ORBi: Bouaziz Ahlem - Analysis of the allergenicity of natural and recombinant Der p 3

Reference : Analysis of the allergenicity of natural and recombinant Der p 3


	Document type :	Scientific congresses and symposiums : Poster
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/126122

Title :	Analysis of the allergenicity of natural and recombinant Der p 3
Language :	English
Author, co-author :	Bouaziz, Ahlem [Université de Liège - ULg > > > Doct. sc. (bioch., biol. mol.&cell., bioinf.&mod.-Bologne)]
	Campisi, vincent [Université de Liège - ULg > > > >]
	Herman, julie [Université de Liège - ULg > > > >]
	Walgraffe, David [Université Libre de Bruxelles - ULB > > > >]
	Jacquet, Alain []
	Hentges, françois []
	Emmanuelle, Adam [Université Libre de Bruxelles - ULB > > > >]
	galleni, Moreno [ulg > > > >]
	Dumez, Marie-Eve []
Publication date :	19-Jun-2012
Page number :	A0 (90x120)
Peer reviewed :	Yes
Audience :	International
Event name :	31éme congrès European Academy of allergy and Clinical Immunology
Event date :	du 16 juin au 20 juin 2012
Event place (city) :	Genève
Event country :	Suisse
Keywords :	[en] allergy, Der p 3, autolysis
Abstract :	[en] Background: Der p 3 a trypsin-like protease is a Dermatophagoides pteronyssinus allergen which is synthesized in the mite under a zymogen form. The enzymatic activity of this allergen has been shown to enhance the inflammatory process of allergy. To date, there are a few studies that described the allergenicity and the IgE reactivity of the group 3 allergens, the allergenic properties of recombinant Der p 3 was also not characterized. Methods: The autolysis of rDer p 3 and rDer p 3 S196A were analyzed by means of SDS-PAGE and enzymatic activity and their allergenicities by means of assays for IgE binding, IgE binding inhibition and basophiles mediator-release. Results: 100% of the sera from allergic patients showed IgE reactivity to natural Der p 3 and recombinant form. However, the IgE binding to the Der p 3 was less 4 times than rDer p 1. The IgE binding to rDer p 3 S196A was higher than rDer p 3. These variations can be linked with the phenomen of autolysis and instability of Der p 3 during the ELISA test. The mediators release performed with RBL sensitized with sera from allergic patients and stimulated with rDer p3, rDer p 3 S196A and natural Der p 3 were similar and lower than Der p 1 for concentration < 10 ng/ml. Conclusions: recombinant mature Der p 3 retained overall identity to its natural form in terms of structure and allergenicity. The instability and autolysis of Der p 3 drastically influence its IgE binding capacity. These results can be explain the considerable variations with the frequencies reactivity (16-100%) of natural Der p 3. The RBL assays demonstrated that the allergenicity of rDer p 3 is similar to rDer p 1 for the concentrations >10 ng /ml.
Permalink :	http://hdl.handle.net/2268/126122

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