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- W2088896628 abstract "<i>Background:</i> The involvement of the storage mite<i> Tyrophagus putrescentiae </i>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 <i>T. putrescentiae</i>. Our aims were to characterize group 3 allergens in<i> T. putrescentiae </i>and to investigate their significance in allergenicity. <i>Methods:</i> cDNAs of PreTyr p 3 and rTyr p 3 from <i>T. putrescentiae</i> were cloned and expressed in <i>Escherichia coli.</i> 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. <i>Results:</i> 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 <i>Blomia</i>. Eight of 10 <i>T. putrescentiae</i>-sensitized individuals showed >50% histamine release after triggering with rTyr p 3. <i>Conclusions:</i> Our studies demonstrate that Tyr p 3 is a frequent allergen (58%) in <i>T. putrescentiae</i>-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." @default.
- W2088896628 created "2016-06-24" @default.
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- W2088896628 date "2009-01-01" @default.
- W2088896628 modified "2023-10-17" @default.
- W2088896628 title "Immunologic Characterization and Allergenicity of Recombinant Tyr p 3 Allergen from the Storage Mite <i>Tyrophagus putrescentiae</i>" @default.
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- W2088896628 doi "https://doi.org/10.1159/000210376" @default.
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