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sinolysis, digestion by trypsin and chymotrypsin results in partial digestion of BLG containing approximately 15% of intact BLG. After dissociation of the intact BLG, the remaining peptide fragments that included proteins with M r <5,000 in size completely lost sensitizing capacity measured by the development of specific IgE responses after intraperitoneal sensitization. This differs from what is known about peanut and cashew digests [4–6] that retain their sensitization potential even after gastric or gastroduodenal digestion that results in virtually complete digestion of the proteins both in vitro and in vivo using animal models. Unfortunately, in the paper by Lindholm Bogh et al. [3] , the sensitizing potential was only assessed based on the development of specific IgE responses and not on the response to an oral feeding test. Even more interestingly, co-administration of intact BLG together with BLG digests resulted in reduced immunogenicity (measured by the development of humoral responses) when compared to the administration of intact BLG alone, although the preparations contained the same amount of intact BLG. As the authors speculate this could be through epitope masking by peptide fragments in the intact protein aggregate, which the authors, however, demonstrated not to occur. Alternatively, BLG peptide fragments could result in the development of toleroCow’s milk is the first foreign protein consumed in large quantities by the infant. Most infants develop oral tolerance to milk protein, i.e. inability to mount systemic immune responses after oral administration of a protein. However, cow’s milk allergy (CMA) develops in approximately 2–3% of young children. Early introduction of milk formula during the first 3 days of life has been associated with an increase in CMA [1] , whereas hydrolyzed formulas have been recommended for the prevention of CMA in high-risk individuals [2] . Caseins are the major allergens responsible for CMA comprising about 80% of the total protein content in cow’s milk, but the whey fraction also includes allergenic proteins such as α-lactalbumin and β-lactoglobulin (BLG). It is currently not fully appreciated what makes some dietary proteins allergens, although resistance against heat-de na turing and gastric fluid treatment may play an important role. Its absence in breast milk may be a crucial component of the allergenicity of BLG, although the presence of caseins in human milk does not exclude them as major allergens. In the paper by Lindholm Bogh et al. [3] , the sensitizing potential of BLG and its gastroduodenal digests was assessed by measuring humoral responses in a food allergy-prone Brown Norway rat model. The authors show that while BLG is virtually completely resistant to pepPublished online: March 15, 2013

Allergy Prevention via Co-Administration of Intact Food Allergen and Its Epitope Soup?