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

DC Field Value Language
dc.contributor.authorKim, CR-
dc.contributor.authorJeong, KY-
dc.contributor.authorYi, MH-
dc.contributor.authorKim, HP-
dc.contributor.authorShin, HJ-
dc.contributor.authorYong, TS-
dc.date.accessioned2017-02-06T04:42:34Z-
dc.date.available2017-02-06T04:42:34Z-
dc.date.issued2015-
dc.identifier.issn1791-2997-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/13482-
dc.description.abstractGroup-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.-
dc.language.isoen-
dc.subject.MESHAdolescent-
dc.subject.MESHAdult-
dc.subject.MESHAllergens-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHAnimals-
dc.subject.MESHAntibody Specificity-
dc.subject.MESHAntigens, Dermatophagoides-
dc.subject.MESHAsthma-
dc.subject.MESHChild-
dc.subject.MESHCross Reactions-
dc.subject.MESHDermatophagoides farinae-
dc.subject.MESHFemale-
dc.subject.MESHHumans-
dc.subject.MESHHypersensitivity-
dc.subject.MESHImmunoglobulin E-
dc.subject.MESHMale-
dc.subject.MESHMiddle Aged-
dc.subject.MESHMolecular Sequence Data-
dc.subject.MESHPyroglyphidae-
dc.subject.MESHRecombinant Proteins-
dc.subject.MESHSequence Alignment-
dc.subject.MESHYoung Adult-
dc.titleCross‑reactivity between group-5 and -21 mite allergens from Dermatophagoides farinae, Tyrophagus putrescentiae and Blomia tropicalis.-
dc.typeArticle-
dc.identifier.pmid26238285-
dc.identifier.urlhttp://www.spandidos-publications.com/mmr/12/4/5467-
dc.contributor.affiliatedAuthor신, 호준-
dc.type.localJournal Papers-
dc.identifier.doi10.3892/mmr.2015.4093-
dc.citation.titleMolecular medicine reports-
dc.citation.volume12-
dc.citation.number4-
dc.citation.date2015-
dc.citation.startPage5467-
dc.citation.endPage5474-
dc.identifier.bibliographicCitationMolecular medicine reports, 12(4). : 5467-5474, 2015-
dc.identifier.eissn1791-3004-
dc.relation.journalidJ017912997-
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Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
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