Proteases of Dermatophagoides pteronyssinus

Randall, Thomas A.; London, Robert E.; Fitzgerald, Michael C.; Mueller, Geoffrey A.

doi:10.3390/ijms18061204

Cited by 15 publications

(15 citation statements)

References 46 publications

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“…HDM is a complex allergen that is comprised of both mites and fecal pellets. 26,59 Important components of HDM allergen are serine and cysteine proteases that signal through PARs, such as PAR-2, to amplify allergic airway inflammation. Furthermore, multiple HDM allergens can activate PAR-2, whereas PAR-2deficient mice have reduced HDM-induced allergic airway inflammation.…”

Section: Discussionmentioning

confidence: 99%

Apolipoprotein E is a concentration-dependent pulmonary danger signal that activates the NLRP3 inflammasome and IL-1β secretion by bronchoalveolar fluid macrophages from asthmatic subjects

Gordon

Yao

et al. 2019

Journal of Allergy and Clinical Immunology

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Background: House dust mite (HDM)-challenged Apoe 2/2 mice display enhanced airway hyperreactivity and mucous cell metaplasia. Objective: We sought to characterize the pathways that induce apolipoprotein E (APOE) expression by bronchoalveolar lavage fluid (BALF) macrophages from asthmatic subjects and identify how APOE regulates IL-1b secretion. Methods: Macrophages were isolated from asthmatic BALF and derived from THP-1 cells and human monocytes. Results: HDM-derived cysteine and serine proteases induced APOE secretion from BALF macrophages through proteaseactivated receptor 2. APOE at concentrations of less than 2.5 nmol/L, which are similar to levels found in epithelial lining fluid from healthy adults, did not induce IL-1b release from BALF macrophages. In contrast, APOE at concentrations of 25 nmol/L or greater induced nucleotide-binding oligomerization domain, leucine-rich repeat-containing protein (NLRP) 3 and pro-IL-1b expression by BALF macrophages, as well as the caspase-1-mediated generation of mature IL-1b secreted from cells. HDM acted synergistically with APOE to both prime and activate the NLRP3 inflammasome. In a murine model of neutrophilic airway inflammation induced by HDM and polyinosinic-polycytidylic acid, APOE reached a concentration of 32 nmol/L in epithelial lining fluid, with associated increases in BALF IL-1b levels. APOE-dependent NLRP3 inflammasome activation in macrophages was primarily mediated through a potassium efflux-dependent mechanism. Conclusion: APOE can function as an endogenous, concentration-dependent pulmonary danger signal that primes and activates the NLPR3 inflammasome in BALF macrophages from asthmatic subjects to secrete IL-1b. This might represent a mechanism through which APOE amplifies pulmonary inflammatory responses when concentrations in the lung are increased to greater than normal levels, which can occur during viral exacerbations of HDM-induced asthma characterized by neutrophilic airway inflammation.

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Section: Discussionmentioning

confidence: 99%

Apolipoprotein E is a concentration-dependent pulmonary danger signal that activates the NLRP3 inflammasome and IL-1β secretion by bronchoalveolar fluid macrophages from asthmatic subjects

Gordon

Yao

et al. 2019

Journal of Allergy and Clinical Immunology

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“…Perhaps the best‐known example is the house dust mite allergen, Der p 1, a proteolytic enzyme capable of cleaving CD23 (FcεRII, the low‐affinity IgE receptor) and CD25 (IL‐2 receptor α‐chain) expressed on the surface of some B cells, resulting in dysregulation of the immune response and induced production of IgE . The allergenicity of these proteins is not limited to their enzymatic activity, however, and both relative abundance and stability have been cited as of equal importance . Pyruvate kinases, enolases and aldolases have been shown to be abundant but heat‐labile proteins in fish and shrimp …”

Section: Discussionmentioning

confidence: 99%

“…36 The allergenicity of these proteins is not limited to their enzymatic activity, however, and both relative abundance and stability have been cited as of equal importance. 37,38 Pyruvate kinases, enolases and aldolases have been shown to be abundant but heat-labile proteins in fish 22 and shrimp. 21 The objective of this work was to identify whether cross-reactive IgE-binding proteins were present in C and fish, which could explain the frequency of sensitizations to these foods.…”

