J.-M. Wal

Oral administration of recombinant Lactococcus lactis expressing bovine beta-lactoglobulin partially prevents mice from sensitization.

Background The use of probiotics such as Lactococcus lactis and other lactic acid bacteria (LAB) has been proposed for the management of food allergy. However, no experimental study has clearly demonstrated any preventive or therapeutic inhibition of an allergen‐specific IgE response.

Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin

Background:  The development of animal models developing specific immunoglobulin (Ig)E presenting the same specificity as human IgE and similar clinical symptoms as those observed in allergic patients are of great interest for the understanding of mechanisms involved in the induction and regulation of food allergy.

Allergy to goat and sheep milk without allergy to cow's milk.

Background:  Cows milk (CM) allergy is the most frequent cause of food allergy in infants. Most children who are allergic to CM are also sensitized to whey proteins and/or to the casein fraction and many of them cannot tolerate goats or sheeps milk (GSM) either. Conversely, the GSM allergies that are not associated with allergic cross‐reactivity to CM are rare.

Detection of caseinophosphopeptides in the distal ileostomy fluid of human subjects

Caseinophosphopeptides (CPP) were detected for the first time in ileostomy fluid, collected at 2 h intervals for 10 h post milk and CPP ingestion, from human volunteers with an ileostomy. The level of CPP present in ileostomy fluid obtained from milk-fed volunteers was markedly higher than that from volunteers fed with selected CPP preparations. The findings are based on HPLC analysis in combination with peptide-bound P determination, thin-layer electrophoresis and amino acid analysis, together with ELISA studies using polyclonal antibodies raised against a set of CPP to detect immunoreactive CPP in ileostomy fluid. These procedures allowed the detection of nm concentrations of CPP. CPP, which can be released during intestinal digestion, may function as bioactive constituents and carriers for different minerals, especially Ca, and may be used as ingredients in functional foods or pharmaceutical preparations.

Gastro‐duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential

Background The process of gastro‐duodenal digestion may play a role in determining the allergenic properties of food proteins. The sensitizing and allergenic potential of digestion products of highly degraded allergens, such as the major peanut allergen Ara h 1, is currently under debate. We evaluated the effect of in vitro gastro‐duodenal digestion of Ara h 1 on T cell reactivity and basophil histamine release.

Capacity of purified peanut allergens to induce degranulation in a functional in vitro assay: Ara h 2 and Ara h 6 are the most efficient elicitors

Background Peanut is a most common and potent food allergen. Many peanut allergens have been characterized using, in particular, IgE‐binding studies.

Post-translational phosphorylation affects the IgE binding capacity of caseins

IgE response specific to those molecular regions of casein that contain a major phosphorylation site was analyzed using native and modified caseins and derived peptides. This study included (i) the naturally occurring common variants A1 and A from β‐ and αs2‐caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of αs2‐casein which lacks one major phosphorylation site, and (iii) the native and dephosphorylated tryptic fragment f(1–25) from β‐casein. Direct and indirect ELISA using sera from patients allergic to milk showed that the IgE response to caseins is affected by modifying or eliminating the major phosphorylation site.

Serological characteristics of peanut allergy in children

Background:  Food challenge is considered an excellent clinical tool for the diagnosis of specific food allergy. However in the case of peanut allergy it may be difficult to perform because of the severity of the reactions. The quantitation of a specific immunoglobulin E (IgE) response to different peanut allergens could also contribute to the improvement of the diagnosis. We characterized the IgE response to a whole peanut protein extract and to Ara h 1 and Ara h 2 in different groups of patients classified according to the severity of their allergic reactions.

Oral tolerance and Treg cells are induced in BALB/c mice after gavage with bovine beta-lactoglobulin

To cite this article: Adel‐Patient K, Wavrin S, Bernard H, Meziti N, Ah‐Leung S, Wal J‐M. Oral tolerance and Treg cells are induced in BALB/c mice after gavage with bovine β‐lactoglobulin. Allergy 2011; 66: 1312–1321.

Oral tolerance and Treg cells are induced in BALB/c mice after gavage with bovine β‐lactoglobulin

To cite this article: Adel‐Patient K, Wavrin S, Bernard H, Meziti N, Ah‐Leung S, Wal J‐M. Oral tolerance and Treg cells are induced in BALB/c mice after gavage with bovine β‐lactoglobulin. Allergy 2011; 66: 1312–1321.