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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1. / Meno, Kåre H; Kastrup, Jette S; Kuo, I-Chun; Chua, Kaw Yan; Gajhede, Michael.

In: Allergy, Vol. 72, No. 4, 13111, 01.04.2017, p. 665-670.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Meno, KH, Kastrup, JS, Kuo, I-C, Chua, KY & Gajhede, M 2017, 'The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1', Allergy, vol. 72, no. 4, 13111, pp. 665-670. https://doi.org/10.1111/all.13111

APA

Meno, K. H., Kastrup, J. S., Kuo, I-C., Chua, K. Y., & Gajhede, M. (2017). The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1. Allergy, 72(4), 665-670. [13111]. https://doi.org/10.1111/all.13111

Vancouver

Meno KH, Kastrup JS, Kuo I-C, Chua KY, Gajhede M. The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1. Allergy. 2017 Apr 1;72(4):665-670. 13111. https://doi.org/10.1111/all.13111

Author

Meno, Kåre H ; Kastrup, Jette S ; Kuo, I-Chun ; Chua, Kaw Yan ; Gajhede, Michael. / The structure of the mite allergen Blo t 1 explains the limited antibody cross-reactivity to Der p 1. In: Allergy. 2017 ; Vol. 72, No. 4. pp. 665-670.

Bibtex

@article{66308365ea9e4dfa8cf87a103d383e42,
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. This article is protected by copyright. All rights reserved.",
author = "Meno, {K{\aa}re H} and Kastrup, {Jette S} and I-Chun Kuo and Chua, {Kaw Yan} and Michael Gajhede",
note = "This article is protected by copyright. All rights reserved.",
year = "2017",
month = apr,
day = "1",
doi = "10.1111/all.13111",
language = "English",
volume = "72",
pages = "665--670",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
issn = "0105-4538",
publisher = "Wiley Online",
number = "4",

}

RIS

TY - JOUR

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

N1 - This article is protected by copyright. All rights reserved.

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. This article is protected by copyright. All rights reserved.

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. This article is protected by copyright. All rights reserved.

U2 - 10.1111/all.13111

DO - 10.1111/all.13111

M3 - Journal article

C2 - 27997997

VL - 72

SP - 665

EP - 670

JO - Allergy: European Journal of Allergy and Clinical Immunology

JF - Allergy: European Journal of Allergy and Clinical Immunology

SN - 0105-4538

IS - 4

M1 - 13111

ER -

ID: 172100696