Section: Discussionmentioning

confidence: 99%

Serum IgE cross‐reactivity between fish and chicken meats in dogs

Bexley

Kingswell

Olivry

2018

Veterinary Dermatology

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Background In humans, a cross‐reactive clinical allergy has been reported between three chicken and fish meat proteins: beta‐enolase, aldolase A and parvalbumin. Objective To evaluate if IgE cross‐reactivity between chicken and fish also existed in the dog. Animals Sera from dogs with suspected allergic skin disease and with IgE against chicken and fish. Methods and materials Sera were analysed by ELISA and immunoblotting with chicken, white fish (haddock and cod) and salmon extracts. Reciprocal inhibition ELISAs and inhibition immunoblots were then performed. Protein sequencing of bands identified on multiple extracts was determined by mass spectrometry. Results Out of 53 archived canine sera tested by ELISA against chicken, white fish or salmon, 15 (28%), 12 (23%) and 26 (49%), respectively, had elevated IgE against one, two or all three of these extracts. Seven of the triple‐reactive sera were subjected to reciprocal inhibition ELISAs. A >50% inhibition was found between chicken–fish, chicken–salmon and fish–salmon in seven, four and five of seven dogs, respectively. Immunoblotting identified multiple IgE‐binding proteins of identical molecular weights in the three extracts; these were partially to fully cross‐reactive by inhibition immunoblotting. Mass spectrometry identified nine cross‐reactive proteins as: pyruvate kinase, creatine kinase, alpha‐actin, glyceraldehyde‐3‐phosphate dehydrogenase, beta‐enolase, aldolase, malate dehydrogenase, lactate dehydrogenase and triose‐phosphate isomerase 1. All of these have been reported previously as fish, shellfish and/or chicken allergens for humans. Conclusions and clinical importance Whether any of these newly identified IgE cross‐reactive chicken–fish allergens is the cause of clinical allergy needs to be determined in dogs reacting to at least two of these common food sources.

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“…HDMs have enzymes with protease activity, and those allergenic are most abundant 77. Group 1 allergens are cysteine protease ( e.g .…”

Section: The Current and Projected Influence Of Environmental Changesmentioning

confidence: 99%

House Dust Mite Allergy Under Changing Environments

Acevedo

Zakzuk

Caraballo

2019

Allergy Asthma Immunol Res

115

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Environmental variations induced by industrialization and climate change partially explain the increase in prevalence and severity of allergic disease. One possible mechanism is the increase in allergen production leading to more exposure and sensitization in susceptible individuals. House dust mites (HDMs) are important sources of allergens inducing asthma and rhinitis, and experimentally they have been demonstrated to be very sensitive to microenvironment modifications; therefore, global or regional changes in temperature, humidity, air pollution or other environmental conditions could modify natural HDM growth, survival and allergen production. There is evidence that sensitization to HDMs has increased in some regions of the world, especially in the subtropical and tropical areas; however, the relationship of this increase with environmental changes is not so clear as has reported for pollen allergens. In this review, we address this point and explore the effects of current and predicted environmental changes on HDM growth, survival and allergen production, which could lead to immunoglobulin E (IgE) sensitization and allergic disease prevalence. We also assess the role of adjuvants of IgE responses, such as air pollution and helminth infections, and discuss the genetic and epigenetic aspects that could influence the adaptive process of humans to drastic and relatively recent environmental changes we are experiencing.

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Proteases of Dermatophagoides pteronyssinus

Cited by 15 publications

References 46 publications

Apolipoprotein E is a concentration-dependent pulmonary danger signal that activates the NLRP3 inflammasome and IL-1β secretion by bronchoalveolar fluid macrophages from asthmatic subjects

Apolipoprotein E is a concentration-dependent pulmonary danger signal that activates the NLRP3 inflammasome and IL-1β secretion by bronchoalveolar fluid macrophages from asthmatic subjects

Serum IgE cross‐reactivity between fish and chicken meats in dogs

House Dust Mite Allergy Under Changing Environments

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