Niemi Merja H, Rytkönen-Nissinen Marja, Miettinen Ilja, Jänis Janne, Virtanen Tuomas, Rouvinen Juha
Department of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.
Department of Clinical Microbiology, Institute of Clinical Medicine and Biocenter Kuopio, University of Eastern Finland, PO BOX 1627, 70211 Kuopio, Finland.
Sci Rep. 2015 Sep 8;5:13841. doi: 10.1038/srep13841.
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.
脂质运载蛋白是吸入性动物过敏原中最重要的类别之一。分析这些蛋白质的结构特征对于深入了解其致敏性很重要。我们已经确定了牛毛发皮脂质运载蛋白Bos d 2的两种不同的二聚体晶体结构，该蛋白此前被描述为单体过敏原。对所有其他已确定的脂质运载蛋白过敏原的晶体结构分析也揭示了寡聚结构，这些结构在二聚体形成过程中广泛利用了β-折叠的固有结构特征。根据单体-单体界面的适度大小，这些二聚体中的大多数在溶液中是短暂存在的。采用原生质体质谱法定量表征了两种脂质运载蛋白过敏原Bos d 2和Bos d 5在溶液中的瞬时二聚化。
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