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.
Highlights
House dust mites (HDM) are the most prevalent source of indoor allergens worldwide, with 1–2% of the total population experiencing an allergic response in their presence [1]
We have examined and report the D. pteronyssinus airmid predicted proteome, mite body proteome and excretome with reference to a wild-type proteome as a means of (i) identifying potentially allergenic proteins, (ii) inferring localisation of allergenic and potentially allergenic molecules, and (iii) identifying proteins involved in key physiological processes
Our results show that D. farinae, D. pteronyssinus, and E. maynei contained at least one Mite group allergen (MGA) ortholog for all groups investigated, with the exception of Groups 23 & 24 in E. maynei
Summary
House dust mites (HDM) are the most prevalent source of indoor allergens worldwide, with 1–2% of the total population experiencing an allergic response in their presence [1]. HDM allergens are major causative agents in the pathogenesis of asthma, allergic rhinitis and atopic dermatitis [2]. Protease allergens disrupt the epithelial barrier and activate immune cells resulting in the production of large amounts of proinflammatory cytokines [3, 4]. Proteome and allergenome of Dermatophagoides pteronyssinus spectrometry facilities were funded by Science Foundation Ireland (SFI 12/RI/2346(3)). We acknowledge the DJEI/DES/SFI/HEA Irish Centre for High-End Computing (ICHEC) for the provision of computational facilities and support. EBM and NG are employees of Airmid Healthgroup Ltd. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
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