Molecular Cloning and the Allergenic Characterization of Tropomyosin from Tyrophagus putrescentiae

Author(s): Kyoung Yong Jeong, Haeseok Lee, Jae Sik Lee, Jongweon Lee, In-Yong Lee, Han-Il Ree, Chein-Soo Hong, Tai-Soon Yong.

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 5 , 2007

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Abstract:

Storage mites have been recognized as a cause of asthma and rhinitis. Studies from several countries have shown that the IgE-mediated allergy to storage mites is of considerable importance, especially in rural populations. This study aimed to identify and characterize new allergens from Tyrophagus putrescentiae. A partial cDNA sequence encoding tropomyosin was isolated from the cDNA library by immunoscreening using anti-mouse IgG1 sera raised against T. putrescentiae whole body extract. The deduced amino acid sequence shares 64-94% identity with previously known allergenic tropomyosins. Its recombinant protein was produced by using a pET 28b expression system and purified by affinity chromatography using Ni-NTA agarose. The IgE reactivities of tropomyosins from T. putrescentiae and Dermatophagoides farinae were compared by enzyme linked immunosorbent assay (ELISA). Recombinant Tyr p 10 showed 12.5% (5/40) IgE-binding reactivity, whereas recombinant Der f 10 showed 25% (10/40) IgE-binding reactivity against the same sera from storage mite-sensitized and house dust mite-sensitized subjects. Both recombinant Tyr p 10 and Der f 10 showed little inhibition of IgE binding to T. putrescentiae crude extract by ELISA. Tropomyosin seems to contribute only a small portion of the cross-reactivity with house dust mites.

Keywords: allergen, cross-reactivity, tropomyosin, tyrophagus putrescentiae

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Article Details

VOLUME: 14
ISSUE: 5
Year: 2007
Page: [431 - 436]
Pages: 6
DOI: 10.2174/092986607780782777
Price: $58

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