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Immunoglobulin E binding reactivity of a recombinant allergen homologous to alpha-Tubulin from Tyrophagus putrescentiae.


ABSTRACT: Storage mites may cause allergic respiratory diseases in urban areas as well as pose an occupational hazard in rural areas. Characterization of storage mite allergens is important for the development of diagnostic and therapeutic agents against mite-associated allergic disorders. Here we report on the cloning and expression of alpha-tubulin from the storage mite (Tyrophagus putrescentiae). The deduced amino acid sequence of the alpha-tubulin from the storage mite showed as much as 97.3% identity to the alpha-tubulin sequences from other organisms. The highly conserved amino acid sequences of alpha-tubulins across different species of mites may indicate that cross-reactivity for this potential allergen exists. The frequency of immunoglobulin E reactivity of this recombinant protein is 29.3% in sera from storage mite-allergic subjects.

SUBMITTER: Jeong KY 

PROVIDER: S-EPMC1317066 | biostudies-literature | 2005 Dec

REPOSITORIES: biostudies-literature

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Immunoglobulin E binding reactivity of a recombinant allergen homologous to alpha-Tubulin from Tyrophagus putrescentiae.

Jeong Kyoung Yong KY   Lee Haeseok H   Lee Jae Sik JS   Lee Jongweon J   Lee In-Yong IY   Ree Han-Il HI   Hong Chein-Soo CS   Park Jung Won JW   Yong Tai-Soon TS  

Clinical and diagnostic laboratory immunology 20051201 12


Storage mites may cause allergic respiratory diseases in urban areas as well as pose an occupational hazard in rural areas. Characterization of storage mite allergens is important for the development of diagnostic and therapeutic agents against mite-associated allergic disorders. Here we report on the cloning and expression of alpha-tubulin from the storage mite (Tyrophagus putrescentiae). The deduced amino acid sequence of the alpha-tubulin from the storage mite showed as much as 97.3% identity  ...[more]

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