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Information on EC 3.4.22.65 - peptidase 1 (mite) and Organism(s) Dermatophagoides pteronyssinus and UniProt Accession P08176
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3.4.22.65 peptidase 1 (mite)Specify your search results
Word Map
- 3.4.22.65
-
allergic
- asthma
- ige
- dermatophagoides
- pteronyssinus
- children
-
home
-
asthmatic
-
atopic
- farinae
- airway
-
indoor
-
immunotherapy
-
mattress
- bronchial
- rhinitis
-
inhale
-
prick
-
allergen-specific
-
floor
-
carpet
-
bedroom
- dermatitis
-
humid
-
hyperresponsiveness
-
airborne
-
household
-
houses
- cockroach
-
aeroallergens
-
vacuum
-
wheeze
-
house-dust
-
ige-binding
-
cleaner
- ras
- blomia
-
anti-der
-
allergen-induced
-
rhinoconjunctivitis
-
component-resolved
-
mite-induced
-
radioallergosorbent
- diagnostics
-
hdm-induced
-
hypoallergenic
- pharmacology
-
nonatopic
- medicine
-
wheal
-
immunocap
-
dander
-
skin-prick
- drug development
The taxonomic range for the selected organisms is: Dermatophagoides pteronyssinus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
the proteolytic activity of Der f 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production
Synonyms
der p 1, mite allergen, der f 1, house dust mite allergen, der p1, house dust mite allergens, der f1, der p 7, allergen der p 1, allergen der p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
allergen Der f1
-
-
-
-
CO1.073
-
-
-
-
Der f 1
-
-
-
-
Der p 1
Der p 1
-
-
-
-
Der p 1
-
-
Der p 1
-
automaturation product of proDer p 1 (proDer p 1.0105 isoform)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-aminobenzoyl)-Val-Ala-norLeu-Ser-Tyr(3-NO2)-Asp + H2O
?
-
ADZ 50,059
-
-
?
2-aminobenzoic acid-Val-Ala-Nle-Ser-(3-nitro)-tyrosinyl-aspartamide + H2O
?
-
-
-
-
?
alpha1-antitrypsin + H2O
?
-
recombinant Der p 1 previously activated with L-cysteine or DTT
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-MCA + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-Gln-Gly-Arg-MCA + H2O
butyloxycarbonyl-Gln-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-Phe-Ser-Arg-MCA + H2O
butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
butyloxycarbonyl-Val-Leu-Lys-MCA + H2O
butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
chestnut cystatin + H2O
?
-
specific proteolytic cleavage between Gly6 and Val7, giving rise to a noninhibitory processed protein. Not cleaved by Der f 1 from Dermatophygoides farinae
-
-
?
Der p 1 propiece + H2O
?
-
potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
succinyl-Leu-Leu-Val-Tyr-MCA + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-4-methylcoumarin 7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pro-Der p 3 + H2O
Der p 3 + Der p 3 propeptide
activation
-
-
?
pro-Der p 3 + H2O
Der p 3 + Der p 3 propeptide
activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen
-
-
?
pro-Der p 6 + H2O
Der p 6 + Der p 6 propeptide
activation
-
-
?
pro-Der p 6 + H2O
Der p 6 + Der p 6 propeptide
pro-Der p 6 zymogen is recombinantly produced in Pichia pastoris, activation mechanism analysis by mite protease Der p 1, overview. The enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen. The N-terminal sequence of rDer p 6 is V35IGGDQ. The propeptide of proDer p 6 inhibits the proteolytic activity of protease Der p 6, but once cleaved, it is degraded by the protease
-
-
?
pro-Der p 9 + H2O
Der p 9 + Der p 9 propeptide
activation
-
-
?
pro-Der p 9 + H2O
Der p 9 + Der p 9 propeptide
activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen
-
-
?
CD23 + H2O
?
-
CD23 is a calcium-dependent type II integral membrane protein. CD23 from the surface of cultured human B cells is cleaved at two sites: Ser155-Ser156 and Glu298-Ser299 to produce a 17000 Da fragment containing the lectin domain and only part of the C-terminal tail. No such effect is demonstrable with mouse CD23
-
-
?
