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1.
Mol Nutr Food Res ; 61(9)2017 09.
Artículo en Inglés | MEDLINE | ID: mdl-28500661

RESUMEN

SCOPE: 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. METHODS AND RESULTS: 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. CONCLUSION: 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.


Asunto(s)
Hipersensibilidad a los Alimentos/inmunología , Penaeidae/inmunología , Tenebrio/inmunología , Adulto , Anciano , Animales , Reacciones Cruzadas , Femenino , Humanos , Inmunoglobulina E/inmunología , Masculino , Persona de Mediana Edad
4.
Regul Toxicol Pharmacol ; 79: 118-124, 2016 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-27012375

RESUMEN

To solve the future food insecurity problem, alternative and sustainable protein sources (e.g. insects, rapeseed, fava bean and algae) are now being explored for the production of food and feed. To approve these novel protein sources for future food a comprehensive risk assessment is needed according to the European food legislation. Allergenicity risk assessment might pose some major difficulties, since detailed guidance on how to assess the allergenic potential of novel foods is not available. At present, the approach relies mostly on the guidance of allergenicity assessment for genetically modified (GM) plant foods. The most recent one was proposed by EFSA (2010 and 2011); "weight-of-evidence approach". However this guidance is difficult to interpret, not completely applicable or validated for novel foods and therefore needs some adjustments. In this paper we propose a conceptual strategy which is based on the "weight-of-evidence approach" for food derived from GM plants and other strategies that were previously published in the literature. This strategy will give more guidance on how to assess the allergenicity of novel food proteins and protein sources.


Asunto(s)
Alérgenos/efectos adversos , Seguridad de Productos para el Consumidor , Hipersensibilidad a los Alimentos/etiología , Inocuidad de los Alimentos , Alimentos Modificados Genéticamente/efectos adversos , Pruebas Inmunológicas , Proteínas de Vegetales Comestibles/efectos adversos , Plantas Modificadas Genéticamente/efectos adversos , Alérgenos/genética , Alérgenos/inmunología , Animales , Seguridad de Productos para el Consumidor/normas , Reacciones Cruzadas , Hipersensibilidad a los Alimentos/inmunología , Guías como Asunto , Humanos , Pruebas Inmunológicas/normas , Proteínas de Vegetales Comestibles/genética , Proteínas de Vegetales Comestibles/inmunología , Plantas Modificadas Genéticamente/genética , Plantas Modificadas Genéticamente/inmunología , Medición de Riesgo
5.
Mol Nutr Food Res ; 59(9): 1855-64, 2015 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-26097070

RESUMEN

SCOPE: 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. METHODS AND RESULTS: 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. CONCLUSION: 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.


Asunto(s)
Alérgenos/inmunología , Manipulación de Alimentos/métodos , Calor , Tenebrio , Adulto , Anciano , Animales , Cromatografía Liquida , Electroforesis en Gel de Poliacrilamida , Femenino , Galectina 3/metabolismo , Humanos , Immunoblotting , Masculino , Persona de Mediana Edad , Hipersensibilidad a los Mariscos/inmunología , Pruebas Cutáneas , Espectrometría de Masas en Tándem , Adulto Joven
6.
J Allergy Clin Immunol Pract ; 1(6): 632-8.e1, 2013.
Artículo en Inglés | MEDLINE | ID: mdl-24565711

RESUMEN

BACKGROUND: Specific IgE (sIgE) to Ara h 2 as a clinical predictor for peanut allergy in children has a diagnostic value comparable with a prediction model that contains sex, skin prick test (SPT), sIgE to peanut extract, and total IgE minus sIgE. In adults, the diagnostic value of peanut components has not yet been studied. OBJECTIVE: To validate a pediatric prediction model in an adult population; to define the diagnostic value of sIgE to peanut components. METHODS: Validation was performed by discrimination with an area under the receiver operating characteristic curve (AUC) and calibration with the Hosmer-Lemeshow test. The diagnostic value of the peanut components was assessed with the AUC. RESULTS: Validation of the pediatric model in 94 adults showed poor discrimination (AUC, 0.64) but good calibration (P = .48); sIgE to Ara h 2 was the best diagnostic predictor (AUC, 0.76). By using a cutoff value with a 100% positive predictive value (≥1.75 kU/L), 28% of patients could be diagnosed with 100% accuracy. The highest negative predictive value was 63%. A higher negative predictive value could not be calculated for any other test. Although sIgE to Ara h 2 was significantly correlated with severity, it did not discriminate between mild and severe allergy in individual patients (AUC < 0.65). CONCLUSION: sIgE to Ara h 2 has the best discriminative ability of all diagnostic tests. It can accurately diagnose peanut allergy in 28% of patients but cannot be used to exclude a peanut allergy in an adult population.


Asunto(s)
Albuminas 2S de Plantas/análisis , Antígenos de Plantas/análisis , Glicoproteínas/análisis , Hipersensibilidad al Cacahuete/diagnóstico , Adulto , Análisis de Varianza , Femenino , Humanos , Inmunoglobulina E/análisis , Masculino , Sensibilidad y Especificidad , Pruebas Cutáneas/métodos
7.
Am J Physiol Gastrointest Liver Physiol ; 292(5): G1302-14, 2007 May.
Artículo en Inglés | MEDLINE | ID: mdl-17272516

RESUMEN

The terminal differentiation phases of intestinal development in mice occur during cytodifferentiation and the weaning transition. Lactase-phlorizin hydrolase (LPH), liver fatty acid binding protein (Fabp1), and sucrase-isomaltase (SI) are well-characterized markers of these transitions. With the use of gene inactivation models in mature mouse jejunum, we have previously shown that a member of the zinc finger transcription factor family (Gata4) and hepatocyte nuclear factor-1alpha (Hnf1alpha) are each indispensable for LPH and Fabp1 gene expression but are both dispensable for SI gene expression. In the present study, we used these models to test the hypothesis that Gata4 and Hnf1alpha regulate LPH, Fabp1, and SI gene expression during development, specifically focusing on cytodifferentiation and the weaning transition. Inactivation of Gata4 had no effect on LPH gene expression during either cytodifferentiation or suckling, whereas inactivation of Hnf1alpha resulted in a 50% reduction in LPH gene expression during these same time intervals. Inactivation of Gata4 or Hnf1alpha had a partial effect ( approximately 50% reduction) on Fabp1 gene expression during cytodifferentiation and suckling but no effect on SI gene expression at any time during development. Throughout the suckling period, we found a surprising and dramatic reduction in Gata4 and Hnf1alpha protein in the nuclei of absorptive enterocytes of the jejunum despite high levels of their mRNAs. Finally, we show that neither Gata4 nor Hnf1alpha mediates the glucocorticoid-induced precocious maturation of the intestine but rather are downstream targets of this process. Together, these data demonstrate that specific intestinal genes have differential requirements for Gata4 and Hnf1alpha that are dependent on the developmental time frame in which they are expressed.


Asunto(s)
Proteínas de Unión a Ácidos Grasos/biosíntesis , Factor de Transcripción GATA4/fisiología , Regulación del Desarrollo de la Expresión Génica , Factor Nuclear 1-alfa del Hepatocito/fisiología , Intestino Delgado/crecimiento & desarrollo , Lactasa-Florizina Hidrolasa/biosíntesis , Complejo Sacarasa-Isomaltasa/biosíntesis , Animales , Femenino , Glucocorticoides/farmacología , Intestino Delgado/efectos de los fármacos , Intestino Delgado/embriología , Ratones , Embarazo , ARN Mensajero/metabolismo , Destete
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