Identification of Der p 23, a Peritrophin-like Protein, as a New Major Dermatophagoides pteronyssinus Allergen Associated with the Peritrophic Matrix of Mite Fecal Pellets

被引:161
作者
Weghofer, Margit [1 ]
Grote, Monika [2 ]
Resch, Yvonne [1 ]
Casset, Anne [1 ]
Kneidinger, Michael [3 ]
Kopec, Jolanta [4 ]
Thomas, Wayne R. [5 ]
Fernandez-Caldas, Enrique [6 ]
Kabesch, Michael [7 ]
Ferrara, Rosetta [8 ]
Mari, Adriano [8 ]
Purohit, Ashok [9 ]
Pauli, Gabrielle [9 ]
Horak, Friedrich [10 ]
Keller, Walter [4 ]
Valent, Peter [3 ]
Valenta, Rudolf [1 ]
Vrtala, Susanne [1 ]
机构
[1] Med Univ Vienna, Div Immunopathol, Dept Pathophysiol & Allergy Res, Ctr Pathophysiol Infectiol & Immunol, A-1090 Vienna, Austria
[2] Univ Munster, Inst Med Phys & Biophys, D-48143 Munster, Germany
[3] Med Univ Vienna, Div Hematol & Hemostaseol, Dept Internal Med 1, A-1090 Vienna, Austria
[4] Karl Franzens Univ Graz, Inst Mol Biosci, Div Struct Biol, A-8010 Graz, Austria
[5] Univ Western Australia, Telethon Inst Child Hlth Res, Ctr Child Hlth Res, Perth 6000, Australia
[6] Inmunotek, Madrid 28006, Spain
[7] KUNO Univ, Childrens Hosp Regensburg, D-93006 Regensburg, Germany
[8] IDI IRCCS, Ctr Mol Allergol, I-00167 Rome, Italy
[9] Strasbourg Univ Hosp, Dept Chest Dis, Div Asthma & Allergol, F-6709 Strasbourg, France
[10] Allergy Ctr Vienna West, A-1150 Vienna, Austria
基金
奥地利科学基金会;
关键词
CONSERVED DOMAIN DATABASE; HOUSE-DUST; BRONCHIAL-ASTHMA; RECOMBINANT; IMMUNOTHERAPY; DER-P-1; CDNA; GUT; CHITINASES; EXPRESSION;
D O I
10.4049/jimmunol.1202288
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
The house dust mite (HDM) Dermatophagoides pteronyssinus is one of most important allergen sources and a major elicitor of allergic asthma. We screened a D. pteronyssinus expression cDNA library with IgE Abs from HDM allergic patients. A cDNA coding for a new major allergen was isolated, which showed sequence homology to peritrophins, which contain chitin-binding domains and are part of the peritrophic matrix lining the gut of arthropods. The mature Der p 23 allergen was expressed in Escherichia coli as an 8-kDa protein without its hydrophobic leader sequence and purified to homogeneity. It reacted with IgE Abs from 74% of D. pteronyssinus allergic patients (n = 347) at levels comparable to the two major HDM allergens, Der p 1 and Der p 2. Thus, Der p 23 represents a new major D. pteronyssinus allergen. Furthermore, rDer p 23 exhibited high allergenic activity as demonstrated by upregulation of CD203c expression on basophils from D. pteronyssinus allergic patients. Immunogold electron microscopy localized the allergen in the peritrophic matrix lining the midgut of D. pteronyssinus as well as on the surface of the fecal pellets. Thus, we identified a new major D. pteronyssinus allergen as peritrophin-like protein. The high allergenic activity of Der p 23 and its frequent recognition as respiratory allergen may be explained by the fact that it becomes airborne and respirable through its association with mite feces. Der p 23 may be an essential component for diagnosis and specific immunotherapy of HDM allergy. The Journal of Immunology, 2013, 190: 3059-3067.
引用
收藏
页码:3059 / 3067
页数:9
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