CD23 + H2O
?
-
cleaves CD23 from the surface of cultured human B cells. The cleavage of the receptor from the B cell sulface is associated with a parallel increase in soluble CD23
-
-
?
CD23 + H2O
?
-
Der p 1 in addition to being highly immunogenic may up-regulate IgE synthesis by virtue of its ability to cleave CD23
-
-
?
lung surfactant protein A + H2O
?
-
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
-
-
?
lung surfactant protein D + H2O
?
-
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
Der p 1 is the most immunodominant allergen involved in the expression of dust mite-specific immunoglobulin (Ig)E-mediated hypersensitivity. The proteolytic activity of Der p 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production
-
-
?
additional information
?
-
-
cysteine protease activity of Der p 1 enhances total IgE production, apart from increasing Der p 1-specific IgE. This allergen may play a central role in destabilizing the micro-environment within target tissues to one that is pro-allergic, and thus aid in the initiation and propagation of the allergic cascade
-
-
?
additional information
?
-
-
the efficient in vivo responses, including production of IgE and IgG against the highly purified rDer p 1, are dependent on the cysteine protease activity in mice. The three types of rDer p 1 differing in function or structure elicit distinctly different immune responses
-
-
?
additional information
?
-
-
the house dust mite allergen Der p 1 stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism
-
-
?
additional information
?
-
-
house dust mite major allergens Der p 1 and Der p 5 activate human airway-derived epithelial cells by protease-dependent and protease-independent mechanisms
-
-
?
additional information
?
-
Der p 7 binds a bacterially-derived lipid product, a common feature of some allergens, ligand binding analysis by NMR analysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-Der p 3 + H2O
Der p 3 + Der p 3 propeptide
activation
-
-
?
pro-Der p 6 + H2O
Der p 6 + Der p 6 propeptide
activation
-
-
?
pro-Der p 9 + H2O
Der p 9 + Der p 9 propeptide
activation
-
-
?
CD23 + H2O
?
-
Der p 1 in addition to being highly immunogenic may up-regulate IgE synthesis by virtue of its ability to cleave CD23
-
-
?
lung surfactant protein A + H2O
?
-
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
-
-
?
lung surfactant protein D + H2O
?
-
degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
-
-
?
additional information
?
-
-
Der p 1 is the most immunodominant allergen involved in the expression of dust mite-specific immunoglobulin (Ig)E-mediated hypersensitivity. The proteolytic activity of Der p 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production
-
-
?
additional information
?
-
-
cysteine protease activity of Der p 1 enhances total IgE production, apart from increasing Der p 1-specific IgE. This allergen may play a central role in destabilizing the micro-environment within target tissues to one that is pro-allergic, and thus aid in the initiation and propagation of the allergic cascade
-
-
?
additional information
?
-
-
the efficient in vivo responses, including production of IgE and IgG against the highly purified rDer p 1, are dependent on the cysteine protease activity in mice. The three types of rDer p 1 differing in function or structure elicit distinctly different immune responses
-
-
?
additional information
?
