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Dive into the research topics where S.J. Koppelman is active.

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Featured researches published by S.J. Koppelman.


Clinical & Experimental Allergy | 2004

Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen

S.J. Koppelman; M. Wensing; M. Ertmann; André C. Knulst; Edward F. Knol

Background A number of allergenic proteins in peanut has been described and the relative importance of these allergens is yet to be determined.


Allergy | 2003

Peanut allergen Ara h 3: Isolation from peanuts and biochemical characterization

S.J. Koppelman; Edward F. Knol; R.A.A. Vlooswijk; Marjolein Wensing; André C. Knulst; Susan L. Hefle; H. Gruppen; Sander Piersma

Background:u2002 Peanut allergen Ara h 3 has been the subject of investigation for the last few years. The reported data strongly depend on recombinant Ara h 3, since a purification protocol for Ara h 3 from peanuts was not available.


Clinical & Experimental Allergy | 2007

Children with peanut allergy recognize predominantly Ara h2 and Ara h6, which remains stable over time

Annebeth E. Flinterman; E. van Hoffen; C.F. den Hartog Jager; S.J. Koppelman; S. G. Pasmans; Maarten O. Hoekstra; C.A.F.M. Bruijnzeel-Koomen; André C. Knulst; Edward F. Knol

Background In peanut‐allergic adults, IgE is mainly directed to Ara h1 and Ara h2. More recently, a role for Ara h6 has been suggested. In contrast to adults, IgE in children can fluctuate over time. Therefore, children may have a more dynamic reactivity to peanut.


Clinical & Experimental Allergy | 2002

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

M. Wensing; André Penninks; Susan L. Hefle; J.H. Akkerdaas; R. van Ree; S.J. Koppelman; Carla A.F.M. Bruijnzeel-Koomen; André C. Knulst

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.


Clinical & Experimental Allergy | 2005

Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: Evidence for cross-reactivity with Ara h 2

S.J. Koppelman; G. A. H. De Jong; M. Laaper‐Ertmann; Kim A.B.M. Peeters; André C. Knulst; Susan L. Hefle; Edward F. Knol

Background IgE‐binding peanut proteins smaller than 15u2003kDa were previously identified as potential allergens in the majority of our peanut allergic population.


Allergy | 2000

Comparison of antibody responses to hen's egg and cow's milk proteins in orally sensitized rats and food-allergic patients

L.M.J. Knippels; H.P.M. van der Kleij; S.J. Koppelman; G.F. Houben; A.H. Penninks; A.A. Felius

Background: No adequate enteral sensitization models are available to study food allergy and the allergenicity of food proteins. To further validate a enteral brown Norway (BN) rat sensitization model under development, we studied specific protein recognition to determine whether a comparable pattern of proteins is recognized by the rat immune system and the human immune system.


Allergy | 2009

Clinical relevance of sensitization to lupine in peanut-sensitized adults

Kim A.B.M. Peeters; S.J. Koppelman; A.H. Penninks; Ans F.M. Lebens; Carla A.F.M. Bruijnzeel-Koomen; Susan L. Hefle; Steve L. Taylor; E. van Hoffen; André C. Knulst

Background:u2002 The use of lupine in food has been increasing during the last decade and allergic reactions to lupine have been reported, especially in peanut‐allergic patients. The frequency and the degree of cross‐reactivity to other legumes are not known. The aim of the study was to investigate the frequency of sensitization to lupine, and in addition to pea and soy, and its clinical relevance, in peanut‐sensitized patients. Furthermore, to determine the eliciting dose (ED) for lupine using double‐blind placebo‐controlled food challenges (DBPCFC).


Detecting allergens in food. | 2006

Detecting allergens in food.

S.J. Koppelman; Susan L. Hefle

Part 1 The basics of food allergy: The nature of food allergy Classifying food allergens. Part 2 Types of detection method: The use of antibodies to detect allergens in food Allergen-specific human IgE antibody-based analysis of food Immunoblotting in allergen detection Enzyme-linked immunosorbent assays (ELISAs) for detecting allergens in foods Polymerase chain reaction (PCR) methods for the detection of allergenic foods Proteomic assessment of allergens in food Detecting food allergens with a surface plasmon resonance immunoassay The use of lateral flow devices to detect food allergens. Part 3 Detection methods for particular allergens: Methods for detecting peanuts in food Detecting tree nuts and seeds in food Detecting dairy and egg residues in food Detecting wheat gluten in food Detecting soy, fish and crustaceans in food. Part 4 Issues in using allergen detection methods: Allergen quality assurance for hypoallergenic formula Common issues in detecting allergenic residues on equipment and in processed foods Factors affecting the effectiveness of allergen detection Reference materials and method validation in allergen detection US regulation of undeclared allergens in food products EU regulation of undeclared allergens in food products.


