Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergy.

摘要: Owners and their domestic animals via skin shedding secretions, mutually exchange microbiomes, potential pathogens innate immune molecules. Among the latter especially lipocalins are multifaceted: they may have an immunomodulatory function and, furthermore, represent one of most important animal allergen families. The amino acid identities, as well structures by superposition modeling were compared among human lipocalins, hLCN1 hLCN2, lipocalin allergens, such Can f 1, 2 4 from dog, Fel d cats, Bos 5 cow's milk, Equ c 1 horses, Mus m mice, all them representing major allergens. β-barrel fold with a central molecular pocket is similar lipocalins. Thereby, able to transport variety biological ligands in highly conserved calyx-like cavity, siderophores strongest known capability complex iron (Fe(3+) ). Levels elevated nonallergic inflammation cancer, associated immunoregulatory functions that critically depend on ligand load. Accordingly, deficient loading allergens establishes capacity induce Th2 hypersensitivity. Our similarity analysis mammalian highlights immunity allergy.