Abstract
A major 18-kD IgE-binding protein from Aspergillus fumigatus (Asp fI) has been purified. Partial amino acid sequencing of Asp f I showed extensive sequence homology (95%) between Asp fI and a cytotoxin (mitogillin) produced by A. restrictus. Crossinhibition radioimmunoassay using murine monoclonal antibody and human IgG and IgE antibodies showed that Asp fI and mitogillin were antigenically indistinguishable. Furthermore, both proteins inhibited protein synthesis in vitro by greater than 90%. Asp fI was expressed in A. fumigatus but not in seven other Aspergillus species. The results suggest that Asp fI could play a dual role in the pathogenesis of A. fumigatus-related diseases by promoting colonization through cytotoxic activity and by causing inflammatory reactions involving IgE antibodies.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Allergens / analysis*
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Allergens / isolation & purification
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Amino Acid Sequence
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Antibodies / analysis
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Antibodies / immunology
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Antigens, Fungal / analysis*
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Antigens, Plant
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Aspergillus fumigatus / immunology*
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Carrier Proteins / analysis*
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Carrier Proteins / immunology
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Carrier Proteins / metabolism
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Cytotoxins / analysis*
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Fungal Proteins*
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Humans
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Immunoglobulin E / immunology
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Immunoglobulin E / metabolism*
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Lymphokines / analysis*
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Lymphokines / immunology
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Lymphokines / metabolism
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Molecular Sequence Data
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Peptides / analysis
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Prostatic Secretory Proteins*
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Radioimmunoassay
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Ribonucleases*
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Sequence Homology, Nucleic Acid
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Skin / chemistry
Substances
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ASPF1 protein, Aspergillus fumigatus
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Allergens
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Antibodies
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Antigens, Fungal
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Antigens, Plant
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Carrier Proteins
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Cytotoxins
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Fungal Proteins
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Lymphokines
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Peptides
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Prostatic Secretory Proteins
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beta-microseminoprotein
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immunoglobulin-binding factors
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MITF protein, Aspergillus restrictus
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Immunoglobulin E
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Ribonucleases