The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1

被引：15

作者：

Meno, K. H. ^{[1
]}

Kastrup, J. S. ^{[2
]}

Kuo, I-C ^{[3
,4
]}

Chua, K. Y. ^{[3
,5
]}

Gajhede, M. ^{[2
]}

机构：

[1] ALK Abello AS, Global Res, Horsholm, Denmark

[2] Univ Copenhagen, Biostruct Res, Dept Drug Design & Pharmacol, Jagtvej 162, DK-2100 Copenhagen, Denmark

[3] Natl Univ Singapore, Yong Loo Lin Sch Med, Dept Paediat, Singapore, Singapore

[4] Natl Univ Hlth Syst, Khoo Teck Puat Natl Univ Childrens Med Inst, Singapore, Singapore

[5] Natl Univ Singapore, Immunol Programme, Ctr Life Sci, Singapore, Singapore

来源：

ALLERGY | 2017年 / 72卷 / 04期

关键词：

Blomia tropicalis mite allergen; crystal structure; cysteine protease; human IgE epitopes; pro-peptide; MONOCLONAL-ANTIBODIES; BLO-T-1; TROPICALIS;

D O I：

10.1111/all.13111

中图分类号：

R392 [医学免疫学];

学科分类号：

100102 ;

摘要：

The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic asthma and rhinitis in tropical and subtropical regions. Here, we report the crystal structure of one of the allergens from Blo t, recombinant proBlo t 1 (rproBlo t 1), determined at 2.1 angstrom resolution. Overall, the fold of rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG epitopes to the same surface patch on Blo t 1, as well as of sequence identity of surface-exposed residues, suggests limited cross-reactivity between these allergens and Blo t 1. This is in agreement with ELISA inhibition results showing that, although cross-reactive human IgE epitopes exist, there are unique IgE epitopes for both Blo t 1 and Der p 1.

引用

页码：665 / 670

页数：6

共 24 条

[1] Structural basis for the recognition and cleavage of histone H3 by cathepsin L [J].

Adams-Cioaba, Melanie A. ;

Krupa, Joanne C. ;

Xu, Chao ;

Mort, John S. ;

Min, Jinrong .

NATURE COMMUNICATIONS, 2011, 2

[2] Towards automated crystallographic structure refinement with phenix.refine [J].

Afonine, Pavel V. ;

Grosse-Kunstleve, Ralf W. ;

Echols, Nathaniel ;

Headd, Jeffrey J. ;

Moriarty, Nigel W. ;

Mustyakimov, Marat ;

Terwilliger, Thomas C. ;

Urzhumtsev, Alexandre ;

Zwart, Peter H. ;

Adams, Paul D. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2012, 68 :352-367

[3] Analysis of mite allergic patients in a diverse territory by improved diagnostic tools [J].

Barber, D. ;

Arias, J. ;

Boquete, M. ;

Cardona, V. ;

Carrillo, T. ;

Gala, G. ;

Gamboa, P. ;

Garcia-Robaina, J. C. ;

Hernandez, D. ;

Sanz, M. L. ;

Tabar, A. I. ;

Vidal, C. ;

Ipsen, H. ;

de la Torre, F. ;

Lombardero, M. .

CLINICAL AND EXPERIMENTAL ALLERGY, 2012, 42 (07) :1129-1138

[4] Lack of human IgE cross-reactivity between mite allergens Blo t 1 and Der p 1 [J].

Cheong, N ;

Soon, SC ;

Ramos, JDA ;

Kuo, IC ;

Kolortkar, PR ;

Lee, BW ;

Chua, KY .

ALLERGY, 2003, 58 (09) :912-920

[5] Molecular Determinants for Antibody Binding on Group 1 House Dust Mite Allergens [J].

Chruszcz, Maksymilian ;

Pomes, Anna ;

Glesner, Jill ;

Vailes, Lisa D. ;

Osinski, Tomasz ;

Porebski, Przemyslaw J. ;

Majorek, Karolina A. ;

Heymann, Peter W. ;

Platts-Mills, Thomas A. E. ;

Minor, Wladek ;

Chapman, Martin D. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (10) :7388-7398

[6]

Chua KY, 2007, PROTEIN PEPTIDE LETT, V14, P325

[7] Structure of allergens and structure based epitope predictions [J].

Dall'Antonia, Fabio ;

Pavkov-Keller, Tea ;

Zangger, Klaus ;

Keller, Walter .

METHODS, 2014, 66 (01) :3-21

[8] Features and development of Coot [J].

Emsley, P. ;

Lohkamp, B. ;

Scott, W. G. ;

Cowtan, K. .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2010, 66 :486-501

[9]

Ghaemmaghami AM, 2001, EUR J IMMUNOL, V31, P1211, DOI 10.1002/1521-4141(200104)31:4<1211::AID-IMMU1211>3.0.CO

[10]

2-R

← 1 2 3 →