Multi-omic analysis of Tyrophagus putrescentiae reveals insights into the allergen complexity of storage mites
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AbstractTyrophagus putrescentiae, commonly referred to as the mould mite or cheese mite, is especially well-known as a storage mite that causes human allergic diseases.1 However, it has fewer reported allergen groups compared to the house dust mites of the Dermatophagoides genus in the WHO/IUIS allergen nomenclature database.2, 3
In this omics era, multiple genome-based approaches have been boosting our understanding of the medically important mites.4-6 Using the mite allergens reported in the WHO/IUIS database as reference genes, 37 allergen groups (up to group 42) were predicted in the genome of T. putrescentiae6 and composed an allergen profile encompassing up to 85 predicted genes (Table S1). Unlike the allergen gene expression of D. farinae and D. pteronyssinus,5 the group 1 allergens (cysteine proteases) of T. putrescentiae were expressed at low levels, while the homologue of group 13 allergen, pTyr p 13.0201, exhibited the highest expression level (Figure 1A). To evaluate the IgE-binding reactivity of novel allergens, recombinant proteins were cloned, expressed and assessed by ELISA with T. putrescentiae-sensitized patient sera (Table S2). Five proteins, rTyr p 6.0101, 9.0101, 18.0101, 20.0101 and 26.0101, were suggested to be novel allergens by ELISA experiments with 11.1%, 22.2%, 11.1%, 44.4% and 50.0% positive rates, but with low IgE levels. Additional information about study methods and findings is available in the following repository
In this omics era, multiple genome-based approaches have been boosting our understanding of the medically important mites.4-6 Using the mite allergens reported in the WHO/IUIS database as reference genes, 37 allergen groups (up to group 42) were predicted in the genome of T. putrescentiae6 and composed an allergen profile encompassing up to 85 predicted genes (Table S1). Unlike the allergen gene expression of D. farinae and D. pteronyssinus,5 the group 1 allergens (cysteine proteases) of T. putrescentiae were expressed at low levels, while the homologue of group 13 allergen, pTyr p 13.0201, exhibited the highest expression level (Figure 1A). To evaluate the IgE-binding reactivity of novel allergens, recombinant proteins were cloned, expressed and assessed by ELISA with T. putrescentiae-sensitized patient sera (Table S2). Five proteins, rTyr p 6.0101, 9.0101, 18.0101, 20.0101 and 26.0101, were suggested to be novel allergens by ELISA experiments with 11.1%, 22.2%, 11.1%, 44.4% and 50.0% positive rates, but with low IgE levels. Additional information about study methods and findings is available in the following repository
All Author(s) ListWan A.T.Y., Xiong Q., Xiao X., Ao K.F.K., Jang S.W., Wong B.S.H., Wang M., Cao Q., Fung C.S.H., Chew F.T., Sun B., Ngai S.M., Leung T.F., Jeong K.Y., Liu X., Tsui S.K.W.
Journal nameClinical and Experimental Allergy
Year2024
Month1
Volume Number54
Issue Number1
PublisherJohn Wiley and Sons Inc
Place of PublicationUnited Kingdom
Pages77 - 81
ISSN0954-7894
eISSN1365-2222
LanguagesEnglish-United Kingdom
Keywordshuman allergic diseases, storage mites, allergens
