Development of animal models and sandwich-ELISA tests to detect the allergenicity and antigenicity of fining agent residues in wines.

Food allergy can cause food-related anaphylaxis. Food allergen labeling is the principal means of protecting sensitized individuals. This motivated European Directive 2003/89 on the labeling of ingredients or additives that could trigger adverse reactions, which has been in effect since 2005.

Uptake of ingested bovine lactoferrin and its accumulation in adult mouse tissues.

Lactoferrin is a glycoprotein with antimicrobial and immunoregulatory properties, which is found in milk, other external secretions, and in the secondary granules of neutrophils. The present study examined the time course of uptake and the pattern of tissue accumulation of bovine lactoferrin (bLf) following intragastric intubation of a single dose to adult naïve mice or to mice daily fed bLf for 4 weeks. Following ingestion, bLf was transferred from the intestine into peripheral blood in a form with intact molecular weight (80 kDa) and localized within 10 to 20 min after oral administration in the liver, kidneys, gall bladder, spleen, and brain of both groups of mice.

Peanut-lupine antibody cross-reactivity is not associated to cross-allergenicity in peanut-sensitized mouse strains.

Background: Peanut hypersensitivity is one of the most common food allergies and one of the most common causes of death by food anaphylaxis in children and adults. Cross-reactivity of peanut-specific antibody (Ab) with other legumes is frequently demonstrated but it still remains to be demonstrated whether these responses could lead to clinical signs of cross-allergenicity.

Objective: We sought to evaluate peanut-specific serum IgE and IgG1 antibody (Ab) responses and anaphylactic reaction in mice strains and to assess both cross-reactivity and cross-allergenicity of peanut and lupine.

The mode of oral bovine lactoferrin administration influences mucosal and systemic immune responses in mice.

Food protein intake interacts with the immune system. In earlier nutritional and immunological studies, nutrients, particularly milk whey proteins, were generally administered in soluble form and by gavage. However, orogastric intubation does not represent a natural way of ingesting nutrients such as lactoferrin (Lf).

Microsphere entrapped bee-venom phospholipase A2 retains specific IgE binding capacity: a possible use for oral specific immunotherapy.

The only specific treatments of allergy are long and exacting desensitization by subcutaneous injections of the allergens. While oral administration of allergens could greatly facilitate these treatments, effective delivery systems are needed to prevent allergen degradation in the gastrointestinal tract and to enable their uptake by Peyer's patches. The potential for bee-venom phospholipase A2 (PLA2) to be used in such oral immunotherapy was tested.