Academic Journal
Molecular, Structural and Immunological Characterization of Der p 18, a Chitinase-Like House Dust Mite Allergen.
| Title: | Molecular, Structural and Immunological Characterization of Der p 18, a Chitinase-Like House Dust Mite Allergen. |
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| Authors: | Yvonne Resch, Katharina Blatt, Ursula Malkus, Christian Fercher, Ines Swoboda, Margit Focke-Tejkl, Kuan-Wei Chen, Susanne Seiberler, Irene Mittermann, Christian Lupinek, Azahara Rodriguez-Dominguez, Petra Zieglmayer, René Zieglmayer, Walter Keller, Vladislav Krzyzanek, Peter Valent, Rudolf Valenta, Susanne Vrtala |
| Source: | PLoS ONE, Vol 11, Iss 8, p e0160641 (2016) |
| Publisher Information: | Public Library of Science (PLoS), 2016. |
| Publication Year: | 2016 |
| Collection: | LCC:Medicine LCC:Science |
| Subject Terms: | Medicine, Science |
| More Details: | BACKGROUND:The house dust mite (HDM) allergen Der p 18 belongs to the glycoside hydrolase family 18 chitinases. The relevance of Der p 18 for house dust mite allergic patients has only been partly investigated. OBJECTIVE:To perform a detailed characterization of Der p 18 on a molecular, structural and immunological level. METHODS:Der p 18 was expressed in E. coli, purified to homogeneity, tested for chitin-binding activity and its secondary structure was analyzed by circular dichroism. Der p 18-specific IgG antibodies were produced in rabbits to localize the allergen in mites using immunogold electron microscopy and to search for cross-reactive allergens in other allergen sources (i.e. mites, crustacea, mollusca and insects). IgE reactivity of rDer p 18 was tested with sera from clinically well characterized HDM-allergic patients (n = 98) and its allergenic activity was analyzed in basophil activation experiments. RESULTS:Recombinant Der p 18 was expressed and purified as a folded, biologically active protein. It shows weak chitin-binding activity and partial cross-reactivity with Der f 18 from D. farinae but not with proteins from the other tested allergen sources. The allergen was mainly localized in the peritrophic matrix of the HDM gut and to a lower extent in fecal pellets. Der p 18 reacted with IgE from 10% of mite allergic patients from Austria and showed allergenic activity when tested for basophil activation in Der p 18-sensitized patients. CONCLUSION:Der p 18 is a rather genus-specific minor allergen with weak chitin-binding activity but exhibits allergenic activity and therefore should be included in diagnostic test panels for HDM allergy. |
| Document Type: | article |
| File Description: | electronic resource |
| Language: | English |
| ISSN: | 1932-6203 |
| Relation: | http://europepmc.org/articles/PMC4993390?pdf=render; https://doaj.org/toc/1932-6203 |
| DOI: | 10.1371/journal.pone.0160641 |
| Access URL: | https://doaj.org/article/461a488a873d4b949bd136a203c70cca |
| Accession Number: | edsdoj.461a488a873d4b949bd136a203c70cca |
| Database: | Directory of Open Access Journals |
| ISSN: | 19326203 |
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| DOI: | 10.1371/journal.pone.0160641 |
| Published in: | PLoS ONE |
| Language: | English |