Molecular, Structural and Immunological Characterization of Der p 18, a Chitinase-Like House Dust Mite Allergen
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081731%3A_____%2F16%3A00465043" target="_blank" >RIV/68081731:_____/16:00465043 - isvavai.cz</a>
Result on the web
<a href="http://journals.plos.org/plosone/article/asset?id=10.1371/journal.pone.0160641.PDF" target="_blank" >http://journals.plos.org/plosone/article/asset?id=10.1371/journal.pone.0160641.PDF</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0160641" target="_blank" >10.1371/journal.pone.0160641</a>
Alternative languages
Result language
angličtina
Original language name
Molecular, Structural and Immunological Characterization of Der p 18, a Chitinase-Like House Dust Mite Allergen
Original language description
Background nThe 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. nnObjective nTo perform a detailed characterization of Der p 18 on a molecular, structural and immunological level. nnMethods nDer 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. nnResults nRecombinant 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. nnConclusion nDer 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
JA - Electronics and optoelectronics
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS ONE
ISSN
1932-6203
e-ISSN
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Volume of the periodical
11
Issue of the periodical within the volume
8
Country of publishing house
US - UNITED STATES
Number of pages
19
Pages from-to
"e0160641:1"-"19"
UT code for WoS article
000381768400017
EID of the result in the Scopus database
2-s2.0-84984688866