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

被引:60
作者
Madhurantakam, Chaithanya [1 ]
Nilsson, Ola B. [2 ]
Uchtenhagen, Hannes [1 ]
Konradsen, Jon [3 ]
Saarne, Tiiu [2 ]
Hogbom, Erik [4 ]
Sandalova, Tatyana [5 ]
Gronlund, Hans [6 ]
Achour, Adnane [1 ]
机构
[1] Karolinska Inst, Karolinska Univ Hosp Huddinge, Dept Med Huddinge, Ctr Infect Med, Stockholm, Sweden
[2] Karolinska Inst, Dept Med, Clin Immunol & Allergy Unit, Stockholm, Sweden
[3] Karolinska Univ Hosp, Astrid Lindgren Childrens Hosp, Stockholm, Sweden
[4] Phadia AB, Uppsala, Sweden
[5] Karolinska Inst, Dept Med Biophys & Biochem, Stockholm, Sweden
[6] Karolinska Inst, Dept Environm Med, Ctr Allergy Res, Stockholm, Sweden
关键词
dog allergen; crystal structure; recombinant Can f 2; epitope; lipocalin fold; RETINOL-BINDING-PROTEIN; BOVINE BETA-LACTOGLOBULIN; 3-DIMENSIONAL STRUCTURE; SALIVARY LIPOCALIN; PHEROMONE BINDING; MAJOR ALLERGEN; TRIGONAL FORM; CRYSTALLIZATION; REFINEMENT; REVEALS;
D O I
10.1016/j.jmb.2010.05.043
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:68 / 83
页数:16
相关论文
共 73 条
[1]   Lipocalins:: unity in diversity [J].
Åkerstrom, B ;
Flower, DR ;
Salier, JP .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 2000, 1482 (1-2) :1-8
[2]   Prediction of residues in discontinuous B-cell epitopes using protein 3D structures [J].
Andersen, Pernille Haste ;
Nielsen, Morten ;
Lund, Ole .
PROTEIN SCIENCE, 2006, 15 (11) :2558-2567
[3]   The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling [J].
Arnold, K ;
Bordoli, L ;
Kopp, J ;
Schwede, T .
BIOINFORMATICS, 2006, 22 (02) :195-201
[4]   PHEROMONE BINDING-PROTEINS OF THE MOUSE, MUS-MUSCULUS [J].
BACCHINI, A ;
GAETANI, E ;
CAVAGGIONI, A .
EXPERIENTIA, 1992, 48 (04) :419-421
[5]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[6]   A MAJOR CONTINUOUS ALLERGENIC EPITOPE OF BOVINE BETA-LACTOGLOBULIN RECOGNIZED BY HUMAN IGE BINDING [J].
BALL, G ;
SHELTON, MJ ;
WALSH, BJ ;
HILL, DJ ;
HOSKING, CS ;
HOWDEN, MEH .
CLINICAL AND EXPERIMENTAL ALLERGY, 1994, 24 (08) :758-764
[7]   CASTp: Computed atlas of surface topography of proteins [J].
Binkowski, TA ;
Naghibzadeh, S ;
Liang, J .
NUCLEIC ACIDS RESEARCH, 2003, 31 (13) :3352-3355
[8]   PHEROMONE BINDING TO 2 RODENT URINARY PROTEINS REVEALED BY X-RAY CRYSTALLOGRAPHY [J].
BOCSKEI, Z ;
GROOM, CR ;
FLOWER, DR ;
WRIGHT, CE ;
PHILLIPS, SEV ;
CAVAGGIONI, A ;
FINDLAY, JBC ;
NORTH, ACT .
NATURE, 1992, 360 (6400) :186-188
[9]   TopDraw: a sketchpad for protein structure topology cartoons [J].
Bond, CS .
BIOINFORMATICS, 2003, 19 (02) :311-312
[10]   Variants of the Antibody Herceptin That Interact with HER2 and VEGF at the Antigen Binding Site [J].
Bostrom, Jenny ;
Yu, Shang-Fan ;
Kan, David ;
Appleton, Brent A. ;
Lee, Chingwei V. ;
Billeci, Karen ;
Man, Wenyan ;
Peale, Franklin ;
Ross, Sarajane ;
Wiesmann, Christian ;
Fuh, Germaine .
SCIENCE, 2009, 323 (5921) :1610-1614