Glucoamylase is a major allergen of Schizophyllum commune

Summary Background Schizophyllum commune is one of the causative agents of basidiomycosis including disorders such as allergic bronchopulmonary mycosis, allergic fungal sinusitis, and mucoid impaction of bronchi, the incidence of those of which has been increasing. These mycoses are difficult to dia...

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Bibliographic Details
Published in:Clinical and experimental allergy 2014-03, Vol.44 (3), p.450-457
Main Authors: Toyotome, T., Satoh, M., Yahiro, M., Watanabe, A., Nomura, F., Kamei, K.
Format: Article
Language:English
Subjects:
Allergens - chemistry
Allergens - immunology
allergic bronchopulmonary mycosis
Amino Acid Sequence
Antibodies, Fungal - blood
Antibodies, Fungal - immunology
Antigens, Fungal - chemistry
Antigens, Fungal - immunology
basidiomycosis
Cross Reactions - immunology
Glucan 1,4-alpha-Glucosidase - chemistry
Glucan 1,4-alpha-Glucosidase - immunology
glucoamylase
Humans
Immunoglobulin E - blood
Immunoglobulin E - immunology
Immunoglobulin G - blood
Immunoglobulin G - immunology
Molecular Sequence Data
Mycoses - blood
Mycoses - immunology
Pulmonary Aspergillosis - immunology
Sch c 1
Schizophyllum - enzymology
Schizophyllum - immunology
Schizophyllum commune
Sequence Alignment
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Summary:Summary Background Schizophyllum commune is one of the causative agents of basidiomycosis including disorders such as allergic bronchopulmonary mycosis, allergic fungal sinusitis, and mucoid impaction of bronchi, the incidence of those of which has been increasing. These mycoses are difficult to diagnose because only a limited number of diagnostic tools are currently available. The biggest problem is that no specific antigens of S. commune have been identified to enable serodiagnosis of the disease. Objective In this study, we attempted to identify a major antigen of S. commune to establish a reliable serodiagnostic method. Methods We used mass spectrometry to identify an antigen that reacted with the serum of a patient with allergic bronchopulmonary mycosis caused by S. commune. The protein was expressed in Escherichia coli, highly purified, and the patient sera IgG and IgE titres against the protein were determined by enzyme‐linked immunosorbent assay. Results The protein identified as a major antigen of S. commune was named Sch c 1; it was a homolog of glucoamylase. The IgG and IgE titres against Sch c 1 in patient sera were significantly higher than those in healthy volunteer sera (P 
ISSN:0954-7894
1365-2222
DOI:10.1111/cea.12260