Der p 1 is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus
The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between protea...
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| Published in | Biochimica et biophysica acta Vol. 1840; no. 3; pp. 1117 - 1124 |
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| Main Authors | , , , , , , , , , |
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Elsevier B.V
01.03.2014
Elsevier Science |
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| Abstract | The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade.
The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus.
All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite.
Der p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases.
This finding suggests that Der p 1 may be valuable target against mites.
•We elicited the activation mechanism of proteases in D. pteronyssinus.•Der p 1 is the major activator of digestive mite cysteine and serine proteases.•Der p 1 (recombinant or natural) cleaves proDer p 1, 3, 6 and probably proDer p 9.•The propeptide inhibits the proteolytic activity of Der p 6.•As Der p 1, Der p 6 chymotrypsin is present in the mite gut. |
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| AbstractList | The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade.BACKGROUNDThe enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade.The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus.METHODSThe cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus.All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite.RESULTSAll peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite.Der p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases.CONCLUSIONSDer p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases.This finding suggests that Der p 1 may be valuable target against mites.GENERAL SIGNIFICANCEThis finding suggests that Der p 1 may be valuable target against mites. The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade.The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus.All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite.Der p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases.This finding suggests that Der p 1 may be valuable target against mites. Background: The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade. Methods: The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfermethod. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanismbymite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus. Results: All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite. Conclusions: Der p 1 in either its recombinant formor in the natural context of house dustmite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases. General significance: This finding suggests that Der p 1 may be valuable target against mites. The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade. The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus. All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite. Der p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases. This finding suggests that Der p 1 may be valuable target against mites. The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim was to elucidate the activation cascade of their corresponding precursor forms and particularly to highlight the interconnection between proteases during this cascade. The cleavage of the four peptides corresponding to the mite zymogen activation sites was studied on the basis of the Förster Resonance Energy Transfer method. The proDer p 6 zymogen was then produced in Pichia pastoris to elucidate its activation mechanism by mite proteases, especially Der p 1. The role of the propeptide in the inhibition of the enzymatic activity of Der p 6 was also examined. Finally, the Der p 1 and Der p 6 proteases were localised via immunolocalisation in D. pteronyssinus. All peptides were specifically cleaved by Der p 1, such as proDer p 6. The propeptide of proDer p 6 inhibited the proteolytic activity of Der p 6, but once cleaved, it was degraded by the protease. The Der p 1 and Der p 6 proteases were both localised to the midgut of the mite. Der p 1 in either its recombinant form or in the natural context of house dust mite extracts specifically cleaves all zymogens, thus establishing its role as a major activator of both mite cysteine and serine proteases. This finding suggests that Der p 1 may be valuable target against mites. •We elicited the activation mechanism of proteases in D. pteronyssinus.•Der p 1 is the major activator of digestive mite cysteine and serine proteases.•Der p 1 (recombinant or natural) cleaves proDer p 1, 3, 6 and probably proDer p 9.•The propeptide inhibits the proteolytic activity of Der p 6.•As Der p 1, Der p 6 chymotrypsin is present in the mite gut. |
