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Polymorphism of Aspergillus fumigatus Major Allergen Genes Associating with Their Isolated Sites Affects Their IgE Epitope Structures

Rumi Konuma1, Maiko Watanabe2, Daisuke Irikura3, Yoshiko Sugita-Konishi2, 4, 5, Akiko Yamazaki6 U Yanagi 7, Doha Yahia8,9, Naoki Kobayashi10, Hiroji Chibana11, Jun-Ichi Onami12 , Yoichi Kamata2,6,14*

The circumstances in which organisms live induce polymorphism in their genes, including fungal allergen genes, leading to altered structures and functions of proteins, related to their pathogenicity. Major allergen genes of Aspergillus fumigatus, Asp f 1, Asp f 2, and Asp f 3, were examined in 59 strains [environment and animal/human- body origin] to determine their nucleotide sequences, and then categorized. The location and number of IgE epitopes on the allergen molecules were predicted using computer software. The Asp f 1 gene was classified into two groups (f1-1 and f1-2). One of the groups possessed one-nucleotide mutation point with one amino-acid substitution. The mutated Asp f 2 gene accompanying 6-amino acid substitution was classified into 7 groups (f2-1 to f2-7). Six of the groups possessed a newborn IgE epitope. The Asp f 3 gene contained two mutations, resulted in three groups (f3-1 to f3-3) without any amino-acid substitutions. Category E, consisting of group’s f1-1, f2-5, and f3-2, was specific to an environmental origin. Our findings suggest that nucleotide mutation of the fungal allergen genes, associated with the origin of the fungus, modifies the structure of proteins, and affects their pathogenic properties, such as the localization of IgE epitopes.