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

Authors
 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 
Citation
 Clinical and Diagnostic Laboratory Immunology, Vol.12(5) : 581-585, 2005 
Journal Title
 Clinical and Diagnostic Laboratory Immunology 
ISSN
 1071-412X 
Issue Date
2005
MeSH
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
Keywords
15879018
Abstract
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.
Files in This Item:
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DOI
10.1128/CDLI.12.5.581-585.2005
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)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/114925
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