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Dermatophagoides pteronyssinus

ABSTRACT: Identification and Characterization of HDM D.p. immunogenic RNA

PROVIDER: PRJNA397017 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5892547_1.fastq.gz	Fastqsanger.gz
	SRR5892547_2.fastq.gz	Fastqsanger.gz
	SRR5892548_1.fastq.gz	Fastqsanger.gz
	SRR5892548_2.fastq.gz	Fastqsanger.gz
	SRR5892549_1.fastq.gz	Fastqsanger.gz

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Proteases of Dermatophagoides pteronyssinus.

Project description:Since the discovery that Der p 1 is a cysteine protease, the role of proteolytic activity in allergic sensitization has been explored. There are many allergens with proteolytic activity; however, exposure from dust mites is not limited to allergens. In this paper, genomic, transcriptomic and proteomic data on Dermatophagoides pteronyssinus (DP) was mined for information regarding the complete degradome of this house dust mite. D. pteronyssinus has more proteases than the closely related Acari, Dermatophagoides farinae (DF) and Sarcoptes scabiei (SS). The group of proteases in D. pteronyssinus is found to be more highly transcribed than the norm for this species. The distribution of protease types is dominated by the cysteine proteases like Der p 1 that account for about half of protease transcription by abundance, and Der p 1 in particular accounts for 22% of the total protease transcripts. In an analysis of protease stability, the group of allergens (Der p 1, Der p 3, Der p 6, and Der p 9) is found to be more stable than the mean. It is also statistically demonstrated that the protease allergens are simultaneously more highly expressed and more stable than the group of D. pteronyssinus proteases being examined, consistent with common assumptions about allergens in general. There are several significant non-allergen outliers from the normal group of proteases with high expression and high stability that should be examined for IgE binding. This paper compiles the first holistic picture of the D. pteronyssinus degradome to which humans may be exposed.

| S-EPMC5486027 | biostudies-literature

Dermatophagoides pteronyssinus

Project description:Dermatophagoides pteronyssinus overview

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Dermatophagoides pteronyssinus

Project description:Dermatophagoides pteronyssinus Genome sequencing and assembly

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Dermatophagoides pteronyssinus

Project description:Dermatophagoides pteronyssinus Genome sequencing and assembly

| PRJNA388362 | ENA

Dermatophagoides pteronyssinus

Project description:Dermatophagoides pteronyssinus Transcriptome or Gene expression

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Dermatophagoides pteronyssinus

Project description:Dermatophagoides pteronyssinus Genome sequencing and assembly

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Dermatophagoides pteronyssinus immunotherapy changes the T-regulatory cell activity.

Project description:Subcutaneous specific immunotherapy (SCIT) has been shown to modify the Dermatophagoides pteronissinus (DP) allergic response, characterized by generation of Treg cells. However, studies have reported no changes in the proportion of Treg cells after immunotherapy, indicating that the effects may be due to modifications in their regulatory activities. We aimed to determine whether Tregs generated by DP-SCIT can switch the allergic response to tolerant and study the involvement of suppressive cytokines on it. Twenty-four DP-allergic rhinitis patients were recruited, 16 treated with DP-SCIT and 8 untreated. Treg and T effector cells were isolated before and after DP-SCIT, and cocultured in different combinations with ?-IL-10, ?-TGF-? blocking antibodies and nDer p 1. Treg cells after DP-SCIT increased Th1 and decreased Th2 and Th9 proliferation. Similarly, they increased IL-10 and decreased IL-4 and IL-9-producing cells. ?-IL-10 affected the activity of Treg cells obtained after DP-SCIT only. Finally, DP-specific IgG4 levels, Treg percentage and IL-10 production were correlated after DP-SCIT. These results demonstrate that DP-SCIT induces Treg cells with different suppressive activities. These changes could be mediated by IL-10 production and appear to play an important role in the induction of the tolerance response leading to a clinical improvement of symptoms.

| S-EPMC5607227 | biostudies-literature

Dermatophagoides pteronyssinus isolate:SZU

Project description:Raw small RNA Sequencing reads of Dermatophagoides pteronyssinus

| PRJNA577524 | ENA

Draft Genome Sequence of Dermatophagoides pteronyssinus, the European House Dust Mite.

Project description:Dermatophagoides pteronyssinus is the European dust mite and a major source of human allergens. Here, we present the first draft genome sequence of the mite, as well as the ab initio gene prediction and functional analyses that will facilitate comparative genomic analyses with other mite species.

| S-EPMC5552995 | biostudies-other

An Engineered Hybrid Protein from Dermatophagoides pteronyssinus Allergens Shows Hypoallergenicity.

Project description:The house dust mite (HDM) Dermatophagoides pteronyssinus is an important risk factor for asthma and rhinitis. Allergen specific immunotherapy that is based on recombinant proteins has been proposed for the safer and more efficient treatment of allergic diseases. The aim of this study was to design and obtain a hybrid protein (DPx4) containing antigenic regions of allergens Der p 1, Der p 2, Der p 7, and Der p 10 from this mite. DPx4 was produced in Escherichia coli and its folding was determined by circular dichroism. Non-denaturing dot-blot, ELISA, basophil activation test, dot blot with monoclonal antibodies, ELISA inhibition, and cysteine protease activity assays were performed. Mice that were immunized with DPx4 were also analyzed. We found that DPx4 had no cysteine protease activity and it showed significantly lower IgE reactivity than Der p 1, Der p 2, and D. pteronyssinus extract. DPx4 induced lower basophil activation than Der p 2 and the allergen extract. Immunized mice produced IgG antibodies that inhibited the binding of allergic patient's IgE to the allergen extract and induced comparatively higher levels of IL-10 than the extract in peripheral blood mononuclear cells (PBMC) culture. These results suggest that DPx4 has immunological properties that are useful for the development of a mite allergy vaccine.

| S-EPMC6628193 | biostudies-literature

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