Stef J. Koppelman

University of Nebraska–Lincoln

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Steve L. Taylor

University of Nebraska–Lincoln

Joseph L. Baumert

University of Nebraska–Lincoln

André C. Knulst

University Medical Center Utrecht

Govardus A. H. de Jong

Wageningen University & Research

Julie A. Nordlee

University of Nebraska–Lincoln

Edward F. Knol

University Medical Center Utrecht

Susan L. Hefle

University of Nebraska–Lincoln

Harmen H. J. de Jongh

Pension Fund for Care and Well-Being

Michel Wensing

Heidelberg University

Benjamin C. Remington

University of Nebraska–Lincoln

Cooperative Institutions

University of Mississippi Medical Center

111

State Street (United States)

106

American College of Allergy, Asthma and Immunology

Utrecht University

Medical University of Vienna

University of Salzburg

Charité - Universitätsmedizin Berlin

University of Nebraska–Lincoln

University Medical Center Utrecht

Wageningen University & Research

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Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity

Molecular Nutrition & Food Research (2008)

Evelien L. van Boxtel L.A.M. van den Broek Stef J. Koppelman Harry Gruppen

Legumin proteins Ara h 3 from peanuts and glycinin from soybeans are increasingly described as important allergens. The stability of an allergen's IgE binding capacity towards heating and digestion is considered an important characteristic for food allergens. We investigated the effects of heating and digestion on the IgE binding of Ara h 3 and glycinin. Both proteins are relatively stable to denaturation, having denaturation temperatures ranging from 70 to 92 degrees C, depending on their quaternary structure and the ionic strength. Aggregates were formed upon heating, which were partly soluble for glycinin. Heating slightly decreased the pepsin digestion rate of both allergens. However, heating did not affect the IgE binding capacity of the hydrolyzates, as after only 10 min of hydrolysis no IgE binding could be detected any more in all samples. Peanut allergen Ara h 1, when digested under equal conditions, still showed IgE binding after 2 h of hydrolysis. Our results indicate that the IgE binding capacity of legumin allergens from peanuts and soybeans does not withstand peptic digestion. Consequently, these allergens are likely unable to sensitize via the gastro-intestinal tract and cause systemic food allergy symptoms. These proteins might thus be less important allergens than was previously assumed.

Legumin

Denaturation (fissile materials)

Digestion

Food allergens

Pepsin

10.1002/mnfr.200700299

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Citations (77)

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

Allergy (2003)

Stef J. Koppelman Edward F. Knol Riek A. A. Vlooswijk Michel Wensing André C. Knulst

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.Peanut allergen Ara h 3 (glycinin), was purified and its posttranslational processing was investigated. Its allergenic properties were determined by studying IgE binding characteristics of the purified protein.Ara h 3 consists of a series of polypeptides ranging from approximately 14 to 45 kDa that can be classified as acidic and basic subunits, similar to the subunit organization of soy glycinin. N-terminal sequences of the individual polypeptides were determined, and using the cDNA deduced amino-acid sequence, the organization into subunits was explained by revealing posttranslational processing of the different polypeptides. IgE-binding properties of Ara h 3 were investigated using direct elisa and Western blotting with sera from peanut-allergic individuals. The basic subunits, and to a lesser extent the acidic subunits, bind IgE and may act as allergenic peptides.We conclude that peanut-derived Ara h 3, in contrast to earlier reported recombinant Ara h 3, resembles, to a large extent, the molecular organization typical for proteins from the glycinin family. Furthermore, posttranslational processing of Ara h 3 affects the IgE-binding properties and is therefore an essential subject of study for research on the allergenicity of Ara h 3.

Peanut Allergy

10.1034/j.1398-9995.2003.00259.x

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Citations (180)

Peanut cross-contamination in randomly selected baked goods

Annals of Allergy Asthma & Immunology (2022)

Travis A. Miller Stef J. Koppelman J. Andrew Bird Vivian Hernandez‐Trujillo Ananth Thyagarajan

Peanut Allergy

10.1016/j.anai.2022.01.037

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Citations (4)

Modeled Quantitative Risk Reduction Through Epicutaneous Immunotherapy for Peanut Allergy: Restaurant Meal Preparation With Shared Cooking Utensils and Equipment

Journal of Allergy and Clinical Immunology (2020)

Benjamin C. Remington Dianne E. Campbell Todd D. Green David M. Fleischer Stef J. Koppelman

Peanut Allergy

Meal preparation

Oral immunotherapy

10.1016/j.jaci.2019.12.455

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Citations (2)

Shared Cooking Equipment in Restaurants: A Quantitative Risk Assessment for Peanut-Allergic Consumers

