scholarly journals An Engineered Hybrid Protein from Dermatophagoides pteronyssinus Allergens Shows Hypoallergenicity

2019 ◽  
Vol 20 (12) ◽  
pp. 3025 ◽  
Author(s):  
Dalgys Martínez ◽  
Marlon Munera ◽  
Jose Fernando Cantillo ◽  
Judith Wortmann ◽  
Josefina Zakzuk ◽  
...  
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Dermatophagoides Pteronyssinus ◽  
Basophil Activation ◽  
Allergen Extract ◽  
Hybrid Protein ◽  
Dot Blot ◽  
Cysteine Protease Activity ◽  
Der P 1 ◽  
Der P 2

The house dust mite (HDM) Dermatophagoides pteronyssinus is an important risk factor for asthma and rhinitis. Allergen specific immunotherapy that is based on recombinant proteins has been proposed for the safer and more efficient treatment of allergic diseases. The aim of this study was to design and obtain a hybrid protein (DPx4) containing antigenic regions of allergens Der p 1, Der p 2, Der p 7, and Der p 10 from this mite. DPx4 was produced in Escherichia coli and its folding was determined by circular dichroism. Non-denaturing dot-blot, ELISA, basophil activation test, dot blot with monoclonal antibodies, ELISA inhibition, and cysteine protease activity assays were performed. Mice that were immunized with DPx4 were also analyzed. We found that DPx4 had no cysteine protease activity and it showed significantly lower IgE reactivity than Der p 1, Der p 2, and D. pteronyssinus extract. DPx4 induced lower basophil activation than Der p 2 and the allergen extract. Immunized mice produced IgG antibodies that inhibited the binding of allergic patient’s IgE to the allergen extract and induced comparatively higher levels of IL-10 than the extract in peripheral blood mononuclear cells (PBMC) culture. These results suggest that DPx4 has immunological properties that are useful for the development of a mite allergy vaccine.

Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity

2005 ◽  
Vol 328 (4) ◽  
pp. 944-952 ◽  
Author(s):  
Toshiro Takai ◽  
Takeshi Kato ◽  
Yasuhisa Sakata ◽  
Hiroshi Yasueda ◽  
Kenji Izuhara ◽  
...  
Keyword(s):  
Serine Protease ◽  
Cysteine Protease ◽  
Protease Activity ◽  
Cysteine Protease Activity ◽  
Serine Protease Activity ◽  
Der P 1

scholarly journals Proteolytic Cleavage of CD25, the α Subunit of the Human T Cell Interleukin 2 Receptor, by Der p 1, a Major Mite Allergen with Cysteine Protease Activity

1998 ◽  
Vol 187 (2) ◽  
pp. 271-275 ◽  
Author(s):  
Oliver Schulz ◽  
Herb F. Sewell ◽  
Farouk Shakib
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Human Peripheral Blood ◽  
Interleukin 2 ◽  
Interferon Γ ◽  
Th2 Cells ◽  
Α Subunit ◽  
Cysteine Protease Activity ◽  
Human T Cell ◽  
Der P 1

Recent reports have indicated that the cysteine protease activity of Der p 1 may play a significant role in its ability to elicit IgE antibody responses, mainly through cleavage of membrane CD23 on B cells and interleukin (IL)-4 synthesis and secretion from mast cells and basophils. Here we demonstrate for the first time that Der p 1 also cleaves the α subunit of the IL-2 receptor (IL-2R or CD25) from the surface of human peripheral blood T cells and, as a result, these cells show markedly diminished proliferation and interferon γ secretion in response to potent stimulation by anti-CD3 antibody. Given that the IL-2R is pivotal for the propagation of Th1 cells, its cleavage by Der p 1 may consequently bias the immune response towards Th2 cells, thereby creating an allergic microenvironment.

scholarly journals The Cysteine Protease Activity of the Major Dust Mite Allergen Der P 1 Selectively Enhances the Immunoglobulin E Antibody Response

1999 ◽  
Vol 190 (12) ◽  
pp. 1897-1902 ◽  
Author(s):  
Lucy Gough ◽  
Oliver Schulz ◽  
Herb F. Sewell ◽  
Farouk Shakib
Keyword(s):  
Cysteine Protease ◽  
Protease Activity ◽  
Immunoglobulin E ◽  
Specific Ige ◽  
Cysteine Protease Inhibitor ◽  
Cysteine Protease Activity ◽  
Dust Mite ◽  
Ige Synthesis ◽  
Der P 1

The house dust mite Dermatophagoides pteronyssinus allergen Der p 1 is the most immunodominant allergen involved in the expression of dust mite–specific immunoglobulin (Ig)E–mediated hypersensitivity. The reason for this potent IgE-eliciting property of Der p 1 remains unknown, but there is mounting in vitro evidence linking the allergenicity of Der p 1 to its cysteine protease activity. Here we demonstrate for the first time that immunization of mice with proteolytically active Der p 1 results in a significant enhancement in total IgE and Der p 1–specific IgE synthesis compared with animals immunized with Der p 1 that was irreversibly blocked with the cysteine protease inhibitor E-64. We conclude that the proteolytic activity of Der p 1 is a major contributor to its allergenicity.

scholarly journals Human glutathione-S-transferase pi potentiates the cysteine-protease activity of the Der p 1 allergen from house dust mite through a cysteine redox mechanism

Redox Biology ◽  
2019 ◽  
Vol 26 ◽  
pp. 101256 ◽  
Author(s):  
Juan Carlos López-Rodríguez ◽  
Juliana Manosalva ◽  
J. Daniel Cabrera-García ◽  
María M. Escribese ◽  
Mayte Villalba ◽  
...  
Keyword(s):  
House Dust ◽  
House Dust Mite ◽  
Cysteine Protease ◽  
Protease Activity ◽  
Glutathione S Transferase ◽  
Redox Mechanism ◽  
Cysteine Protease Activity ◽  
Dust Mite ◽  
Der P 1
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