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Clinical and Diagnostic Laboratory Immunology, May 2005, p. 581-585, Vol. 12, No. 5
1071-412X/05/$08.00+0     doi:10.1128/CDLI.12.5.581-585.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Immunoglobulin E Reactivity of Recombinant Allergen Tyr p 13 from Tyrophagus putrescentiae Homologous to Fatty Acid Binding Protein

Kyoung Yong Jeong,^1, Woo Kyung Kim,^2, Jae Sik Lee,¹ Jongweon Lee,¹ In-Yong Lee,¹ Kyu-Earn Kim,³ Jung Won Park,⁴ Chein-Soo Hong,⁴ Han-Il Ree,¹ and Tai-Soon Yong^1*

Department of Parasitology and Institute of Tropical Medicine, Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea,¹ Department of Pediatrics and Inje University Seoul Paik Hospital, Seoul, Korea,² Department of Pediatrics and Institute of Allergy, Yonsei University College of Medicine, Seoul, Korea,³ Department of Internal Medicine and Institute of Allergy, Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea⁴

Received 7 December 2004/ Returned for modification 18 January 2005/ Accepted 10 March 2005

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 µg/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.

K.Y.J. and W.K.K. contributed equally to this study.

This article has been cited by other articles:

• Jeong, K. Y., Lee, H., Lee, J. S., Lee, J., Lee, I.-Y., Ree, H.-I., Hong, C.-S., Park, J. W., Yong, T.-S. (2005). Immunoglobulin E Binding Reactivity of a Recombinant Allergen Homologous to {alpha}-Tubulin from Tyrophagus putrescentiae. CVI 12: 1451-1454 [Abstract] [Full Text]