Allergy | 2001

Hidden hazelnut is a threat to allergic patients

Marjolein Wensing; S.J. Koppelman; André Penninks; Carla A.F.M. Bruijnzeel-Koomen; André C. Knulst

. A 5-YEAR-OLD boy with a history of urticaria pigmentosa and asthma developed severe colic and itching of his urticaria pigmentosa lesions 12 h after eating bread with chocolate spread. These symptoms resolved spontaneously about 1 h later. He had never suffered from adverse reactions to chocolate spread before. However, 2 years before, his parents had noticed urticaria around his mouth after he had eaten hazelnutcontaining chocolate spread. Subsequently, hazelnut-containing food products had been eliminated from his diet. Skin prick tests (SPT) were performed and speci®c IgE was determined by the CAP System (Pharmacia, Uppsala, Sweden) for several food allergens. The results showed a monosensitization to hazelnut (SPT 3+ and CAP 1.79 kU/l). The reference standard for diagnosing adverse reactions to food is the double-blind, placebo-controlled food challenge (DBPCFC). However, in view of the history of urticaria pigmentosa, it would not have been ethical to challenge this patient. The boy did not eat any suspected hazelnutcontaining food that day, except for the chocolate spread. It was prepacked chocolate spread in 10-g cups for `singleuse. Although the label listed only lactose, vegetable oil, cacao, and vanillin, the possibility of contamination of the chocolate spread with hazelnut was considered because hazelnut-containing products (hazelnut-containing chocolate spread) are produced by the same manufacturer. A sample of chocolate spread (a 10-g cup) from the same production batch as the complaint sample was provided by the parents. This sample and six other samples from different production batches, supplied by the manufacturer, were analyzed together with hazelnut-containing chocolate spread as a positive control. An enzyme immunoassay, speci®c for hazelnut protein (1), demonstrated the presence of hazelnut in all the samples (Table 1). As mentioned earlier, the patient had eaten chocolate spread before without having symptoms. This can be explained by the varying levels of contamination (up to 20-fold). Probably, the previously ingested chocolate spread contained lower amounts of hazelnut than the complaint sample and therefore was not able to induce an allergic reaction. In summary, a 5-year-old boy, allergic to hazelnut, as shown by a history of adverse reactions to hazelnut, an elevated speci®c IgE level, and a positive SPT, developed gastrointestinal and cutaneous symptoms after ingestion of chocolate spread highly contaminated with hazelnut. Because of the relatively long period between ingestion and the development of symptoms, the association between the chocolate spread and the described symptoms is uncertain. However, this case illustrates that varying amounts of hazelnut can be present in chocolate spread without declaration on the label. Little is known yet about the minimal provoking doses of hazelnut in hazelnutallergic patients. Malmheden Yman et al. described a patient with an adverse reaction after ingestion of 7.2 mg of hazelnut protein, corresponding to about 30 mg of hazelnut (2). Assuming a consumption of 10 g of chocolate spread, about 56 mg of hazelnut would have been ingested by this patient. As such minute quantities of allergenic foods can induce severe allergic reactions, these allergen-contaminated consumer products can be a threat to foodallergic patients (2, 3). ALLERGY 2001: 56:191^197 . COPYRIGHT G MUNKSGAARD 2001 . ISSN 0105-4538 . ALL RIGHTS RESERVED . CONTRIBUTIONS TO THIS SECTION WILL NOT UNDERGO PEER REVIEW, BUT WILL BE REVIEWED BY THE ASSOCIATE EDITORS .


Clinical & Experimental Allergy | 2014

Chemical modification of peanut conglutin reduces IgE reactivity but not T cell reactivity in peanut‐allergic patients

E. van Hoffen; H. P. M. van der Kleij; C.F. den Hartog Jager; W. A. van Doorn; Edward F. Knol; D.-J. Opstelten; S.J. Koppelman; André C. Knulst

Specific immunotherapy for peanut allergy is associated with significant side‐effects. Chemically modified allergens may provide a safer alternative.

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Susan L. Hefle

University of Nebraska–Lincoln

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Joseph L. Baumert

University of Nebraska–Lincoln

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M. Wensing

University of Michigan

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