Clinical & Experimental Allergy

Glucoamylase is a major allergen of Schizophyllum commune

Authors

  • T. Toyotome,

    Corresponding author
    1. Division of Clinical Research, Medical Mycology Research Center, Chiba University, Chiba, Japan
    2. Research Center for Animal Hygiene and Food Safety, Obihiro University of Agriculture and Veterinary Medicine, Hokkaido, Japan
    • Correspondence:

      Takahito Toyotome, Research Center for Animal Hygiene and Food Safety, Obihiro University of Agriculture and Veterinary Medicine, Nishi 2-11, Inadacho, Obihiro, Hokkaido, Japan.

      E-mail: tome@obihiro.ac.jp

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  • M. Satoh,

    1. Clinical Proteomics Research Center, Chiba University Hospital, Chiba, Japan
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  • M. Yahiro,

    1. Division of Clinical Research, Medical Mycology Research Center, Chiba University, Chiba, Japan
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  • A. Watanabe,

    1. Division of Clinical Research, Medical Mycology Research Center, Chiba University, Chiba, Japan
    2. Division of Control and Treatment of Infectious Diseases, Chiba University Hospital, Chiba, Japan
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  • F. Nomura,

    1. Clinical Proteomics Research Center, Chiba University Hospital, Chiba, Japan
    2. Department of Molecular Diagnosis, Graduate School of Medicine, Chiba University, Chiba, Japan
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  • K. Kamei

    1. Division of Clinical Research, Medical Mycology Research Center, Chiba University, Chiba, Japan
    2. Division of Control and Treatment of Infectious Diseases, Chiba University Hospital, Chiba, Japan
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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 < 0.01).

Conclusions and Clinical Relevance

Sch c 1 is recognized by the host immune system of patients as an antigen/allergen. The purified glucoamylase Sch c 1 is a promising candidate antigen for the serodiagnosis of S. commune-induced mycosis.

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