Proteome and allergenome of the European house dust mite Dermatophagoides pteronyssinus

Abstract

The European house dust mite Dermatophagoides pteronyssinus is of significant medical importance as it is a major elicitor of allergic illnesses. In this analysis we have undertaken comprehensive bioinformatic and proteomic examination of Dermatophagoides pteronyssinus airmid, identified 12,530 predicted proteins and validated the expression of 4,002 proteins. Examination of homology between predicted proteins and allergens from other species revealed as much as 2.6% of the D . pteronyssinus airmid proteins may cause an allergenic response. Many of the potential allergens have evidence for expression ( n = 259) and excretion ( n = 161) making them interesting targets for future allergen studies. Comparative proteomic analysis of mite body and spent growth medium facilitated qualitative assessment of mite group allergen localisation. Protein extracts from house dust contain a substantial number of uncharacterised D . pteronyssinus proteins in addition to known and putative allergens. Novel D . pteronyssinus proteins were identified to be highly abundant both in house dust and laboratory cultures and included numerous carbohydrate active enzymes that may be involved in cuticle remodelling, bacteriophagy or mycophagy. These data may have clinical applications in the development of allergen-specific immunotherapy that mimic natural exposure. Using a phylogenomic approach utilising a supermatrix and supertree methodologies we also show that D . pteronyssinus is more closely related to Euroglyphus maynei than Dermatophagoides farinae .

Mechanisms of allergen-specific immunotherapy for allergic rhinitis and food allergies

“…For instance, patients with IgE sensitivities to grass pollen profilin Phl p12 might lead to up-regulated sIgE production and false skin prick test to whole birch pollen due to the cross-reactivity with birch profilin Bet v2 while the patients with high IgE levels to Phl p 1 and Phl p5 might represent good candidates for grass pollen immunotherapy [6]. To better improve patient selection for AIT, more effort has been invested on the characterization of allergen extracts using transcriptomics and proteomics approaches and profiling of their IgE reactivity [183][184][185]. The development and use of purified recombinant allergen, fusion of several allergens or hypoallergenic allergen derivatives will allow standardization of the allergen as compared to currently used natural allergen extracts, thereby expanding our knowledge on the disease mechanism and improving diagnosis and AIT for allergies [186].…”

Susceptibility Factors in Chronic Lung Inflammatory Responses to Engineered Nanomaterials

“…Proteolytic allergens from the house dust mite (HDM) Dermatophagoides pteronyssinus are common indoor allergens [ 176 , 228 , 229 ]. Early life exposure to HDM allergens, including Der p1 and Der p2, has been linked to the development of asthma in humans [ 230 , 231 , 232 ].…”

Characterisation of three novel β-1,3 glucanases from the medically important house dust mite Dermatophagoides pteronyssinus (airmid)

“…Culture and protein extraction from D. pteronyssinus airmid mite body (MB) and spent culture medium (SM) were conducted as described in Waldron et al (2019). Briefly, SM was obtained by sieving (300 μm mesh) whole cultures to remove mites and ultimately contained leftover diet, mite faeces and a small number of live mites (10.8 mites per mg).…”

“…Protein extracts from D pteronyssinus airmid were prepared and analysed by LC-MS/MS as described by Waldron et al (2019). Protein identification and label free quantitative (LFQ) analysis was conducted using MaxQuant (Version 1.6.1.0; http://maxquant.org/), statistical analysis of MaxQuant output data was performed by Perseus (Version 1.6.2.2) as described in O'Keeffe et al (2014) using a custom contaminants database containing yeast and porcine proteins (Waldron et al, 2019). Yeast-derived proteins are degraded by HDM during the feeding process and are effectively absent from SM prior to proteomic analysis.…”

“…In previous work, we identified six putative GH16 proteins with predicted β-1,3 glucanase activity in D. pteronyssinus airmid, four were https://doi.org/10.1016/j.ibmb.2019.103242 Received 17 June 2019; Received in revised form 9 September 2019; Accepted 9 September 2019 validated as expressed (Waldron et al, 2019). Moreover, previous studies have demonstrated βglucosidase activity to be present in protein extracts from D. pteronyssinus (Martinez et al, 1999).…”