Vacuolar Serine Protease Is a Major Allergen of Fusarium proliferatum and an IgE-Cross Reactive Pan-Fungal Allergen.
10.4168/aair.2016.8.5.438
- Author:
Chang Ching YEH
1
;
Hsiao Yun TAI
;
Hong CHOU
;
Keh Gong WU
;
Horng Der SHEN
Author Information
1. Department of Obstetrics and Gynecology, Taipei Veterans General Hospital and Institute of Clinical Medicine, National Yang-Ming University, Taipei, Taiwan, R.O.C.
- Publication Type:Original Article
- Keywords:
F. proliferatum;
allergen;
vacuolar serine protease;
IgE cross-reactivity
- MeSH:
Allergens;
Animals;
Antibodies;
Clone Cells;
Diagnosis;
DNA, Complementary;
Fungi;
Fusarium*;
Humans;
Hypersensitivity;
Immunoglobulin E;
Mice;
Penicillium chrysogenum;
Serine Proteases*;
Serine*
- From:Allergy, Asthma & Immunology Research
2016;8(5):438-444
- CountryRepublic of Korea
- Language:English
-
Abstract:
PURPOSE: Fusarium species are among prevalent airborne fungi and causative agents of human respiratory atopic disorders. We previously identified a 36.5-kDa F. proliferatum component recognized by IgE antibodies in 9 (53%) of the 17 F. proliferatum-sensitized atopic serum samples. The purpose of this study is to characterize the 36.5-kDa allergen of F. proliferatum. METHODS: Characterization of allergens and determination of IgE cross-reactivity were performed by cDNA cloning/expression and immunoblot inhibition studies. RESULTS: Based on the finding that the 36.5-kDa IgE-binding component reacted with the mouse monoclonal antibody FUM20 against fungal vacuolar serine protease allergens, the cDNA of F. proliferatum vacuolar serine protease (Fus p 9.0101) was subsequently cloned. Nine serum samples from respiratory atopic patients with IgE binding to the vacuolar serine protease allergen of Penicillium chrysogenum (Pen ch 18) also showed IgE-immunoblot reactivity to rFus p 9.0101. The purified rFus p 9.0101 can inhibit IgE and FUM20 binding to the 36.5-kDa component of F. proliferatum. Thus, a novel and important Fus p 9.0101 was identified. The rPen ch 18 can inhibit IgE binding to Fus p 9.0101. It indicates that IgE cross-reactivity between Fus p 9.0101 and Pen ch 18 also exists. Furthermore, neither rFus p 9.0101 K88A nor rPen ch 18 K89A mutants inhibited IgE binding to rFus p 9.0101. Lys88 was considered a critical core amino acid in IgE binding to r Fus p 9.0101 and a residue responsible for IgE cross-reactivity between Fus p 9.0101 and Pen ch 18 allergens. CONCLUSIONS: Results obtained from this study indicate that vacuolar serine protease may be a major allergen of F. proliferatum and an important IgE cross-reactive pan-fungal allergen, and provide important bases for clinical diagnosis of fungal allergy.