-
-
the house dust mite allergen Der p 1 stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
dithiothreitol dependent proteolytic activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a flexible metal binding site is present in pro-Der p 1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3S)-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxo-N-(4-sulfamoylbenzyl)pentanamide
-
(3S)-N-benzyl-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanamide
-
(3S)-N-[4-[(dimethylamino)methyl]benzyl]-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanamide
-
3-methyl-N-(naphthalen-1-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
3-methyl-N-(pyridin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-([2-oxo-2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)pentan-3-yl]-L-alaninamide
-
3-methyl-N-[(1-methylpiperidin-4-yl)carbonyl]-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
4-([[(3S)-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanoyl]amino]methyl)-N-methylbenzamide
-
Der p 1 propeptide
the propeptide of 80 amino acids plays an essential role in zymogen folding (as an intramolecular chaperone) and in the inhibition of its own enzymatic activity
-
N-(naphthalen-1-ylcarbonyl)-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(cyclopropylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-([4-[(dimethylamino)methyl]benzyl]amino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-amino-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[(1H-pyrazol-4-ylmethyl)amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[(4-sulfamoylbenzyl)amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[4-(trifluoromethyl)benzyl]amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1-(methylamino)-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-b,b-dimethyl-L-phenylalanyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1,2-dioxo-1-(pyrrolidin-1-yl)heptan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-1,2-dioxoheptan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4,4-dimethyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-norvalinamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-[[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-1-[[2-(4,4-dimethylpiperazin-4-ium-1-yl)-2-oxoethyl]amino]-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-2-oxo-1-(pyrrolidin-1-yl)heptan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-(tetrahydro-2H-pyran-4-ylamino)pentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-([2-oxo-2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)pentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[2-oxo-2-(piperidin-1-yl)ethyl]amino]pentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[(1-methylpiperidin-4-yl)amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[(2S)-1-(4-methylpiperazin-1-yl)-1-oxopropan-2-yl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(morpholin-4-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-benzoyl-L-valyl-N-[(3S)-1-(benzoyloxy)-2-oxoheptan-3-yl]-L-alaninamide
irreversible inhibitor
N-[(1,1-dimethylpiperidinium-4-yl)carbonyl]-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
N-[(1S)-2-[[(2S)-1-[[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]amino]-1-oxopropan-2-yl]amino]-2-oxo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]benzamide
-
N-[(3,5-dimethyl-1H-pyrazol-4-yl)carbonyl]-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
-
Der p 1 allergen
-
ADZ 50,000, irreversible inactivation, active site titrant
-
Der p 1 prodomain
-
PP-02, recombinant, apparently competitive
-
Der p 1 propiece
-
potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction
-
PTL11028
-
a highly potent and specific inhibitor, being effective against both purified protease and Der p 1 within HDM extract
E-64
cysteine protease-specific inhibitor, 0.1 mM, complete inhibition
E-64
-
cysteine protease-specific inhibitor, complete inhibition
E-64
-
trans-epoxysuccinyl L-leucylamido (4-guanidine) butane, 0.01 mM, complete inhibition of interleukine production in A549 epithelial cells
additional information
inhibition efficiency in vivo, overview
-
additional information
-
Der f1 from Dermatophagoides farinae is highly susceptible, Der p 1 from Dermatophagoides pteronyssinus is not affected by chestnut cystatin. Der p 1 inactivates chestnut chystatin by a specific proteolytic cleavage between Gly6 and Val7
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine
-
the enzyme is completely dependent on preactivation with cysteine
additional information
-
Der p 1 dose-dependently increase the production of IL-6 and IL-8, can be blocked by heat treatment and cell desquamation
-
additional information
-
Der p 1 induce the release of IL-1beta, IL-6, IL-10, tumor necrosis factor-alpha and granulocyte macrophage colony-stimulating factor from eosinophils, surface expression of CD18 and ICAM-1, can activate NK-KB, AP-1 activity and p38 MAPK in BEAS-2B cells and eosinophils alone and in co-culture
-
additional information
-
Der p 1 induces chemokine production (CXCL8, CXCL10, CCL2, CCL5 and CCL20) by bronchial epithelial cells BEAS-2B and BECs from nonatopic controls through protease-activated receptor (PAR)-2 cleavage
-
additional information
-
Der p 1 stimulates the expression of Interleukin-8 in human pulmonary epithelial cells via the ERK1/2 signaling pathway
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
2-aminobenzoic acid-Val-Ala-Nle-Ser-(3-nitro)-tyrosinyl-aspartamide
-
pH 8.3
0.0154
(2-aminobenzoyl)-Val-Ala-norLeu-Ser-Tyr(3-NO2)-Asp
-
Der p 1 purified from Dermatophagoides pteronyssinus
14.4
(2-aminobenzoyl)-Val-Ala-norLeu-Ser-Tyr(3-NO2)-Asp
-
recombinant Der p 1, expressed in Pichia pastoris
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
2-aminobenzoic acid-Val-Ala-Nle-Ser-(3-nitro)-tyrosinyl-aspartamide
-
pH 8.3
