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Ouahidi I.,Laboratoire des molecules bioactives LMBSF | Barakat A.,Center National Of Reference En Neonatologie Et En Nutrition | El Youbi El Hamsas A.,Laboratoire des molecules bioactives LMBSF | Aarab L.,Laboratoire des molecules bioactives LMBSF
Immuno-Analyse et Biologie Specialisee | Year: 2011

Background: The aim of the present work was first to evaluate the sensitivity and recognition of human IgE and rabbit IgG to native and treated gliadins by acid or heating. Methods: For this, 451 adults were recruited to evaluate specific IgE levels and their reactivity to native and to heat- and acid-treated gliadins. Reactivity was evaluated by Elisa and immunoblots. This later was done to characterize the allergenic components. Results: They showed that 0.4% of the patients reported allergy to wheat flour. From those patients, 5.9% showed levels of specific IgE between 40 and 100. UI/ml. Immunoreactivity of IgG showed a reduction in recognition of gliadins heated at 100. °C or by acidification. With IgE, gliadins treated showed a decrease in their reactivity in 50% of patients under heating and 80% under acid treatment. By immunoblot we have observed that the sera tested showed a high IgE sensitivity to α, β, and γ-gliadins. On these blots, heating reduced highly the reactivity of IgE and IgG to α and β-gliadins, where it, remarkably, increases the sensitivity to ω-gliadins. Conclusions: Allergen-specific IgE measurement indicates an important number of adults who are sensitive to gliadins. Physico-chemical treatment against gliadins was able to reduce partially their allergenicity. © 2010 Elsevier Masson SAS.


Peanuts are one of the major allergens responsible for food allergy in children and adults. The prevalence of peanut allergy varies according to the country, which can be explained by the different habits of eating peanuts in the populations concerned. The objectives of the present work were, first, to evaluate the sensitivity to peanuts in the population in the region of Fès-Meknès in Maroc, and then to study the effect of acid treatment and heating on the allergenicity of peanut proteins. A cross-sectional study had been carried out at the University Hospital in Fès and at analytical laboratories in Meknès in which 442 adults were recruited to establish a serum bank. A detailed questionnaire on possible allergies was completed by these patients. This serum bank was used to evaluate specific IgE reactivity to peanut and the reactivity of this IgE to native and to heat- and acid-treated peanut proteins. Immunoblots were also done to characterize the allergenic components. The results showed that 9.5% of the patients reported allergy to food. Among these patients, 4.2% reported allergy to eggs, 2.5% to peanuts and 0.4 % to wheat flour. The study of the effect of temperature and acidity on the allergenicity of peanut proteins showed that it was reduced by more than 30% by heating at 100 °C and by acid treatment in sera of 50% of the patients. With a combination of these treatments, 81.3% of the sera showed a reduction of greater than 30%. Immunoblots showed that the majority of the sera reacted with Arah1. This reactivity was strongly reduced by treatment of the peanut proteins, especially by treatment with acid. © 2009.


Bousfiha A.,Laboratoire des molecules bioactives LMBSF | Aarab L.,Laboratoire des molecules bioactives LMBSF
Immuno-Analyse et Biologie Specialisee | Year: 2012

The aim is to assess the sensitivity of the population of Fez and Casablanca in Morocco to chicken meat and the effect of heating on this sensitivity. The work is based on a serum bank consisting of 146 sera from patients with suspected allergy. The evaluation of specific IgE to chicken meat showed that 46% of children and 38% of adults have positive values with 12.3% of children and 10% of adults have a higher rate than 20. UI/mL. This high sensitivity shows only partial cross-recognition to the egg whites ranging from 16 to 60%. Heat treatment of meat proteins in chicken showed that more than 80% of these patients show a decrease in the recognition of proteins above 30% after 1. hour at 80. °C. This demonstrates a high thermolability of epitopes recognized by sera from these patients indicating conformational antigenic sites rather than sequential. © 2012 Elsevier Masson SAS.

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