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

Kim,Chung‑Ryul; Jeong,Kyoung Yong; Yi,Myung‑Hee; Kim,Hyoung‑Pyo; Shin,Ho‑Joon; Yong,Tai‑Soon

doi:10.3892/mmr.2015.4093

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
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Affiliations: Department of Environmental Medical Biology and Arthropods of Medical Importance Resource Bank, Institute of Tropical Medicine, Yonsei University College of Medicine, Seoul 120‑752, Republic of Korea, Department of Internal Medicine, Institute of Allergy, Yonsei University College of Medicine, Seoul 120‑752, Republic of Korea, Department of Microbiology, Ajou University School of Medicine, Suwon, Gyeonggi-do 443‑721, Republic of Korea
Published online on: July 20, 2015 https://doi.org/10.3892/mmr.2015.4093
Pages: 5467-5474

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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.

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