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http://purl.uniprot.org/citations/9412580http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9412580http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9412580http://www.w3.org/2000/01/rdf-schema#comment"From an Aspergillus fumigatus complementary deoxyribonucleic acid (cDNA) library displayed on phage surface, an allergen formally termed rAsp f 3 was cloned. The open-reading frame of the cloned gene for the allergen encodes a protein of 168 amino acids with a predicted molecular mass of 18.5 kD, showing 36% identity and 58% similarity to two peroxisomal membrane proteins of Candida boidinii. Recombinant Asp f 3 was expressed as a [His]6-tagged fusion protein in Escherichia coil at yields of 30 mg/L, and was purified by Ni(2+)-chelate chromatography. In an enzyme-linked immunosorbent assay (ELISA), serum IgE antibody reactivity to rAsp f 3 could be detected in 72% of 89 individuals sensitized to A. fumigatus, demonstrating that the protein represents a major allergen of the mold. IgE specific to rAsp f 3 and the two recombinant Candida proteins was further demonstrated by IgE-immunoblot analysis. IgE binding to rAsp f 3 could be inhibited in the ELISA by adding either of the recombinant Candida peroxisomal proteins to sera containing IgE directed against Asp f 3. Taken together, these observations prove that the Asperigillus allergen and the two Candida proteins share IgE-binding epitopes."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.org/dc/terms/identifier"doi:10.1164/ajrccm.156.6.9702087"xsd:string
http://purl.uniprot.org/citations/9412580http://purl.org/dc/terms/identifier"doi:10.1164/ajrccm.156.6.9702087"xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Blaser K."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Blaser K."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Crameri R."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Crameri R."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Hemmann S."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/author"Hemmann S."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/name"Am. J. Respir. Crit. Care Med."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/name"Am. J. Respir. Crit. Care Med."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/pages"1956-1962"xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/pages"1956-1962"xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/title"Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/title"Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding epitopes."xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/volume"156"xsd:string
http://purl.uniprot.org/citations/9412580http://purl.uniprot.org/core/volume"156"xsd:string
http://purl.uniprot.org/citations/9412580http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9412580
http://purl.uniprot.org/citations/9412580http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9412580
http://purl.uniprot.org/citations/9412580http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9412580
http://purl.uniprot.org/citations/9412580http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9412580