The effect of Dermatophagoides pteronyssinus group 7 allergen (Der p 7) on dendritic cells and its role in T cell polarization

Tsai, Jaw‐Ji; Wang, Hsin-Chieh; Chiu, Chih-Liang; Liao, En-Chih

doi:10.1016/j.imbio.2016.04.002

Cited by 12 publications

(6 citation statements)

References 20 publications

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“…There is a large degree of T cell cross-reactivity between the whole purified allergen from each species, according to the proliferative and cytokine response to the group 1 and group 7 allergens [71]. Der p 7 is a glycoprotein and performs its function partially through glycan binding, it can activate BMDCs through TLR4 and DC-SIGN, and establish a link between innate TLR4-C-type lectin receptors and adaptive Th2 immunity [72]. Normally, the frequency of IgE-binding to the allergen in sera from an allergic population is used to determine the relative importance of the individual house dust mite allergens, and the equivalent increased IL-5 response of PBMC to group 7 and group 1 allergen (different IgE-inducing activity) indicates that allergens may be equally capable of contributing to an asthmatic response by inducing eosinophilia [73].…”

Section: Discussionmentioning

confidence: 99%

Transcriptome-based analysis of putative allergens of Chorioptes texanus

Xie

et al. 2019

Parasites Vectors

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BackgroundMites of the genus Chorioptes are non-burrowing and cause mange in a wide range of domestic and wild animals including cattle, horses, sheep, goats, panda, moose, camelids, mydaus and alpacas. Molecular biology and host-parasite interactions of Chorioptes texanus are poorly understood, and only a few C. texanus genes and transcript sequences are available in public databases including the allergen genes.MethodsChorioptes texanus RNA was isolated from mites, and the transcriptome of C. texanus was analyzed using bioinformatics tools. Chorioptes texanus unigenes were compared with the allergen protein sequences from the mite allergen database website to predict the potential allergens. Chorioptes texanus putative allergen unigenes were compared with hydrolase genes by building a C. texanus hydrolase gene library with the best match of the homologous sequences. Three allergen genes were cloned and expressed, their recombinant proteins were purified and their allergenic activities were preliminarily investigated.ResultsTranscriptome sequencing (RNA-Seq) of C. texanus was analyzed and results demonstrated that 33,138 unigenes were assembled with an average length of 751 bp. A total of 15,130 unigenes were annotated and 5598 unigenes were enriched in 262 KEGG signaling pathways. We obtained 209 putative allergen genes and 34 putative allergen-hydrolase genes. Three recombinant allergen proteins were observed to induce different degrees of allergic reactions on rabbit skin.ConclusionsThe present transcriptome data provide a useful basis for understanding the host-parasite interaction and molecular biology of the C. texanus mite. The allergenic activities of recombinant Euroglyphus maynei 1-like (Eur m 1-like) protein, Dermatophagoides ptreronyssinus 1-like (Der p 1-like) protein and Dermatophagoides ptreronyssinus 7-like (Der p 7-like) protein were preliminarily investigated by intradermal skin test. Meanwhile, differences in eosinophil counts were observed in different injected sites of the skin. The identification of putative allergen genes and hydrolase genes offers opportunities for the development of new diagnostic, prevention and treatment methods.

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Section: Discussionmentioning

confidence: 99%

Transcriptome-based analysis of putative allergens of Chorioptes texanus

Xie

et al. 2019

Parasites Vectors

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“…Der p 1 and Der p 2 are naturally glycosylated and interact with mannose receptor and DC-SIGN, respectively (33)(34)(35)(36). Recombinant Der p 7 produced in P. pastoris could bind to DC-SIGN as well but the glycosylation and the binding to CLR were not evidenced for native Der p 7 (37). The only HDM allergen showing binding activity to epithelial Dectin-1 was the structural tropomyosin Der p 10 allergen, however devoid of glycosylation (16).…”

Section: Purified Natural or Recombinant Hdm Allergensmentioning

confidence: 99%

Characterization of Innate Immune Responses to House Dust Mite Allergens: Pitfalls and Limitations

