Allergens with Protease Activity from House Dust Mites

Abstract

Globally, house dust mites (HDM) are one of the main sources of allergens causing Type I allergy, which has a high risk of progressing into a severe disabling disease manifestation such as allergic asthma. The strong protease activities of a number of these allergens are thought to be involved in several steps of the pathophysiology of this allergic disease. It has been a common notion that protease activity may be one of the properties that confers allergenicity to proteins. In this review we summarize and discuss the roles of the different HDM proteases in the development of Type I allergy.

House dust mites activate nociceptor–mast cell clusters to drive type 2 skin inflammation

“…The sensing of allergen-associated proteolytic activity has been proposed to be an important mechanism of environmental allergen detection that could contribute to the initiation of allergic diseases 31,36 . Our data suggest that the clusters of TRPV1 + nociceptors and MRGPRB2 + mast cells might represent tissue-resident "sensory systems" that would detect allergens with cysteine-like protease activity in the skin and initiate type 2 immunityassociated allergic skin disease.…”

“…Next, we investigated whether the proteolytic activity of D. farinae was required for triggering DRG neuron activation ex vivo. Like other common environmental allergens, HDM strains, including D. farinae 31 have intrinsic proteolytic activity that can degrade epithelial junctions [32][33][34][35] or full-length IL-33 36 in vivo. To characterize the type of proteolytic activity present in the D. farinae extracts used, we measured the proteolytic activities of D. farinae with or without specific and irreversible inhibitors of cysteine or serine protease activities.…”

“…4a,b). We next investigated whether other clinically-relevant environmental allergens with either predominant cysteine protease activity, such as the HDM strain D. pteronyssinus 31 or serine-like protease activities 36 from pollen (ragweed), fungus (Alternaria alternata) or the German cockroach could also directly activate DRG neurons. Only D. pteronyssinus triggered significant influx of calcium in DRG neurons, comparable to those obtained after stimulation with D. farinae (Fig.…”

Mouse Models for Food Allergies: Where Do We Stand?

“…In addition, the specific properties of the allergens themselves contribute to their allergenicity. Here, increased sensitizing properties were attributed to allergen molecules with either intrinsic immune activating properties (reviewed in [21]), proteolytic activity [22], or increased stability towards heat and proteases [22,23,24].…”

A genomic analysis and transcriptomic atlas of gene expression inPsoroptes ovisreveals feeding- and stage-specific patterns of allergen expression

“…In total, 73 of the 526 genes in this cluster (14%) were assigned Enzyme Commission (EC) codes, distributed as follows: hydrolases (n=27), oxidoreductases (n=21), transferases (n=15), lyases (n=5), ligases (n=4) and isomerases (n=1). A further factor contributing to the large numbers of enzymes within this cluster could be the presence of numerous putative P. ovis allergens, many of which are homologues of HDM allergens and several of which show protease activity [52]. Putative allergen genes enriched within the tritonymph cluster included some of the most abundant P. ovis allergens, i.e.…”