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

Kåre H Meno; Jette S Kastrup; I-Chun Kuo; Kaw Yan Chua; Michael Gajhede

doi:10.1111/all.13111

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

Kåre H Meno, Jette S Kastrup, I-Chun Kuo, Kaw Yan Chua, Michael Gajhede

8 Citations (Scopus)

Abstract

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 Å 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.

Original language	English
Article number	13111
Journal	Allergy
Volume	72
Issue number	4
Pages (from-to)	665-670
Number of pages	6
ISSN	0105-4538
DOIs	https://doi.org/10.1111/all.13111
Publication status	Published - 1 Apr 2017

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

abstract = "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 {\AA} 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.",

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T1 - The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1

AU - Meno, Kåre H

AU - Kastrup, Jette S

AU - Kuo, I-Chun

AU - Chua, Kaw Yan

AU - Gajhede, Michael

PY - 2017/4/1

Y1 - 2017/4/1

N2 - 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 Å 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.

AB - 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 Å 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.

U2 - 10.1111/all.13111

DO - 10.1111/all.13111

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

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