{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T09:35:27Z","timestamp":1789896927846,"version":"4.0.1"},"reference-count":27,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,5,12]],"date-time":"2006-05-12T00:00:00Z","timestamp":1147392000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Clin Experimental Allergy"],"published-print":{"date-parts":[[2006,6]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p><jats:bold>Background\n\t\t\t\t\t<\/jats:bold> House dust mites <jats:italic>Dermatophagoides pteronyssinus<\/jats:italic> and <jats:italic>Dermatophagoides farinae<\/jats:italic> cause allergic disease in humans as well as in dogs. In geographical regions where the two mite species coexist, they both elicit specific immunoglobulin (Ig E) responses in humans whereas dogs preferentially react to <jats:italic>D. farinae<\/jats:italic> extracts. In dogs the main IgE binding is directed to the <jats:italic>D. farinae<\/jats:italic> chitinase allergens Der f 15 and Der f 18 and not to the groups 1 and 2 allergens as found for humans. Although the IgE response of humans to Der f 18 has been investigated there is no report on Der f 15\u2010specific IgE in humans.<\/jats:p><jats:p><jats:bold>Objective\n\t\t\t\t\t<\/jats:bold> This study aimed to characterize the chitinase allergens Der p 15 and Der p 18 of <jats:italic>D. pteronyssinus<\/jats:italic> and to find out whether they are important allergens for humans.<\/jats:p><jats:p><jats:bold>Methods\n\t\t\t\t\t<\/jats:bold> cDNA was cloned by a polymerase chain reaction strategy from <jats:italic>D. pteronyssinus<\/jats:italic> libraries using primers based on conserved chitinase sequences. IgE binding to the recombinant polypeptides was measured by immunosorbent assay. Mice were immunized with the polypeptides and cross\u2010reactivity examined.<\/jats:p><jats:p><jats:bold>Results\n\t\t\t\t\t<\/jats:bold> Two variants of Der p 15 were isolated, encoding mature proteins of 58.8 and 61.4\u2003kDa. The amino acid sequences had 90% identity to Der f 15. The cDNA for Der p 18 encoded a mature protein of 49.2\u2003kDa with 88% sequence identity to Der f 18. Der p 15\u2010specific IgE was detected in 70% and Der p 18\u2010specific IgE in 63% of a panel of 27 human allergic sera.<\/jats:p><jats:p><jats:bold>Conclusions\n\t\t\t\t\t<\/jats:bold> The <jats:italic>D. pteronyssinus<\/jats:italic> chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs.<\/jats:p>","DOI":"10.1111\/j.1365-2222.2006.02497.x","type":"journal-article","created":{"date-parts":[[2006,5,12]],"date-time":"2006-05-12T14:49:56Z","timestamp":1147445396000},"page":"831-839","source":"Crossref","is-referenced-by-count":46,"title":["The chitinase allergens Der p 15 and Der p 18 from <i>Dermatophagoides pteronyssinus<\/i>"],"prefix":"10.1111","volume":"36","author":[{"given":"S. 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