Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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The Basophil Activation Test reduces the need for a food challenge test in children suspected of IgE-mediated cow's milk allergy
Ruinemans-Koerts, Janneke ; Schmidt-Hieltjes, Yvonne ; Jansen, Ad ; Savelkoul, Huub F.J. ; Plaisier, Annejet ; Setten, Petra van - \ 2019
Clinical and Experimental Allergy 49 (2019)3. - ISSN 0954-7894 - p. 350 - 356.

Background: The gold standard for the diagnosis of cow's milk allergy is the Double-Blind Placebo-Controlled Food Challenge (DBPCFC) test. However, disadvantages of the DBPCFC are the potential risk of anaphylactic reactions, the time-consuming procedure and high costs. Objective: The aim of this study was to determine the reliability of the Basophil Activation Test (BAT) both for the initial diagnosis of cow's milk allergy in children and for the determination of tolerance in children with cow's milk allergy. Methods: Ninety-seven BATs and cow's milk-specific IgE (sIgE) tests were performed in 86 infants/young children, suspected of (persistent) cow's milk allergy, who were qualified for an in-hospital DBPCFC. The BAT was performed with cow's milk extract and the purified major allergens casein, α-lactalbumin, β-lactoglubulin. Basophil activation was determined by CD63 upregulation measured by flow cytometry. The BAT results were compared to the DBPCFC outcomes. Results: Based on unequivocal DBPCFC and BAT result combinations (80%), the BAT had a sensitivity and specificity of 100% (CI: 86%-100% and 68%-100%, respectively) in IgE-sensitized children (41% of the tested children). All non-IgE-sensitized children (59%) had a negative DBPCFC and BAT, except for five patients. These latter showed delayed and relatively mild symptoms in the DBPCFC with a negative BAT, supporting a non-IgE-mediated allergy in these children. Conclusions and Clinical Relevance: The BAT seems reliable and cost-effective to diagnose patients with an IgE-mediated cow's milk allergy. In IgE-sensitized patients, a BAT might replace a DBPCFC. For non-IgE-sensitized patients presenting with mild symptoms, we propose to consider a (double-blind) extended (time) challenge test at home.

An alternative inhibition method for determining cross-reactive allergens
Schmidt-Hieltjes, Yvonne ; Teodorowicz, Gosia ; Jansen, Ad ; Hartog, Gerco Den; Elfvering-Berendsen, Lisette ; Jong, Nicolette W. De; Savelkoul, Huub F.J. ; Ruinemans-Koerts, Janneke - \ 2017
Clinical Chemistry and Laboratory Medicine 55 (2017)2. - ISSN 1434-6621 - p. 248 - 253.
basophil activation test (BAT) - cross-reactivity - immuno-inhibition - ImmunoCap
Inhibition assays are an useful tool to identify the allergen of primary sensitization of cross-reactive allergens. Classical ELISA-based inhibition assays are limited by both the availability of commercial standardized allergen extracts and the experience and knowledge needed for making home-made extracts. Moreover the direct comparison of the inhibition ELISAs outcomes between different laboratories is difficult because of different sources of used allergen extracts and a number of methodological variations. Therefore, we propose a novel ImmunoCap (Phadia, Thermofisher Scientific) based immunoinhibition method with the use of commercially available Caps as the allergen source. The novel ImmunoCap based immunoinhibition method was developed and tested with sera from patients with a well-known cross-reactive sensitization for fig (Ficus carica) and ficus (Ficus benjamina). Results were compared with a classically applied inhibition method, i.e. addition of homemade allergen extract to patient serum. The amount of allergens (fig and ficus extracts) needed to reach a similar degree of inhibition was comparable for both inhibition methods. The ImmunoCap based inhibition assay, in addition to classical inhibition methods, is a valuable tool as the ImmunoCap analyzer and commercial allergens (Caps) are more widely available which makes the outcomes of inhibition tests comparable between different laboratories. Furthermore, in the ImmunoCap inhibition method the same protein source is used for both the inhibition of sIgE and sIgE measurement, which might be even more relevant when multiple cross-reactive allergens are tested.
