The chitinase allergens Der p 15 and Der p 18 from <i>Dermatophagoides pteronyssinus</i>

O’Neil, Serena; Heinrich, Tatjana; Hales, Belinda J.; Hazell, L.A.; Holt, Deborah C.; Fischer, Katja; Thomas, Wayne R.

doi:10.1111/j.1365-2222.2006.02497.x

Cited by 57 publications

(61 citation statements)

References 25 publications

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“…Together with the data obtained with the group 2 and the lipid-binding group 13 and 14 mite allergens [69,70], lipid-binding properties could represent an important common feature of some HDM allergens. The association of natural lipidic adjuvants with these groups of mite allergens more likely facilitates the allergen sensitization process.The chitinase activity of group 15 and 18 mite allergens [71] could probably amplify the sensitization to HDM as mammalian chitinases or chitinase-like proteins, overproduced under a Th2-bias environment (IL-4, IL-13), may play a key role in the allergic inflammation [72,73]. …”

Section: Other Mite Allergen Groupsmentioning

confidence: 99%

The Role of the House Dust Mite-Induced Innate Immunity in Development of Allergic Response

Jacquet

2010

Int Arch Allergy Immunol

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House dust mite (HDM) represents one of the most common sources of aeroallergens worldwide and more than 50% of allergic patients are sensitized to these allergenic molecules. HDM allergy research in the past has been mainly focused on adaptive, mite allergen-dependent immune responses. In recent years it has become clear that, although the allergen-specific CD4+ Th2 cellsorchestrate HDM allergic response,the innate immune system also plays a critical role in HDM-induced allergy pathogenesis. This review will summarize insights into diverse determinants that contribute to the HDM allergenicity through the activation of innate immunity. In addition to the capacity of mite allergens to directly activate mainly skin keratinocytes and airway epithelial cells, innate pattern recognition receptor ligands derived from HDM carriers are also involved in the development of allergic response by HDM.

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Section: Other Mite Allergen Groupsmentioning

confidence: 99%

The Role of the House Dust Mite-Induced Innate Immunity in Development of Allergic Response

Jacquet

2010

Int Arch Allergy Immunol

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“…Interestingly, Der p 23 showed homology at the C terminus to the chitin-binding domain type 2 and the chitinbinding peritrophin-A domain. Chitin-binding domains were also identified in two other mite allergens, Der p 15 and Der p 18 (45). Der p 15 contains each of the three domains typical for insect chitinases (family 18 chitinases), an N-terminal glycosyl hydrolase catalytic region, a PEST-like domain, which is rich in amino acids proline (P), glutamate (E), serine (S), and threonine (T) and a C-terminal chitin-binding domain (46).…”

Section: Discussionmentioning

confidence: 99%

“…Der p 15 contains each of the three domains typical for insect chitinases (family 18 chitinases), an N-terminal glycosyl hydrolase catalytic region, a PEST-like domain, which is rich in amino acids proline (P), glutamate (E), serine (S), and threonine (T) and a C-terminal chitin-binding domain (46). Der p 18 has a truncated N-terminal glycosyl hydrolase catalytic region and the C-terminal chitin-binding domain but lacks the PEST-like region (45). However, Der p 23 is different from the two allergens because it lacks a catalytic region but possesses a PEST-like region and a chitin binding peritrophin-A domain.…”

Section: Discussionmentioning

confidence: 99%

Identification of Der p 23, a Peritrophin-Like Protein, As a New Major Dermatophagoides Pteronyssinus Allergen Associated with the Peritrophic Matrix of Mite Fecal Pellets

Vrtala¹,

Weghofer²,

Casset³

et al. 2013

Journal of Allergy and Clinical Immunology

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“…For HDM-allergic humans, the prevalence of IgE binding to Der p 15 and Der p 18 has previously been reported to be 70 [8] and 60% [8], respectively. For Der f 18, a 54% prevalence of binding has been reported [2].…”

Section: Introductionmentioning

confidence: 99%

Quantitation of IgE Binding to the Chitinase and Chitinase-Like House Dust Mite Allergens Der p 15 and Der p 18 Compared to the Major and Mid-Range Allergens

Hales

Elliot

Chai

et al. 2012

Int Arch Allergy Immunol

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Background: The prevalence of IgE binding to the group 15 and 18 house dust mite (HDM) allergens of the Dermatophagoides species is reported to be >50% and they are the major allergens of HDM-sensitised dogs. The objective was to quantitate the IgE titres to Der p 15 and Der p 18 and evaluate their importance in human HDM sensitisation compared to the known major and mid-tier allergens. Methods: Der p 15 and Der p 18 were produced in Pichia pastoris, and their structure validated by circular dichroism. IgE binding was measured in 37 Australian HDM-allergic adults using a quantitative DELFIA™ assay. Results: The prevalence of IgE titres to Der p 15 and Der p 18 >0.1 ng/ml was low (38%) and only one subject had a titre >10 ng/ml to either allergen. The mean anti-Der p 15 and Der p 18 titres were 1.2 and 2.6 ng/ml, respectively, i.e. approximately 10- to 20-fold lower than the response to the major Der p 1 and Der p 2 allergens (p < 0.001). The IgE responses to Der p 15 and Der p 18 were lower than the mid-tier allergens Der p 5 and Der p 7 and although they correlated with each other, they did not correlate with titres to either the major or mid-tier allergens. Conclusions: Sensitisation to Der p 15 and Der p 18 makes a minor contribution to anti-HDM IgE titres, and the titres do not correlate with the size of the response to the major allergens.

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The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus

Abstract: The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs.

Cited by 57 publications

References 25 publications

The Role of the House Dust Mite-Induced Innate Immunity in Development of Allergic Response

The Role of the House Dust Mite-Induced Innate Immunity in Development of Allergic Response

Identification of Der p 23, a Peritrophin-Like Protein, As a New Major Dermatophagoides Pteronyssinus Allergen Associated with the Peritrophic Matrix of Mite Fecal Pellets

Quantitation of IgE Binding to the Chitinase and Chitinase-Like House Dust Mite Allergens Der p 15 and Der p 18 Compared to the Major and Mid-Range Allergens

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