Abstract
A vacuolar serine protease (Pen ch 18) has been identified as a major allergen of Penicillium chrysogenum. The molecular features of antigenic determinant(s) on Pen ch 18 recognized by human IgE antibodies, however, have remained unclear. Here, we show that a dominant IgE epitope on the N-terminally processed Pen ch 18 allergen was narrowed down to residues 83-91. In addition, Lys89, Lys90, and possibly Phe91 were identified as the core residues. Substitution of Lys89, Lys90, or Phe91 with alanine can significantly reduce IgE-binding to Pen ch 18. Immunoblot inhibition confirmed that Lys89 and Phe91 played a significant role in IgE-binding against Pen ch 18. Molecular modeling suggests they are located on a loop-like structure at or near the surface of the major fungal allergen.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allergens / chemistry
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Allergens / genetics
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Allergens / immunology*
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Antibodies, Fungal / immunology*
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Epitope Mapping
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Fungal Proteins / immunology*
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Humans
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Immunodominant Epitopes / chemistry
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Immunodominant Epitopes / genetics
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Immunodominant Epitopes / immunology*
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Immunoglobulin E / immunology*
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Lysine / genetics
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Lysine / immunology
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Mutation
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Penicillium chrysogenum / immunology*
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Phenylalanine / genetics
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Phenylalanine / immunology
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
Substances
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Allergens
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Antibodies, Fungal
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Fungal Proteins
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Immunodominant Epitopes
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Pen n 18 protein, Penicillium chrysogenum
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Recombinant Proteins
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Immunoglobulin E
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Phenylalanine
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Lysine