• Allergy · Aug 2009

    Molecular and immunological characterization of Asp f 34, a novel major cell wall allergen of Aspergillus fumigatus.

    • A G Glaser, A I Kirsch, S Zeller, G Menz, C Rhyner, and R Crameri.
    • Department Molecular Allergology, Swiss Institute of Allergy and Asthma Research, University of Zürich, Zürich, Switzerland.
    • Allergy. 2009 Aug 1; 64 (8): 1144-51.

    BackgroundAlthough fungal spores have been recognized as triggers of respiratory allergy and asthma, only two allergenic fungal cell wall components have so far been described.MethodsEighty-one sequences derived from an Aspergillus fumigatus cDNA library encoding putative allergens were examined for the presence of cell wall components. A new allergen (Asp f 34) was evaluated by Western blots, enzyme-linked immunosorbent assay (ELISA), peripheral blood mononuclear cell (PBMC) proliferation assays, and skin prick test (SPT).ResultsThe cDNA encoding Asp f 34 contained an open reading frame predicting a protein of 185 amino acids with a molecular weight of 19.38 kDa, showing sequence homology to phiA, an essential protein for the formation of conidia in the genus Aspergillus. The recombinant Asp f 34 was binding IgE from sensitized individuals in Western blots. An ELISA survey showed that 94% of the ABPA and 46% of the A. fumigatus-sensitized individuals tested had Asp f 34-specific serum IgE. Asp f 34 induced allergen-specific proliferation exclusively of PBMCs from patients sensitized to the allergen. Eight patients with anti-Asp f 34 serum IgE tested reacted positively in SPT, whereas four A. fumigatus-sensitized individuals without Asp f 34-specific IgE and eight healthy controls scored negatively.ConclusionsA cell wall protein of the phialides of A. fumigatus was identified as a major allergen. Asp f 34 belongs to the Aspergillus-specific proteins of the phiA family and has relevant potential for a specific diagnosis of Aspergillus sensitization.

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