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Immunoglobulin E reactivity of recombinant allergen Tyr p 13 from Tyrophagus putrescentiae homologous to fatty acid binding protein

 Kyoung Yong Jeong  ;  Woo Kyung Kim  ;  Tai-Soon Yong  ;  Han-Il Ree  ;  Chein-Soo Hong  ;  Jung Won Park  ;  Kyu-Earn Kim  ;  In-Yong Lee  ;  Jongweon Lee  ;  Jae Sik Lee 
 Clinical and Diagnostic Laboratory Immunology, Vol.12(5) : 581-585, 2005 
Journal Title
 Clinical and Diagnostic Laboratory Immunology 
Issue Date
Acaridae/immunology* ; Adolescent ; Allergens/chemistry ; Allergens/immunology* ; Allergens/isolation & purification ; Animals ; Base Sequence ; Carrier Proteins ; Child ; Child, Preschool ; Cloning, Molecular ; Fatty Acid-Binding Proteins ; Female ; Humans ; Hypersensitivity/diagnosis ; Immunoglobulin E/immunology* ; Korea ; Male ; Proteins/chemistry* ; Proteins/isolation & purification ; Recombinant Proteins ; Sequence Homology, Nucleic Acid
The storage mite, Tyrophagus putrescentiae, is one of the important causes of allergic disorders. Fifteen allergenic components were demonstrated in storage mite by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting, but only the group 2 allergen Tyr p 2 has been cloned and characterized. In this study, we attempted to identify and characterize new allergens from T. putrescentiae, which is a dominant species of storage mite in Korea. Expressed sequence tags were analyzed to identify possible storage mite allergens, and the cDNA sequence encoding a protein homologous to fatty acid binding protein, a mite group 13 allergen, was identified and named Tyr p 13. Its deduced amino acid sequence showed 61.1 to 85.3% identity with other mite group 13 allergens. The recombinant protein was expressed in Escherichia coli using a pET 28b vector system, and its allergenicity was investigated by enzyme-linked immunosorbent assay (ELISA). The recombinant allergen was detected in 5 of 78 (6.4%) T. putrescentiae-positive sera tested, and it inhibited 61.9% of immunoglobulin E binding to crude extract at an inhibitor concentration of 10 mug/ml by inhibition ELISA using serum from the patient who showed the strongest reaction by ELISA. In this study, a novel allergen was identified in T. putrescentiae. This allergen could be helpful for more-detailed characterizations of storage mite allergy.
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Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Pediatrics (소아청소년과학교실) > 1. Journal Papers
5. Research Institutes (연구소) > Institute of Allergy (알레르기연구소) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Kyu Earn(김규언)
Park, Jung Won(박중원) ORCID logo https://orcid.org/0000-0003-0249-8749
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
Lee, Jae Sik(이재식)
Ree, Han Il(이한일)
Jeong, Kyoung Yong(정경용) ORCID logo https://orcid.org/0000-0001-9887-1426
Hong, Chein Soo(홍천수)
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