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Updated: Apr 4, 2026

Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
Dimerization of lipocalin allergens
Merja H Niemi1, Marja Rytkönen-Nissinen2,3, Ilja Miettinen1
1Department of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
Abstract:
Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution.
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