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Molecular, Structural and Immunological Characterization of Der p 18, a Chitinase-Like House Dust Mite Allergen
Y. Resch, K. Blatt, U. Malkus, C. Fercher, I. Swoboda, M. Focke-Tejkl, KW. Chen, S. Seiberler, I. Mittermann, C. Lupinek, A. Rodriguez-Dominguez, P. Zieglmayer, R. Zieglmayer, W. Keller, V. Krzyzanek, P. Valent, R. Valenta, S. Vrtala,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články
NLK
Directory of Open Access Journals
od 2006
Free Medical Journals
od 2006
Public Library of Science (PLoS)
od 2006
PubMed Central
od 2006
Europe PubMed Central
od 2006
ProQuest Central
od 2006-12-01
Open Access Digital Library
od 2006-10-01
Open Access Digital Library
od 2006-01-01
Open Access Digital Library
od 2006-01-01
Medline Complete (EBSCOhost)
od 2008-01-01
Nursing & Allied Health Database (ProQuest)
od 2006-12-01
Health & Medicine (ProQuest)
od 2006-12-01
Public Health Database (ProQuest)
od 2006-12-01
ROAD: Directory of Open Access Scholarly Resources
od 2006
- MeSH
- antigeny roztočů domácího prachu chemie genetika imunologie MeSH
- antisérum chemie MeSH
- bazofily cytologie účinky léků imunologie MeSH
- chitin chemie imunologie MeSH
- Escherichia coli genetika metabolismus MeSH
- exprese genu MeSH
- interakční proteinové domény a motivy MeSH
- klonování DNA MeSH
- konformace proteinů, alfa-helix MeSH
- konformace proteinů, beta-řetězec MeSH
- králíci MeSH
- lidé MeSH
- proteiny členovců chemie genetika imunologie MeSH
- protilátky krev chemie izolace a purifikace MeSH
- Pyroglyphidae chemie ultrastruktura MeSH
- rekombinantní proteiny chemie genetika imunologie MeSH
- respirační alergie chemicky indukované imunologie patofyziologie MeSH
- sbalování proteinů MeSH
- sekvence aminokyselin MeSH
- sekvenční homologie aminokyselin MeSH
- sekvenční seřazení MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- lidé MeSH
- mužské pohlaví MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
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.
Division of Structural Biology Institute of Molecular Biosciences University of Graz Graz Austria
Institute of Medical Physics and Biophysics University of Münster Münster Germany
Citace poskytuje Crossref.org
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- $a 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.
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