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Der-p2 ( Dermatophagoides pteronyssinus) allergen-like protein from the hard tick Ixodes ricinus - a novel member of ML (MD-2-related lipid-recognition) domain protein family
J. Horácková, N. Rudenko, M. Golovchenko, L. Grubhoffer,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
ProQuest Central
od 2001-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 2001-01-01 do Před 1 rokem
Public Health Database (ProQuest)
od 2001-01-01 do Před 1 rokem
ROAD: Directory of Open Access Scholarly Resources
od 1908
- MeSH
- alergeny chemie genetika imunologie metabolismus MeSH
- antigeny roztočů domácího prachu chemie genetika imunologie metabolismus MeSH
- Dermatophagoides pteronyssinus imunologie MeSH
- imunoglobulin E imunologie metabolismus MeSH
- klíště genetika růst a vývoj imunologie metabolismus MeSH
- larva růst a vývoj imunologie MeSH
- lymfocytární antigen 96 chemie imunologie MeSH
- molekulární modely MeSH
- nymfa růst a vývoj imunologie MeSH
- rekombinantní proteiny chemie genetika imunologie metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční analýza DNA MeSH
- zvířata MeSH
- Check Tag
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
OBJECTIVE: Expression of the gene encoding Der-p2 allergen-like protein in the castor bean tick Ixodes ricinus is induced by blood intake. Tick Der-p2 allergen-like protein belongs to a diverse family of ML proteins that includes major allergens of house dust mites, human MD-2 or similar proteins from Drosophila melanogaster. In ticks, genes encoding proteins belonging to the ML protein family were identified, but their protein products have not been characterized yet. METHODS: A gene encoding tick Der-p2 allergen-like protein was amplified from cDNA of engorged I. ricinus female using the gene-specific primers designed on a basis of partial sequences of related allergen-like genes. The tissue and state specific patterns of expression of the gene were analysed. The IgE binding activity of the produced recombinant protein was studied by use of ELISA. RESULTS: Analysis of the expression pattern showed that the gene encoding the tick Der-p2 allergen-like protein is strongly induced by the bloodmeal in gut and haemolymph throughout all tick developmental stages. Der-p2 allergen-like protein possesses a putative lipid-binding site, according to the comparisons with the related proteins. The ability of tick Der-p2 allergen-like protein to bind immunoglobulin E (IgE) was revealed. DISCUSSION: The presence of a putative lipid-binding domain in Der-p2 allergen-like protein and its ability to interact with IgE might indicate the involvement of the protein in the tick's immune response.
Citace poskytuje Crossref.org
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