Jacquet

2021

Front.Allergy

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Whereas house dust mite (HDM) allergy results from a dysregulated Th2-biased adaptive immune response, activation of innate immune signaling pathways is a critical prerequisite for the initiation of HDM sensitizations. Such innate sensing is mainly controlled by the airway epithelium and the skin. The resulting release of epithelial-derived proinflammatory cytokines and innate alarmins such as GM-CSF, IL-25, IL-33 and TSLP mediates the activation of ILC2 cells and cDCs to promote Th2-biased inflammation. Significant progress in the elucidation of HDM innate immune activation has been made in the past decade and highlighted key roles of the LPS/TLR4 axis, chitin-dependent pathways together with HDM protease allergens. However, the precise mechanisms by which HDM allergens are sensed by the innate immune system remain largely unknown. Such investigations are made difficult for several reasons. Among these are (1) the natural association of HDM allergens with immunostimulators from the mite exoskeleton as well as from environmental microorganisms/pollutants or endosymbiotic bacteria; (2) the purification of individual HDM allergens from extracts in sufficient amounts and devoid of any microbial and protein impurities; (3) the production of correctly folded recombinant HDM allergens which could display the same biological activity than their natural counterparts; (4) the accessibility to human epithelial samples with cellular heterogeneities and inter-donor variations; (5) the translation of experimental data from mouse models to humans is almost missing. The goal of the present mini-review is to emphasize some important limitations and pitfalls in the elucidation of innate immunostimulatory properties of HDM allergens.

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“…Bactericidal permeability-increasinglike protein 78,79 TLR2 > TLR4 80,81 In rodent models, TLR2 redundant for allergy? 22 this suppressive mechanism underpins the protection against allergy associated with increased TLR4 exposure in children born to mothers exposed to high levels of LPS.…”

Section: Chymotrypsin-like Serine Proteasesmentioning

confidence: 99%

“…Group 7 allergens from D pteronyssinus and D farinae possess a lipid‐binding domain, formed from antiparallel β‐sheets woven around a helical core, which can weakly bind the lipopeptide polymyxin . Although structural homology with LPS‐binding protein suggests that LPS might be their preferred ligand, surprisingly this is probably not so; while rDer p 7 (glycosylated) stimulated the dendritic cell–specific intercellular adhesion molecule‐3‐grabbing nonintegrin (DC‐SIGN)–dependent expression of IL‐6, OX40L and Jagged‐1 by DCs, it was relatively insensitive to the blockade of TLR4 . The group 7 allergen, Blo t 7, from the tropical mite Blomia tropicalis is less identical (~30%) to its Dermatophagoides genus counterparts (>85% identical), but the lipid‐binding site is well conserved and binds hydrophobic ligands.…”

Section: Hdm Allergens and Toll‐like Receptorsmentioning

confidence: 99%

Proteolytic, lipidergic and polysaccharide molecular recognition shape innate responses to house dust mite allergens

Jacquet

Robinson

2019

Allergy

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House dust mites (HDMs) are sources of an extensive repertoire of allergens responsible for a range of allergic conditions. Technological advances have accelerated the identification of these allergens and characterized their putative roles within HDMs. Understanding their functional bioactivities is illuminating how they interact with How to cite this article: Jacquet A, Robinson C. Proteolytic, lipidergic and polysaccharide molecular recognition shape innate responses to house dust mite allergens. Allergy.

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The effect of Dermatophagoides pteronyssinus group 7 allergen (Der p 7) on dendritic cells and its role in T cell polarization

Cited by 12 publications

References 20 publications

Transcriptome-based analysis of putative allergens of Chorioptes texanus

Transcriptome-based analysis of putative allergens of Chorioptes texanus

Characterization of Innate Immune Responses to House Dust Mite Allergens: Pitfalls and Limitations

Proteolytic, lipidergic and polysaccharide molecular recognition shape innate responses to house dust mite allergens

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