. Shrimp allergy was confirmed in 18 shrimp-allergic patients. Skin prick test and IgE antibodies to shrimp were positive in all shrimp-allergic patients; sIgE to rPen a 1 was detected in 98% of these patients. Of the 18 shrimp-tolerant patients, 61% had positive SPT to shrimp, 55% were IgE-positive to shrimp, and 33% showed IgE antibodies to rPen a 1. Determination of IgE to rPen a 1 yielded a positive predictive value of 0.72 and a negative predictive value of 0.91. IgE levels to rPen a 1 provided additional value to the diagnosis of shrimp allergy. Some allergens in mite extract are recognized by patients who are allergic to shrimp, though their clinical relevance remains unknown.

Causes of Food-Induced Anaphylaxis in Italian Adults: A Multi-Centre Study

Background: Data about food-induced anaphylaxis in Italy are missing. Objective: It was the aim of this study to detect the main foods/food allergens causing anaphylaxis in Italy. Methods: The frequency of anaphylaxis and the relative importance of many offending foods were assessed in 1,110 adult patients with food allergy diagnosed by common criteria at 19 allergy centres scattered throughout Italy from 1 January to 31 December 2007. Results: Fifty-eight of 1,110 (5%) food-allergic patients experienced at least 1 episode of anaphylaxis. On average, they were older than other food-allergic patients (34 vs. 31 years; p < 0.05). The majority of anaphylactic episodes occurred in patients sensitized to lipid transfer protein (LTP; n = 19), followed by shrimp (n = 10), tree nuts (n = 9), legumes other than peanut (n = 4), and seeds (n = 2); peanut, spinach, celery, buckwheat, wheat, avocado, tomato, fish, meat, and Anisakis caused an anaphylactic reaction in single patients. Among LTP-hypersensitive patients, peach caused 13/19 anaphylactic episodes. Shrimp-allergic patients were significantly older than other patients with food-induced anaphylaxis (p < 0.05), whereas patients allergic to LTP experienced their anaphylactic episodes at a younger age (p < 0.001). The frequency of anaphylaxis among patients sensitized to LTP, shrimp or tree nuts did not differ between northern and central/southern Italy. Conclusion: LTP is the most important allergen causing food-induced anaphylaxis in Italy, peach being the most frequently offending food. Peanut-induced anaphylaxis seems very uncommon. Geographic and environmental differences both between Italy and other countries and within Italy seem to play a relevant role in the pattern of sensitization to foods.

Allergènes de poissons et crustacés

Concerning fish allergy, the major allergens are the β isoforms of muscle parvalbumins. Fish parvalbumins share among themselves important homologies in amino acid composition, which gives rise to extensive cross-sensitizations. Allergic cross-reactions with frog parvalbumin have been described. Due to the frequent sensitization to parvalbumins, the role of other allergens is masked. Allergy to fish gelatin has been reported. Additional muscle allergens have been incompletely described, but their exact role remains to be defined. With respect to shellfish allergy, muscle tropomyosin is the major allergen. Tropomyosins give rise to important cross-sensitization between shellfish, but also with gastropods, mites, cockroaches and other arthropods. The myosin light chain has been shown to be an allergen in 60% of white shrimp-allergic patients. A muscle arginine kinase has been recognized as an allergen in a third of patients sensitized to black tiger shrimp. A sarcoplasmic calcium-binding protein of the same tiger shrimp is recognized by IgE antibodies of 60% of shrimp-allergic patients.

Allergy To Shrimp: A Double Blind, Placebo-controlled, Food Challenge Study And Allergens Implicated In Spain.

