Please use this identifier to cite or link to this item:
https://doi.org/10.1038/s41598-019-48688-y
DC Field | Value | |
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dc.title | Blo t 2: Group 2 allergen from the dust mite Blomia tropicalis | |
dc.contributor.author | Reginald, K. | |
dc.contributor.author | Pang, S.L. | |
dc.contributor.author | Chew, F.T. | |
dc.date.accessioned | 2021-12-16T07:44:04Z | |
dc.date.available | 2021-12-16T07:44:04Z | |
dc.date.issued | 2019 | |
dc.identifier.citation | Reginald, K., Pang, S.L., Chew, F.T. (2019). Blo t 2: Group 2 allergen from the dust mite Blomia tropicalis. Scientific Reports 9 (1) : 12239. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-019-48688-y | |
dc.identifier.issn | 20452322 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/210687 | |
dc.description.abstract | Blomia tropicalis has been recognized as a cause of allergic diseases in the tropical and subtropical regions. Here we report the immuno-characterization of its group 2 allergen, Blo t 2. Allergen Blo t 2 was amplified from the cDNA of B. tropicalis using degenerate primers, expressed in Escherichia coli as a recombinant protein and purified to homogeneity. The mature protein of Blo t 2 was 126 amino acids long with 52% sequence identity to Der p 2 and apparent molecular mass of 15 kDa. Circular dichroism spectroscopy showed that Blo t 2 is mainly a beta-sheeted protein. We confirmed the presence of three disulfide bonds in recombinant (r) Blo t 2 protein using electrospray mass spectrometry. Thirty-four percent of dust-mite allergic individuals from the Singapore showed specific IgE binding to rBlo t 2 as tested using immuno dot-blots. IgE-cross reactivity assays showed that Blo t 2 had between 20–50% of unique IgE-epitopes compared to Der p 2. IgE binding of native and recombinant forms of Blo t 2 were highly concordant (r2 = 0.77, p < 0.0001) to rBlo t 2. Dose-dependent in vitro histamine was observed when rBlo t 2 was incubated with whole blood of Blo t 2 sensitized individuals, demonstrating that it is a functional allergen. Nine naturally occurring isoforms of Blo t 2 were identified in this study, each having between 1–3 amino acid variations compared to the reference clone. Blo t 2 is a clinically relevant allergen of B. tropicalis as it has unique IgE epitopes compared to major group 2 allergens from Dermatophagoides spp. © 2019, The Author(s). | |
dc.publisher | Nature Publishing Group | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | Scopus OA2019 | |
dc.type | Article | |
dc.contributor.department | BIOLOGICAL SCIENCES | |
dc.contributor.department | DEAN'S OFFICE (SCIENCE) | |
dc.description.doi | 10.1038/s41598-019-48688-y | |
dc.description.sourcetitle | Scientific Reports | |
dc.description.volume | 9 | |
dc.description.issue | 1 | |
dc.description.page | 12239 | |
Appears in Collections: | Elements Staff Publications |
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