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

Kyoung Yong Jeong, Woo Kyung Kim, Jae Sik Lee, Jongweon Lee, In Yong Lee, Kyu Earn Kim, Jung Won Park, Chein Soo Hong, Han Il Ree, Tai Soon Yong

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)581-585
Number of pages5
JournalClinical and Diagnostic Laboratory Immunology
Volume12
Issue number5
DOIs
Publication statusPublished - 2005 May 1

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Fatty Acid-Binding Proteins
Acaridae
Allergens
Immunoglobulin E
Immunosorbents
Assays
Mites
Enzyme-Linked Immunosorbent Assay
Allergies
Enzyme inhibition
Tyrophagus putrescentiae Tyr p 2 protein
Expressed Sequence Tags
Enzymes
Korea
Electrophoresis
Complex Mixtures
Serum
Recombinant Proteins
Immunoblotting
Sodium Dodecyl Sulfate

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology
  • Clinical Biochemistry
  • Microbiology (medical)

Cite this

Jeong, Kyoung Yong ; Kim, Woo Kyung ; Lee, Jae Sik ; Lee, Jongweon ; Lee, In Yong ; Kim, Kyu Earn ; Park, Jung Won ; Hong, Chein Soo ; Ree, Han Il ; Yong, Tai Soon. / Immunoglobulin E reactivity of recombinant allergen Tyr p 13 from Tyrophagus putrescentiae homologous to fatty acid binding protein. In: Clinical and Diagnostic Laboratory Immunology. 2005 ; Vol. 12, No. 5. pp. 581-585.
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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 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.",
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Immunoglobulin E reactivity of recombinant allergen Tyr p 13 from Tyrophagus putrescentiae homologous to fatty acid binding protein. / Jeong, Kyoung Yong; Kim, Woo Kyung; Lee, Jae Sik; Lee, Jongweon; Lee, In Yong; Kim, Kyu Earn; Park, Jung Won; Hong, Chein Soo; Ree, Han Il; Yong, Tai Soon.

In: Clinical and Diagnostic Laboratory Immunology, Vol. 12, No. 5, 01.05.2005, p. 581-585.

Research output: Contribution to journalArticle

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AU - Jeong, Kyoung Yong

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