ArticlePloS one2017
A combined transcriptome and proteome analysis extends the allergome of house dust mite Dermatophagoides species.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- Expanding grass pollen allergomes: benefits for the molecular profiling of products used forFrontiers in allergy · 2026Article
- Article
- House Dust Mite Extract Forms a Der p 2 Corona on Multi-Walled Carbon Nanotubes: Implications for Allergic Airway Disease.Environmental science. Nano · 2024Article
- Construction by artificial intelligence and immunovalidation of hypoallergenic mite allergen Der f 36 vaccine.Frontiers in immunology · 2024Article
- Predicting Blomia tropicalis allergens using a multiomics approach.Clinical and translational allergy · 2023Article
- Caspase-11 regulates lung inflammation in response to house dust mites.Cellular immunology · 2021Article
- Chromosome-level assembly ofThe World Allergy Organization journal · 2021Article
- Pyroptotic and non-pyroptotic effector functions of caspase-11.Immunological reviews · 2020Review
- Insights Into Mucosal Innate Immune Responses in House Dust Mite-Mediated Allergic Asthma.Frontiers in immunology · 2020Review
- The Role of Dust Mites in Allergy.Clinical reviews in allergy & immunology · 2019Review
- Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus.PloS one · 2019Article
- Characterization of Der f 22 - a paralogue of the major allergen Der f 2.Scientific reports · 2018Article
- Consideration of methods for identifying mite allergens.Clinical and translational allergy · 2018Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHouse dust mites (HDMs) such as Dermatophagoides farinae and D. pteronyssinus represent major causes of perennial allergy. HDM proteomes are currently poorly characterized, with information mostly restricted to allergens. As of today, 33 distinct allergen groups have been identified for these 2 mite species, with groups 1 and 2 established as major allergens. Given the multiplicity of IgE-reactive mite proteins, potential additional allergens have likely been overlooked.
objectiveTo perform a comprehensive characterization of the transcriptomes, proteomes and allergomes of D. farinae and D. pteronyssinus in order to identify novel allergens.
methodsTranscriptomes were analyzed by RNA sequencing and de novo assembly. Comprehensive mass spectrometry-based analyses proteomes were combined with two-dimensional IgE reactivity profiling.
resultsTranscripts from D. farinae and D. pteronyssinus were assembled, translated into protein sequences and used to populate derived sequence databases in order to inform immunoproteomic analyses. A total of 527 and 157 proteins were identified by bottom-up MS analyses in aqueous extracts from purified HDM bodies and fecal pellets, respectively. Based on high sequence similarities (>71% identity), we also identified 2 partial and 11 complete putative sequences of currently undisclosed D. pteronyssinus counterparts of D. farinae registered allergens. Immunoprofiling on 2D-gels revealed the presence of unknown 23 kDa IgE reactive proteins in both species. Following expression of non-glycosylated recombinant forms of these molecules, we confirm that these new allergens react with serum IgEs from 42% (8/19) of HDM-allergic individuals.
conclusionsUsing combined transcriptome and immunoproteome approaches, we provide a comprehensive characterization of D. farinae and D. pteronyssinus allergomes. We expanded the known allergen repertoire for D. pteronyssinus and identified two novel HDM allergens, now officially referred by the International Union of Immunological Societies (IUIS) Nomenclature Subcommittee as Der f 36 and Der p 36.
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