17 25

Cited 0 times in

Identification of Tyrophagus putrescentiae allergens and evaluation of cross-reactivity with Dermatophagoides pteronyssinus

Authors
 S Munhbayarlah  ;  Jung Won Park  ;  Si Hwon Ko  ;  Han Il Ree  ;  Chein Soo Hong 
Citation
 YONSEI MEDICAL JOURNAL, Vol.39(2) : 109-116, 1998 
Journal Title
 YONSEI MEDICAL JOURNAL 
ISSN
 0513-5796 
Issue Date
1998
MeSH
Allergens/analysis* ; Allergens/immunology* ; Animals ; Cross Reactions/immunology ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Humans ; Immunoblotting ; Immunoglobulin E/analysis ; Immunoglobulin E/immunology ; Mites/classification ; Mites/immunology*
Abstract
House dust mites are the most common cause of allergic sensitization in respiratory allergic patients in the world. Tyrophagus putrescentiae (TP), which was followed by Dermatophagoides farinae (DF) and Dermatophagoides pteronyssinus (DP), has been reported as the third most common house mite in Korea. We previously reported that many respiratory allergic patients had become concomitantly sensitized to DP, DF and TP. The aims of this study were to identify the allergic components of TP and to evaluate the cross-reactivity between TP and DP. The allergenic components of TP and DP extracts were determined with SDS-PAGE and IgE immunoblotting analysis. The cross-reactivity as evaluated by ELISA inhibition and inhibitory immunoblotting experiments. According the SDS-PAGE, the protein components of the two extracts were somewhat different, although a few components displayed identical molecular weights. The 18 kD protein of TP was the most prevalent allergen in the sera of patients sensitized to TP and DP. Both of the maximum inhibition percentages of optic densities of TP-specific IgE in ELISA with TP and DP extract were 100%, respectively and the 50% inhibitory dose (ID50) of TP extract and DP extract were 0.01 µg/ml and 0.02 µg/ml, respectively. Maximum inhibition of optic densities of DP-specific IgE in ELISA with TP and DP extracts were 29% and 100%, respectively and the ID50 of DP extract was 0.007 µg/ml. On inhibitory immunoblotting of DP specific IgE, 5 µg/ml of TP extract completely inhibited 16 kD without inhibiting the other allergic component. Whereas, on inhibitory immunoblotting of TP-specific IgE, 5 µg/ml of DP extract completely inhibited all the IgE binding components of TP. These results suggested that the major allergen of TP may be the 18 kD component and we also concluded that TP allergens have a strong cross-reactivity with DP extracts, but that DP allergens only have partial cross-reactivity with TP extracts.
Files in This Item:
T199801781.pdf Download
DOI
10.3349/ymj.1998.39.2.109
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Park, Jung Won(박중원) ORCID logo https://orcid.org/0000-0003-0249-8749
Ree, Han Il(이한일)
Hong, Chein Soo(홍천수)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/176902
사서에게 알리기
  feedback

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse

Links