A mite subversive: cleavage of CD23 and CD25 by Der p 1 enhances allergenicity

Shakib, F; Schulz, Oliver; Sewell, Herb F.

doi:10.1016/s0167-5699(98)01284-5

Cited by 158 publications

(136 citation statements)

References 46 publications

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“…Given its high prevalence, it is necessary to understand the mechanisms involved in triggering and perpetuating the allergic response. Recent work has suggested that the non-immunological properties, such as enzyme activity, of some allergens may contribute to their allergenicity (40). This is best exemplified by the major HDM allergen Der p 1, which elicits IgE responses in more than 80% of patients who are sensitive to D. pteronyssinus and is the most immunodominant allergen involved in the expression of IgEmediated dust mite hypersensitivity (24).…”

Section: Discussionmentioning

confidence: 99%

“…Based on cleavage sites of known protein substrates and using a panel of synthetic peptide substrates, it appears that Der p 1 has a preference for small aliphatic residues (Gly/Ala/Val) in the P2 position, charged residues (Asp/Glu/Arg) in the P1 position, and small hydrophobic/hydrophilic residues (Thr/Ser/Ala/Gly) in the P1Ј position (where the sequence surrounding the cleavage site is represented by P3, P2, P1, P1Ј, P2Ј, and P3Ј, and the site of cleavage is between P1 and P1Ј) (38,40). NhSP-D appeared to have several such potential cleavage sites throughout its sequence, whereas NhSP-A had only one within the CRD (Fig.…”

Section: Potential Cleavage Sites Of Der P In Sp-a and Sp-d-mentioning

confidence: 99%

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Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Section: Potential Cleavage Sites Of Der P In Sp-a and Sp-d-mentioning

confidence: 99%

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Deb

Shakib

Reid

et al. 2007

Journal of Biological Chemistry

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“…Dust mites represent a significant source of indoor allergens and are responsible for a substantial percentage of asthma cases (2). Experimental animal models using Dermatophagoides pteronyssinus to induce allergic responses through respiratory sensitization and challenge are now widely used and have led to a greater understanding of allergenicity (2)(3)(4)(5)(6). However, less attention has been paid to another major mite allergen, Blomia tropicalis, which is prevalent in tropical and subtropical regions of the world (7,8), where .2 billion people live.…”

mentioning

confidence: 99%

GM-CSF–Licensed CD11b+ Lung Dendritic Cells Orchestrate Th2 Immunity to Blomia tropicalis

Zhou

Schlitzer

et al. 2014

The Journal of Immunology

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The Blomia tropicalis dust mite is prevalent in tropical and subtropical regions of the world. Although it is a leading cause of asthma, little is known how it induces allergy. Using a novel murine asthma model induced by intranasal exposure to B. tropicalis, we observed that a single intranasal sensitization to B. tropicalis extract induces strong Th2 priming in the lung draining lymph node. Resident CD11b+ dendritic cells (DCs) preferentially transport Ag from the lung to the draining lymph node and are crucial for the initiation of Th2 CD4+ T cell responses. As a consequence, mice selectively deficient in CD11b+ DCs exhibited attenuated Th2 responses and more importantly did not develop any allergic inflammation. Conversely, mice deficient in CD103+ DCs and CCR2-dependent monocyte-derived DCs exhibited similar allergic inflammation compared with their wild-type counterparts. We also show that CD11b+ DCs constitutively express higher levels of GM-CSF receptor compared with CD103+ DCs and are thus selectively licensed by lung epithelial-derived GM-CSF to induce Th2 immunity. Taken together, our study identifies GM-CSF–licensed CD11b+ lung DCs as a key component for induction of Th2 responses and represents a potential target for therapeutic intervention in allergy.

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“…It has been reported that more than half of anti-mite allergen antibodies and 10 -20% of total IgE in aller-gic patients are anti-Der p 1 antibodies, which indicates that Der p 1 is one of the most immunodominant allergens (19,21). Der p 1 is a 25-kDa cysteine proteinase; its amino acid sequence conserves 3 critical amino acids (Cys-34, His-170, and Asn-190) comprising the catalytic triad as other cysteine proteinases (23). The structure of Der p 1 has been modeled based on the crystal structure of papain, suggesting that Der p 1 is composed of two domains separated by a cleft, where the active site with the catalytic triad locates (24).…”

mentioning

confidence: 99%

The Squamous Cell Carcinoma Antigen 2 Inhibits the Cysteine Proteinase Activity of a Major Mite Allergen, Der p 1

Sakata¹,

Arima²,

Takai

et al. 2004

Journal of Biological Chemistry

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The squamous cell carcinoma antigens 1 (SCCA1) and SCCA2 belong to the ovalbumin-serpin family. Although SCCA1 and SCCA2 are closely homologous, these two molecules have distinct properties; SCCA1 inhibits cysteine proteinases such as cathepsin K, L, and S, whereas SCCA2 inhibits serine proteinases such as cathepsin G and human mast cell chymase. Although several intrinsic target proteinases for SCCA1 and SCCA2 have been found, the biological roles of SCCA1 and SCCA2 remain unknown. A mite allergen, Der p 1, is one of the most immunodominant allergens and also acts as a cysteine proteinase probably involved in the pathogenesis of allergic diseases. We have recently shown that both SCCA1 and SCCA2 are induced by two related Th2-type cytokines, IL-4 and IL-13, in bronchial epithelial cells and that SCCA expression is augmented in bronchial asthma patients. In this study, we explored the possibility that SCCA proteins target Der p 1, and it turned out that SCCA2, but not SCCA1, inhibited the catalytic activities of Der p 1. We furthermore analyzed the inhibitory mechanism of SCCA2 on Der p 1. SCCA2 contributed the suicide substrate-like mechanism without formation of a covalent complex, causing irreversible impairment of the catalytic activity of Der p 1, as SCCA1 does on papain. In addition, resistance to cleavage by Der p 1 also contributed to the inhibitory mechanism of SCCA2. These results suggest that SCCA2 acts as a crossclass serpin targeting an extrinsic cysteine proteinase derived from house dust mites and that it may have a protective role against biological reactions caused by mites.

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A mite subversive: cleavage of CD23 and CD25 by Der p 1 enhances allergenicity

Cited by 158 publications

References 46 publications

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

Major House Dust Mite Allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 Degrade and Inactivate Lung Surfactant Proteins A and D

GM-CSF–Licensed CD11b+ Lung Dendritic Cells Orchestrate Th2 Immunity to Blomia tropicalis

The Squamous Cell Carcinoma Antigen 2 Inhibits the Cysteine Proteinase Activity of a Major Mite Allergen, Der p 1

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