Crystal Structure of the Dog Lipocalin Allergen Can f 2: Implications for Cross-reactivity to the Cat Allergen Fel d 4

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• 作者：Chaithanya Madhurantakam ; Ola B. Nilsson ; Hannes Uchtenhagen ; Jon Konradsen ; Tiiu Saarne ; Erik Hö ; gbom ; Tatyana S ; alova ; Hans Grö ; nlund ; Adnane Achour
• 关键词：dog allergen ; crystal structure ; recombinant Can f 2 ; epitope ; lipocalin fold
• 刊名：Journal of Molecular Biology
• 出版年：2010
• 出版时间：6 August 2010
• 年：2010
• 卷：401
• 期：1
• 页码：68-83
• 全文大小：2502 K

文摘

The dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. Here, the first crystal structure of recombinant rCan f 2 at 1.45 Å resolution displays a classical lipocalin fold with a conserved Gly-Xaa-Trp motif, in which Trp19 stabilizes the overall topology of the monomeric rCan f 2. Phe38 and Tyr84 localized on the L1 and L5 loops, respectively, control access to the highly hydrophobic calyx. Although the rCan f 2 calyx is nearly identical with the aero-allergens MUP1, Equ c 1 and A2U from mouse, horse and rat, respectively, no IgE cross-reactivity was found using sera from five mono-sensitized subjects. However, clear IgE cross-reactivity was demonstrated between Can f 2 and the cat allergen Fel d 4, although they share less than 22 % sequence identity. This suggests a role for these allergens in co-sensitization between cat- and dog-allergic patients.