Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/69327
DC FieldValueLanguage
dc.contributor.authorLiao, E.C.en_US
dc.contributor.authorHsu, E.L.en_US
dc.contributor.authorTsai, J.J.en_US
dc.contributor.authorHo, C.M.en_US
dc.date2009zh_TW
dc.date.accessioned2014-06-11T05:58:10Z-
dc.date.available2014-06-11T05:58:10Z-
dc.identifier.issn1018-2438zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/69327-
dc.description.abstractBackground: The involvement of the storage mite Tyrophagus putrescentiae in allergies has been increasingly reported in many countries. Molecular analysis has shown that group 3 mite allergens are homologous to trypsin. Similar allergens have not been identified in T. putrescentiae. Our aims were to characterize group 3 allergens in T. putrescentiae and to investigate their significance in allergenicity. Methods: cDNAs of PreTyr p 3 and rTyr p 3 from T. putrescentiae were cloned and expressed in Escherichia coli. Native Tyr p 3 (nTyr p 3) was purified from spent growth medium with an affinity column coupling of antibody. Biological activities of rTyr p 3 were compared with nTyr p 3 in terms of IgE activity, enzymatic activity and histamine release. Results: Full-length cDNA of PreTyr p 3 encodes a 285-amino acid trypsin-like protease and acquires enzymatic activity after removing the pre- and pro-sequences. rTyr p 3 is a 26-kDa protein with equivalent IgE reactivity but weaker enzymatic activity than that of nTyr p 3. A limited level of cross-reactivity has been found between rTyr p 3, Der p 3 and Blomia. Eight of 10 T. putrescentiae-sensitized individuals showed > 50% histamine release after triggering with rTyr p 3. Conclusions: Our studies demonstrate that Tyr p 3 is a frequent allergen (58%) in T. putrescentiae-sensitized patients. Since rTyr p 3 displays equivalent biological activities as nTyr p 3, the role of group 3 allergens can be studied using rTyr p 3 to elucidate the pathogenic effects and diagnostic applications of Tyr p 3. Copyright (C) 2009 S. Karger AG, Baselen_US
dc.language.isoen_USzh_TW
dc.relationInternational Archives of Allergy and Immunologyen_US
dc.relation.ispartofseriesInternational Archives of Allergy and Immunology, Volume 150, Issue 1, Page(s) 15-24.en_US
dc.relation.urihttp://dx.doi.org/10.1159/000210376en_US
dc.subjectBasophil histamine releaseen_US
dc.subjectIgE antibodyen_US
dc.subjectMite group 3 allergensen_US
dc.subjectStorage miteen_US
dc.subjectTrypsin-like serine proteaseen_US
dc.subjectTyr p 3 allergenen_US
dc.subjectTyrophagusen_US
dc.subjectputrescentiaeen_US
dc.subjectprotease-activated receptor-2en_US
dc.subjectgroup-iii allergenen_US
dc.subjectdermatophagoides-pteronyssinusen_US
dc.subjectblomia-tropicalisen_US
dc.subjectfarinaeen_US
dc.subjectcloningen_US
dc.subjectsensitizationen_US
dc.subjectreactivityen_US
dc.subjecturbanen_US
dc.subjectpurificationen_US
dc.titleImmunologic Characterization and Allergenicity of Recombinant Tyr p 3 Allergen from the Storage Mite Tyrophagus putrescentiaeen_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1159/000210376zh_TW
item.grantfulltextnone-
item.openairetypeJournal Article-
item.languageiso639-1en_US-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextno fulltext-
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