RATIONALE: Our study aimed to investigate clinical characteristics and allergens recognized by patients with suspected shrimp allergy. METHODS: We studied 35 patients with suspected allergic reactions to shrimp, mostly urticaria. In all patients double-blind placebo controlled oral challenge (DBPCOC) was performed. Prick-by-prick tests and serum specific IgE (CAP system) with mites, anisakis, mosquito, cockroach, shrimp, clam, snail, mussel, scallop, cockle, squid, octopus and cuttlefish were performed as well as IgE to rPen a1 (tropomyosin). All patient's sera were tested individually by IgE immunodetection after SDS-PAGE with shrimp crude extract. Seven patients sensitized to mites and with good tolerance to shrimp were included as controls. RESULTS: 20 (57%) patients were considered allergic (14 + DBPCOC and 6 anaphylaxis). Specific IgE was positive to all of extracts tested by CAP, except in 2 patients. 17 were sensitized to mites. All but 2 had specific IgE to tropomyosin, in 1 only detected by immunoblotting. In patients with negative DBPCOC, 5 had specific IgE to other seafood and 10 to mites. In the control group all CAP determinations were negative except in one patient who had specific IgE to shrimp and other patient a 37 kDa IgE-binding band. Immunoblots demonstrated several IgE binding-bands. The main bands were of 37 and 20 kDa in 12 allergic patients. These bands were also detected in 3 patients with negative DBPCOC. CONCLUSIONS: This study shows the need to perform food challenges for a correct diagnosis. Tropomyosin seems the major allergen in shrimp allergic patients in Spain, although, other allergens may be implicated.

CD4 T-Cell Cytokine Response to Mite Recombinant Tropomyosin in Mite, Snail and Shrimp Allergic Patients

Allergies to snails and mites are definitely linked. Snail allergens have been already identified and there is no evidence of crossreaction between snail and mite tropomyosin. This work is a preliminary study on immune cell function, evaluating possible tropomyosin-triggering in a snail-mite-shrimp cross-reaction. Peripheral blood mononuclear cells from 6 different phenotype patients in relation to snails, mites and crustaceans, were cultured with mite recombinant tropomyosin (rDer p 10), anti-CD28 and brefeldin A. Phytohemagglutinin mitogen was used as a positive control. CD4 T-cell response was evaluated towards CD69, IFN-γ, IL-2, IL-4, IL-5 and IL-13, in flow cytometry. rDer p 10 induced different cytokine expression in the six phenotypes. Allergen-specific IFN-γ stimulation was suggested by an increase in IFN-γ, IL-5, and IL-13 only in allergic to crustaceans, with a dose-dependent effect on IL-5 and IL-13. Tropomyosin is probably the main allergen responsible for the mite-shrimp crossreactivity but may not play a major role in snail-mite-shrimp cross-reactions. This work was done in the Laboratory of Immunology from Hospital de S. Bernardo, Setubal, Portugal.

물리적 처리에 의한 새우유래 Allergen 및 Allergenicity 변화

Ci-ELISA를 이용하여 여러 가지 물리적 처리(초고압, 가압가열, 초음파 및 microwave 처리)에 의한 새우 allergen 및 allergenicity의 변화를 살펴본 결과는 다음과 같다. 초고압 처리에 의해 새우의 allergenicity는 압력이 400 ㎫까지 증가함에 따라 새우 allergen과 mAb, 환자혈청과의 결합력이 감소하였으며, 특히 400 ㎫로 압력 처리했을 때 mAb와 새우 allergen과의 결합력이 50% 이하로 감소하였다. 새우 allergy의 allergenicity 변화를 알아보기 위해 5, 10, 30, 60분간 초음파 처리한 결과는 5, 10, 30분간 초음파 처리 시 처리시간이 길어짐에 따라 새우 allergen과 mAb와의 결합력이 감소하였으며 특히 60분간 처리한 경우에 있어서는 결합력이 60% 이하로 감소하였다. 가압 가열 처리(121℃, 1.4㎏/㎠)와 microwave 처리(2,450 ㎒)에 의한 새우 allergy의 allgergenicity 변화를 살펴본 결과 처리시간이 증가하여도 새우 allergen과 mAb와의 결합력이 크게 감소하지 않았다. 즉 20분간 microwave 처리 시 85% 이상의 높은 결합력을 보였으며 60분간 가압 가열처리에 의해서는 70% 이상의 결합력을 보였다.