Immunological Characterization of Dutch Sesame Seed-Allergic Patients
Teodorowicz, Malgorzata ; Terlouw, Rozine J. ; Jansen, Ad ; Savelkoul, Huub F.J. ; Ruinemans-Koerts, Janneke - \ 2016
International Archives of Allergy and Immunology 169 (2016)1. - ISSN 1018-2438 - p. 13 - 22.
Allergen extracts - Basophil activation test - IgE inhibition test - Oleosin - Sesame allergy

Background: Sesame seed is an allergen of growing importance worldwide. However, knowledge of the clinically relevant sesame allergen and its cross-reactivity with homologous allergens is limited. The aim of this study was the immunological characterization of Dutch sesame seed-allergic patients and evaluation of cross-reactivity between sesame seed, tree nut and pollen allergens using different sources of allergen extracts. Methods: Six patients with a medical history of sesame seed allergy were included, i.e. 5 with an anaphylactic reaction and 1 with an oral allergy syndrome (OAS). The immunological background of the sesame seed and tree nut IgE sensitization was characterized with Western blotting and a basophil activation test (BAT). The major sesame allergen was identified by nanoLC-MS/MS. Cross-reactivity was measured using an immuno-inhibition assay with the Phadia ImmunoCAP system. Results: Oleosin was identified as the major allergen for the 5 patients with an anaphylactic reaction to sesame seed, but no cross-reactivity between sesame and tree nut proteins was observed. For the patient with OAS, IgE specific to oleosin was not detected but cross-reactivity between sesame seed and tree nut proteins was observed. The BAT and ImmunoCAP inhibition test added value to the clinical and immunological characterization of sesame seed-sensitized patients, distinguishing relevant and non-relevant sensitizations. Conclusions: Our immunological approach enabled us to fully characterize the sensitization pattern of 6 sesame seed-allergic patients. The different protein composition of commercially available allergen extracts influences the outcomes of the immunological assays and thus also the diagnosis to a large extent.

Is the basophil activation test (BAT) a reliable tool in the diagnosis of soy allergy?
Teodorowicz, M. ; Breedveld, A.C. ; Ruinemans-Koerts, J. ; Jansen, A.P.H. ; Savelkoul, H.F.J. ; Wichers, H.J. - \ 2014
Diagnostische waarde van de IgE-screeningstest (Phadiatop Infant) bij kinderen tot 4 jaar
Verlaet, A. ; Jansen, A. ; Plaisier, A. ; Huystee, B. van; Vissers, Y.M. ; Savelkoul, H.F.J. ; Ruinemans-Koerts, J. - \ 2012
Nederlands Tijdschrift voor Allergie en Astma 4 (2012). - ISSN 1879-9434 - p. 172 - 179.
Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut
Vissers, Y.M. ; Blanc, F. ; Stahl Skov, P. ; Johnson, P.E. ; Rigby, N.M. ; Przybylski-Nicaise, L. ; Bernhard, H. ; Wal, J.M. ; Ballmer-Weber, B. ; Zuidmeer-Jongejan, L. ; Szepfalusi, Z. ; Ruinemans-Koerts, J. ; Jansen, A.P.H. ; Savelkoul, H.F.J. ; Wichers, H.J. ; Mackie, A.R. ; Mills, E.N.C. ; Adel-Patient, K. - \ 2011
PLoS ONE 6 (2011)8. - ISSN 1932-6203 - 9 p.
ige-binding epitopes - t-cell responses - lipid transfer protein - in-vitro assay - maillard reaction - food allergens - cytokine production - major allergen - b-cell - digestion
Background Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.
Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6: the necessity of degranulation assays
Vissers, Y.M. ; Iwan, M. ; Adel-Patient, K. ; Stahl Skov, P. ; Rigby, N.M. ; Johnson, P.E. ; Mandrup Muller, P. ; Przybylski-Nicaise, L. ; Schaap, M. ; Ruinemans-Koerts, J. ; Jansen, A.P.H. ; Mills, E.N.C. ; Savelkoul, H.F.J. ; Wichers, H.J. - \ 2011
Clinical and Experimental Allergy 41 (2011)11. - ISSN 0954-7894 - p. 1631 - 1642.
plant food allergens - ige-binding - enzyme immunoassays - maillard reaction - cooking methods - protein - children - ara-h-1 - purification - reactivity
Background - Peanuts are often consumed after roasting, a process that alters the three-dimensional structure of allergens and leads to Maillard modification. Such changes are likely to affect their allergenicity. Objective - We aimed to establish the effect of thermal treatment mimicking the roasting process on the allergenicity of Ara h 1 and a mix of 2S albumins from peanut (Ara h 2/6). Methods - Ara h 1 and Ara h 2/6 were purified from raw peanuts and heated in a dry form for 20 min at 145 °C in the presence (R+g) or absence (R-g) of glucose, and soluble proteins were then extracted. Sera obtained from 12 well-characterized peanut-allergic patients were used to assess the IgE binding and degranulation capacities of the allergens. Results - Extensive heating at low moisture resulted in the hydrolysis of both Ara h 1 and Ara h 2/6. However, in contrast to Ara h 2/6, soluble R+g Ara h 1 formed large aggregates. Although the IgE-binding capacity of R+g and R-g Ara h 1 was decreased 9000- and 3.6-fold, respectively, compared with native Ara h 1, their capacity to elicit mediator release was increased. Conversely, both the IgE-binding capacity and the degranulation capacity of R-g Ara h 2/6 were 600–700-fold lower compared with the native form, although the presence of glucose during heating significantly moderated these losses. Conclusions - and Clinical Relevance Extensive heating reduced the degranulation capacity of Ara h 2/6 but significantly increased the degranulation capacity of Ara h 1. This observation can have important ramifications for component-resolved approaches for diagnosis and demonstrates the importance of investigating the degranulation capacity in addition to IgE reactivity when assessing the effects of food processing on the allergenicity of proteins.
IgE component-resolved allergen profile and clinical symptoms in soy and peanut allergic patients
Vissers, Y.M. ; Jansen, A.P.H. ; Ruinemans-Koerts, J. ; Wichers, H.J. ; Savelkoul, H.F.J. - \ 2011
Allergy 66 (2011)8. - ISSN 0105-4538 - p. 1125 - 1127.
europe
Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity
Blanc, F. ; Vissers, Y.M. ; Adel-Patient, K. ; Rigby, N.M. ; Mackie, A.R. ; Gunning, A.P. ; Wellner, N.K. ; Skov, P.S. ; Przybylski-Nicaise, L. ; Ballmer-Weber, B. ; Zuidmeer-Jongejan, L. ; Szépfalusi, Z. ; Ruinemans-Koerts, J. ; Jansen, A.P. ; Bernard, H. ; Wal, J.M. ; Savelkoul, H.F.J. ; Wichers, H.J. ; Mills, E.N.C. - \ 2011
Molecular Nutrition & Food Research 55 (2011)12. - ISSN 1613-4125 - p. 1887 - 1894.
food allergens - ige binding - proteins - ara-h-1
Scope: Roasting rather than boiling and Maillard modifications may modulate peanut allergenicity. We investigated how these factors affect the allergenic properties of a major peanut allergen, Ara h 1. Methods and results: Ara h 1 was purified from either raw (N-Ara h 1) or roasted (R-Ara h 1) peanuts. Boiling (100°C 15¿min; H-Ara h 1) resulted in a partial loss of Ara h 1 secondary structure and formation of rod-like branched aggregates with reduced IgE-binding capacity and impaired ability to induce mediator release. Glycated Ara h 1 (G-Ara h 1) formed by boiling in the presence of glucose behaved similarly. However, H- and G-Ara h1 retained the T-cell reactivity of N-Ara h 1. R-Ara h 1 was denatured, comprised compact, globular aggregates, and showed no evidence of glycation but retained the IgE-binding capacity of the native protein. Conclusion: Ara h 1 aggregates formed by boiling were morphologically distinct from those formed by roasting and had lower allergenic activity. Glycation had no additional effect on Ara h 1 allergenicity compared with heating alone. Taken together with published data on the loss of Ara h 2/6 from boiled peanuts, this supports the hypothesis that boiling reduces the allergenicity of peanuts
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