Dog allergen in indoor air and dust during dog shows

Abstract

Proteins (CMP) involved in milk allergy are numerous and heterogeneous, with very few structural or functional common features. This heterogeneity is complicated by their genetic polymorphism, resulting in several variants for each protein. These variants are characterized by point substitutions of amino acids or by deletions of peptide fragments of varying size or by post-translational modifications such as phosphorylation or glycosylation. All of these modifications may affect allergenicity. No common molecular structure can be associated with allergenicity, although some homologous regions such as casein phospho-peptides can explain an IgE cross-reactivity. Three-dimensional structure is an important feature in CMP allergenicity but denatured and linear epitopes are also involved. Epitopes are numerous and widely spread along the CMP molecule. They may be located in hydrophobic parts of the molecule where they are inaccessible for IgE antibodies in the native conformation of the protein but become bioavailable after digestive processes. Peptides as short as ca. 12-14 amino acid residues may account for a significant part of the allergenicity of the whole molecule, which justifies the need to be careful before proposing any CMP hydrolysate for highly allergenic children.

Eosinophilic Gastroenteritis due to Cow’s Milk Allergy Presenting with Acute Pancreatitis

“…The allergen was thought to be casein, β-lactoglobulin, or both. They are major heat-resistant milk allergens, and ingestion of products such as pasta with cream sauce, cheese, or dairy-based ice cream could induce allergic reactions [28]. It is possible that EGE has various pathogenic mechanisms.…”

Milk processing as a tool to reduce cow’s milk allergenicity: a mini-review

“…Ena et al (1995) found that a filter with molecular mass cut-off 3,000 Da decreased residual antigenicity of the Corolase 7092 WPC hydrolysate, but had little effect on the pepsin/carolase PP hydrolysate. Peptides still have allergenicity if epitopes exist, although their molecular masses may be very low (Wal 2001). This result suggests that it is crucial to choose the appropriate enzyme having specificities in antigenic epitopes to effectively decrease the allergenicity of proteins.…”

Physiological phosphatidylcholine protects bovine β‐lactoglobulin from simulated gastrointestinal proteolysis

“…The resistance of b-Lg to digestion, particularly in the gastric compartment, coupled with its absence from human milk has been proposed to contribute to the allergenicity of bovine b-Lg in human [16]. Several other allergens belonging to the lipocalin family have also been identified, including inhalant allergens such as mouse urinary protein, and several dander allergens [17].…”