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Cross‑reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis

Authors
 CHUNG‑RYUL KIM  ;  KYOUNG YONG JEONG  ;  MYUNG‑HEE YI  ;  HYOUNG‑PYO KIM  ;  HO‑JOON SHIN  ;  TAI‑SOON YONG 
Citation
 MOLECULAR MEDICINE REPORTS, Vol.12(4) : 5467-5474, 2015 
Journal Title
 MOLECULAR MEDICINE REPORTS 
ISSN
 1791-2997 
Issue Date
2015
MeSH
Adolescent ; Adult ; Allergens/chemistry ; Allergens/genetics ; Allergens/immunology* ; Amino Acid Sequence ; Animals ; Antibody Specificity/immunology ; Antigens, Dermatophagoides/chemistry ; Antigens, Dermatophagoides/genetics ; Antigens, Dermatophagoides/immunology* ; Asthma/blood ; Asthma/immunology ; Child ; Cross Reactions/immunology* ; Dermatophagoides farinae/genetics ; Dermatophagoides farinae/immunology* ; Female ; Humans ; Hypersensitivity/blood ; Hypersensitivity/immunology ; Immunoglobulin E/blood ; Immunoglobulin E/immunology ; Male ; Middle Aged ; Molecular Sequence Data ; Pyroglyphidae/genetics ; Pyroglyphidae/immunology* ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Sequence Alignment ; Young Adult
Abstract
Group-5 and group-21 allergens, produced by house dust mites and storage mites are 36.6-55.8% identical in their sequences and are recognized by at least 50% of immunoglobulin (Ig)E from the sera of individuals allergic to dust mites. In the present study, recombinant group-5 and ‑21 allergens from three mite species, Dermatophagoides farinae (rDer f 5 and 21), Tyrophagus putrescentiae (rTyr p 5 and 21), and Blomia tropicalis (rBlo t 5 and 21), were purified from Escherichia coli, and the IgE reactivities and cross‑reactivities of these allergen variants were assessed. The IgE binding frequencies of rDer f 5, rDer f 21, rTyr p 5, rTyr p 21, rBlo t and rBlo t 21 proteins were 64.95, 65.98, 30.41, 41.24, 30.93 and 21.65%, respectively. The IgE reactivity of rDer f 5 correlated highly with that of rDer f 21 (r=0.733). rTyr p 5 exhibited the highest level of correlation with rTyr p 21 (r=0.950), while the correlation of rBlo t 5 with rBlo t 21 was the lowest observed (r=0.104). The binding of IgE to rDer f 5 and rDer f 21 was not inhibited by any allergens but themselves. While rDer f 5 inhibited only 60.3% of IgE binding to rBlo t 5, rDer f 21 exhibited a high inhibitory effect against rTyr p 5 (93.01%), rTyr p 21 (92.12%), rBlo t 5 (86.97%) and rBlo t 21 (70.30%), implying cross‑reactivity among mite species. The results of the present study demonstrated that the majority of the IgE reactivity to group-5 and -21 storage mite allergens is due to cross‑reaction. It is therefore imperative to develop an accurate, component‑resolved diagnosis for dust mite allergies.
Full Text
https://www.spandidos-publications.com/mmr/12/4/5467
DOI
10.3892/mmr.2015.4093
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Thoracic and Cardiovascular Surgery (흉부외과학교실) > 1. Journal Papers
Yonsei Authors
Kim, Hyoung Pyo(김형표) ORCID logo https://orcid.org/0000-0003-1441-8822
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
Yi, Myung Hee(이명희) ORCID logo https://orcid.org/0000-0001-9537-5726
Jeong, Kyoung Yong(정경용) ORCID logo https://orcid.org/0000-0001-9887-1426
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/157199
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