Identification of IgE binding components of Tetranychus urticae (TU): species-specific and cross-reacting allergens with house dust mite (HDM).
- Author:
Soo Keol LEE
1
;
Young Koo JEE
;
Yoon Keun KIM
;
Jung Hee SUH
;
Myung Hyun LEE
;
Hae Sim PARK
Author Information
1. Department of Allergy and Clinical Immunology, Ajou University, School of Medicine, Korea.
- Publication Type:Original Article
- Keywords:
Tetranychus urticae;
house dust mite;
allergenic cross-reactivity
- MeSH:
Allergens*;
Dust*;
Electrophoresis, Polyacrylamide Gel;
Enzyme-Linked Immunosorbent Assay;
Flowers;
Fruit;
Humans;
Hypersensitivity;
Immunoglobulin E*;
Korea;
Pyroglyphidae*;
Skin;
Trees
- From:Journal of Asthma, Allergy and Clinical Immunology
2000;20(6):879-886
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
BACKGROUND: The Tetranychus urticae (TU) is commonly found on fruit trees and green house flowers. A recent investigation demonstrated that the sensitization rate to TU was as high as that of HDM in respiratory allergy patients in middle part of South Korea. MATERIAL AND METHODS: To identify IgE binding components within TU, sera from 8 TU-sen-sitive asthmatic patients and sera from unexposed controls showing negative response to TU on skin prick test were enrolled. SDS-PAGE and immunoblot analysis were applied. To evaluate cross-allergenicity with house dust mite (HDM) two kinds of serum pool were used: one (A) showing isolated positive response to TU and the other (B) showing positive responses to both TU and HDM. ELISA inhibition tests using sera A and B were were used. RESULTS: TU-ELISA inhibition test using serum pool A showed significant inhibition with TU and CRM and minimal inhibition with HDM, while ELISA inhibition test using serum pool B showed significant inhibition with addition of TU and CRM and partial inhibition with HDM. Immunoblot analysis using individual sera showed six IgE binding components (75, 56, 41, 37, 28, 14 kDa) and three (75, 41, 14 kDa) were bound to IgE in more than 50% of sera tested. CONCLUSIONS: Six IgE binding components were identified within TU and three (75, 41, 14 kDa) could be considered major allergens. Extensive cross-allergenicity was noted between TU and CRM TU-derived extracts contain TU-specific addition to common sharing allergens witHDM, Further investigations will be needed to identify species-specific, or common allergenic components within TU.