| Author | Mailleux, Anne-Catherine Dumez, Marie-Eve De Pauw, Edwin Cloes, Marie Chevigné, Andy Herman, Julie Thelen, Nicolas Luxen, André Galleni, Moreno Smargiasso, Nicolas |
| Author_xml | – sequence: 1 givenname: Julie surname: Herman fullname: Herman, Julie organization: Macromolécules Biologiques, Centre for Protein Engineering, University of Liège, 4000 Liège, Belgium – sequence: 2 givenname: Nicolas surname: Thelen fullname: Thelen, Nicolas organization: Unit of Cell and Tissue Biology, GIGA-Neurosciences, University of Liège, 4000 Liège, Belgium – sequence: 3 givenname: Nicolas surname: Smargiasso fullname: Smargiasso, Nicolas organization: Mass Spectrometry Laboratory, GIGA-R, Department of Chemistry, University of Liège, 4000 Liège, Belgium – sequence: 4 givenname: Anne-Catherine surname: Mailleux fullname: Mailleux, Anne-Catherine organization: Earth and Life Institute, Université catholique de Louvain, 1348 Louvain-la-Neuve, Belgium – sequence: 5 givenname: André surname: Luxen fullname: Luxen, André organization: Centre de Recherche du Cyclotron, University of Liège, 4000 Liège, Belgium – sequence: 6 givenname: Marie surname: Cloes fullname: Cloes, Marie organization: Unit of Cell and Tissue Biology, GIGA-Neurosciences, University of Liège, 4000 Liège, Belgium – sequence: 7 givenname: Edwin surname: De Pauw fullname: De Pauw, Edwin organization: Mass Spectrometry Laboratory, GIGA-R, Department of Chemistry, University of Liège, 4000 Liège, Belgium – sequence: 8 givenname: Andy surname: Chevigné fullname: Chevigné, Andy organization: Laboratory of Retrovirology, CRP-Santé, 1526 Luxembourg, Luxembourg – sequence: 9 givenname: Moreno surname: Galleni fullname: Galleni, Moreno email: mgalleni@ulg.ac.be organization: Macromolécules Biologiques, Centre for Protein Engineering, University of Liège, 4000 Liège, Belgium – sequence: 10 givenname: Marie-Eve surname: Dumez fullname: Dumez, Marie-Eve organization: Macromolécules Biologiques, Centre for Protein Engineering, University of Liège, 4000 Liège, Belgium |
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| Keywords | SBTI Mite allergen HDM(e) E-64 DAPI pDp6 FP PMg Digestion Dermatophagoides pteronyssinus nDer p 6 Protease AMC rDer p 6 FRET AMg rDer p 1 Hg Förster Resonance Energy Transfer natural Der p 6 recombinant Der p 1 hindgut 7-amido-4-methylcoumarin proDer p 6 recombinant Der p 6 4′,6-DiAmidino-2-PhenylIndole anterior midgut posterior midgut soybean trypsin inhibitor house dust mite (extracts) l-trans-epoxysuccinyl-leucylamido (4-guanidino) butane faecal pellet |
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| Snippet | The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of allergy. Our aim... Background: The enzymatic activity of the four proteases found in the house dust mite Dermatophagoides pteronyssinus is involved in the pathogenesis of... |
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| SubjectTerms | Allergens Allergens - metabolism AMC AMg Amino Acid Sequence Animals Antigens, Dermatophagoides Antigens, Dermatophagoides - analysis Antigens, Dermatophagoides - metabolism Arthropod Proteins Arthropod Proteins - analysis Arthropod Proteins - metabolism Biochemistry, biophysics & molecular biology Biochimie, biophysique & biologie moléculaire cysteine Cysteine Endopeptidases Cysteine Endopeptidases - analysis Cysteine Endopeptidases - metabolism DAPI Dermatophagoides pteronyssinus Dermatophagoides pteronyssinus - immunology Digestion dust dust mites E-64 energy transfer Enzyme Activation enzyme activity enzyme inhibition Enzyme Precursors Enzyme Precursors - metabolism Forster resonance energy transfer FRET Förster Resonance Energy Transfer HDM(e) hypersensitivity Komagataella pastoris Life sciences midgut Mite allergen Molecular Sequence Data pathogenesis peptides Pichia pastoris PMg Protease proteinases Proteolysis Recombinant Proteins Recombinant Proteins - metabolism SBTI Sciences du vivant serine Serine Endopeptidases Serine Endopeptidases - analysis Serine Endopeptidases - metabolism zymogens |
| Title | Der p 1 is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus |
| URI | https://dx.doi.org/10.1016/j.bbagen.2013.11.017 https://www.ncbi.nlm.nih.gov/pubmed/24291687 https://www.proquest.com/docview/1492683416 https://www.proquest.com/docview/2000226508 http://orbi.ulg.ac.be/handle/2268/163997 |
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