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Mol Med Rep. 2015 Oct;12(4):5467-74. doi: 10.3892/mmr.2015.4093. Epub 2015 Jul 20.

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

Author information

1
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.
2
Department of Internal Medicine, Institute of Allergy, Yonsei University College of Medicine, Seoul 120‑752, Republic of Korea.
3
Department of Microbiology, Ajou University School of Medicine, Suwon, Gyeonggi-do 443‑721, Republic of Korea.

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.

PMID:
26238285
DOI:
10.3892/mmr.2015.4093
[Indexed for MEDLINE]

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