Molecular cloning of IgE-binding fragments of Alternaria alternata allergens.

Exposure to the hyphomycete Alternaria alternata is recognized as an important risk factor for asthma. IgE immunoblotting has been used to catalogue the number and Mr of allergens in A. alternata extracts, with estimates ranging from 10 to 30, although few are present in nearly all extracts studied.

Isolation and expression of a cDNA clone encoding an Alternaria alternata Alt a 1 subunit.

Alternaria alternata is recognized as an important source of fungal aeroallergens. Alt a 1, the major allergen of this mold, is a dimer of disulfide-linked subunits that migrate in SDS-PAGE under reducing conditions at apparent M(r)s of 14,500 and 16,000. IgE antibodies to this protein are present in the sera of >90% of A.

An allergenic polypeptide representing a variable region of hsp 70 cloned from a cDNA library of Cladosporium herbarum.

Background: Extracts of Cladosporium herbarum, a major source of fungal aeroallergens, exhibit a complex profile of IgE-binding proteins. Yields of conventionally purified allergens from this mold have been insufficient to permit further molecular analyses.

Objective: To enhance and simplify the purification of allergens from C.

N-terminus of a major allergen, Alt a I, of Alternaria alternata defined to be an epitope.

A 20mer peptide representing the N-terminus of a major allergen, Alt a I, of Alternaria alternata was synthesized and examined for its antibody binding and antibody induction activities. Alt a I peptide-BSA conjugate reacted with both human IgE and rabbit anti-Alt a I IgG in ELISA, albeit the binding of the peptide to IgE was relatively weak. Control conjugate showed no antibody binding.