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http://purl.uniprot.org/citations/16911365http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16911365http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16911365http://www.w3.org/2000/01/rdf-schema#comment"

Background

Profilins are ubiquitous panallergens that have been extensively characterized; yet, their clinical relevance is still unclear.

Objective

The aim of the present study was to produce recombinant apple profilin (rMal d 4) and to evaluate its allergenic activity and its potency for component-resolved allergy diagnosis.

Methods

Complementary DNA-derived Mal d 4 was cloned, expressed in Escherichia coli and subsequently purified via poly (l-proline) sepharose. A total of 28 sera from apple-allergic patients were used for IgE-ELISA, immunoblot, RAST and basophil histamine release (BHR) test. In addition, skin prick tests (SPTs) were performed in five patients.

Results

Four different complementary DNA coding for apple profilin, Mal d 4, each with an open reading frame of 393 nucleotides, were identified. One isoform Mal d 4.0101 was expressed in Escherichia coli and subsequently purified. Mass spectroscopy revealed the expected mass of 13.826 for rMal d 4.0101, and circular dichroism analysis data were typical for a folded protein and small-angle X-ray scattering measurement identified the protein as a monomer. All the serum samples displayed IgE binding to rMal d 4.0101 in IgE ELISA, immunoblot and RAST. In immunoblotting, IgE binding to natural Mal d 4 was partially/completely inhibited by preincubation with rMal d 4.0101, and RAST values to apple extract were significantly reduced upon serum pretreatment with rMal d 4.0101. SPTs and BHR assays using purified rMal d 4.0101 were positive. Purified rMal d 4.0101 was destroyed within seconds when subjected to pepsin digestion.

Conclusions

Apple profilin complementary DNAs were identified. The physicochemical and allergenic properties of purified recombinant Mal d 4.0101 were evaluated showing that the recombinant protein was equal to the natural protein as shown by inhibition assays. Thus, Mal d 4 represents another example suitable for component-resolved diagnosis of food allergy."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2222.2006.02541.x"xsd:string
http://purl.uniprot.org/citations/16911365http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2222.2006.02541.x"xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Breiteneder H."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Breiteneder H."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Fernandez-Rivas M."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Fernandez-Rivas M."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ferreira F."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ferreira F."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Himly M."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Himly M."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Knulst A.C."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Knulst A.C."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ma Y."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ma Y."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ebner C."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Ebner C."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Hoffmann-Sommergruber K."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Hoffmann-Sommergruber K."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Gadermaier G."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"Gadermaier G."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"van Ree R."xsd:string
http://purl.uniprot.org/citations/16911365http://purl.uniprot.org/core/author"van Ree R."xsd:string
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