Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 401, Issue 1, Pages 68-83Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.05.043
Keywords
dog allergen; crystal structure; recombinant Can f 2; epitope; lipocalin fold
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Funding
- Swedish Asthma and Allergy Research
- Konsul Th C Bergh's Foundations
- Center for Allergy Research
- European community [FP7/2007-2013, 226716]
- Bernard Osher Initiative for Research on Severe Asthma at the Karolinska Institute
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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 angstrom 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. (C) 2010 Elsevier Ltd. All rights reserved.
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