Journal of Allergy and Clinical Immunology (2019)

Benjamin C. Remington Stef J. Koppelman

Peanut butter

Peanut oil

10.1016/j.jaci.2018.12.729

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Citations (1)

810 Anaphylaxis due to the unexpected presence of casein in salmon: Implications of novel enzymes in food processig

Journal of Allergy and Clinical Immunology (2000)

Stef J. Koppelman

10.1016/s0091-6749(00)91238-7

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Citations (0)

Determination of Pepsin-Susceptible and Pepsin-Resistant Epitopes in Native and Heat-Treated Peanut Allergen Ara h 1

Journal of Agricultural and Food Chemistry (2008)

Evelien L. van Boxtel Stef J. Koppelman L.A.M. van den Broek Harry Gruppen

This study was aimed at the determination of the pepsin-susceptible and pepsin-resistant epitopes in native and heat-treated Ara h 1, a major allergen from peanuts. Both the oligomeric structure and the trimeric structure of the allergen were investigated. Under the in vitro conditions applied, oligomeric Ara h 1, either unheated or preheated, was hydrolyzed by pepsin at a lower rate than trimeric Ara h 1. Peptides with relatively high molecular masses were shown to be able to bind IgE, whereas peptides with lower molecular masses (<2 kDa) did not. In these latter fractions, fragments of 15 previously published epitopes of mature Ara h 1 were identified. As a result, these epitopes are not likely responsible for the induction of systemic food allergic reactions to peanuts. Using sequential chymotrypsin digestion, the pepsin-resistant IgE-binding peptides were deduced to contain the previously identified intact epitopes EDWRRPSHQQ (amino acids 50-59) and PRKIRPEG (amino acids 60-67). The presence of four additional earlier published intact epitopes (covering amino acids 6-13, 14-21, 24-31, and 40-47) on the pepsin-resistant peptides could be neither deduced nor ruled out. The two deduced and four possible pepsin-resistant epitopes are all situated in the N-terminal part of Ara h 1, which does not show homology with other vicilin proteins. Consequently, this unique N-terminal part of Ara h 1 is proposed to be responsible for the allergen's ability to induce systemic allergic reactions.

Pepsin

10.1021/jf072907n

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Citations (27)

A perspective on pea allergy and pea allergens

Trends in Food Science & Technology (2021)

Steve L. Taylor Justin Marsh Stef J. Koppelman Jamie Kabourek Philip E. Johnson

Hypoallergenic

Pea protein

Vicilin

Pathogenesis-related protein

Field pea

10.1016/j.tifs.2021.07.017

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Citations (65)

Basophil response to peanut allergens in Mediterranean peanut‐allergic patients

Allergy (2014)

Cristobalina Mayorga F. Gómez Ana Aranda Stef J. Koppelman Araceli Díaz‐Perales

Ara h 1, Ara h 2, and Ara h 3 are important sensitizers in peanut allergy. Ara h 9 has also been shown to be relevant in the Mediterranean area. We evaluated the basophil response to peanut allergens and Pru p 3 in Mediterranean patients: Group 1, peanut and peach allergy; Group 2, peanut allergy and tolerance to peach; Group 3, peach allergy and tolerance to peanut; Group 4, nonallergic subjects that tolerate both peanut and peach. Compared to controls (Group 4), there was an increased basophil activation with Ara h 2 (P = 0.031) and Pru p 3 (P = 0.009) in Group 1 and with Ara h 1 (P = 0.016), Ara h 2 (P = 0.001), and Ara h 9 (P = 0.016) in Group 2. Importantly, only Ara h 2 showed an increased activation (P = 0.009) in Group 2 compared to Group 3. Ara h 2 is the best discriminating allergen for peanut allergy diagnosis in a Mediterranean population showing two patterns: patients also allergic to peach, responding to Ara h 2 and Pru p 3, and patients allergic only to peanut, responding to Ara h 1, Ara h 2, and Ara h 9.

Peanut Allergy

Mediterranean area

Basophil activation

Arachis hypogaea

10.1111/all.12421

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Citations (25)

Increasing Clinical Peanut Thresholds Through Immunotherapy: Quantitative Assessment of the Safety Benefits Associated with Achieving a 300 or 1000 mg Peanut Protein Threshold.

Journal of Allergy and Clinical Immunology (2017)

Joseph L. Baumert Charles Ruban Laurent Martin Claude Thébault Luis M. Salmun

Peanut Allergy

Peanut butter

Threshold dose

Oral immunotherapy

10.1016/j.jaci.2016.12.576

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