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000003
(3S)-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxo-N-(4-sulfamoylbenzyl)pentanamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000007
(3S)-N-benzyl-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000004
(3S)-N-[4-[(dimethylamino)methyl]benzyl]-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.00002
3-methyl-N-(naphthalen-1-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000013
3-methyl-N-(pyridin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000018
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000013
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000003
3-methyl-N-(quinolin-4-ylcarbonyl)-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-([2-oxo-2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.00019
3-methyl-N-[(1-methylpiperidin-4-yl)carbonyl]-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000004
4-([[(3S)-3-([N-[(2S)-3,3-dimethyl-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)butanoyl]-L-alanyl]amino)-4-methyl-2-oxopentanoyl]amino]methyl)-N-methylbenzamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.00002
N-(naphthalen-1-ylcarbonyl)-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000009
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000014
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000017
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-(cyclopropylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000008
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-([4-[(dimethylamino)methyl]benzyl]amino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000006
N-benzoyl-3-methyl-L-valyl-N-[(3S)-1-amino-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000011
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[(1H-pyrazol-4-ylmethyl)amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000006
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[(4-sulfamoylbenzyl)amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000117
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[(1R)-1-phenylethyl]amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000017
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[(1S)-1-phenylethyl]amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000047
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[4-(trifluoromethyl)benzyl]amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000024
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1-(methylamino)-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000014
N-benzoyl-3-methyl-L-valyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000042
N-benzoyl-b,b-dimethyl-L-phenylalanyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000997
N-benzoyl-L-phenylalanyl-N-[(3S)-1,2-dioxo-1-(pyrrolidin-1-yl)heptan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000012
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000008 - 0.000017
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-1,2-dioxoheptan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.00917
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4,4-dimethyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000018
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000164
N-benzoyl-L-phenylalanyl-N-[(3S)-1-(cyclohexylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-norvalinamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000006
N-benzoyl-L-phenylalanyl-N-[(3S)-1-[[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000017
N-benzoyl-L-phenylalanyl-N-[(3S)-1-[[2-(4,4-dimethylpiperazin-4-ium-1-yl)-2-oxoethyl]amino]-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000065
N-benzoyl-L-phenylalanyl-N-[(3S)-2-oxo-1-(pyrrolidin-1-yl)heptan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000055
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-(tetrahydro-2H-pyran-4-ylamino)pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000004
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-([2-oxo-2-[4-(propan-2-yl)piperazin-1-yl]ethyl]amino)pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000014
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1,2-dioxo-1-[[2-oxo-2-(piperidin-1-yl)ethyl]amino]pentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000115
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[(1-methylpiperidin-4-yl)amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.00001
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[(2S)-1-(4-methylpiperazin-1-yl)-1-oxopropan-2-yl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000014
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000009
N-benzoyl-L-phenylalanyl-N-[(3S)-4-methyl-1-[[2-(morpholin-4-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000006
N-[(1,1-dimethylpiperidinium-4-yl)carbonyl]-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000005
N-[(1S)-2-[[(2S)-1-[[(3S)-4-methyl-1-[[2-(4-methylpiperazin-1-yl)-2-oxoethyl]amino]-1,2-dioxopentan-3-yl]amino]-1-oxopropan-2-yl]amino]-2-oxo-1-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]benzamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000067
N-[(3,5-dimethyl-1H-pyrazol-4-yl)carbonyl]-3-methyl-L-valyl-N-[(3S)-1-(benzylamino)-4-methyl-1,2-dioxopentan-3-yl]-L-alaninamide
Dermatophagoides pteronyssinus
pH and temperature not specified in the publication
0.000051
Der p 1 prodomain
Dermatophagoides pteronyssinus
-
recombinant Der p 1, expressed in Pichia pastoris
-
0.0000569
Der p 1 prodomain
Dermatophagoides pteronyssinus
-
Der p 1 purified from Dermatophagoides pteronyssinus
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
physiological function
additional information
evolution
enzyme Der p 1 is a cysteine protease from the papain family
evolution
mannosylation is a unique feature of the allergens within the cysteine protease family of enzymes, e.g. Der 1 p, papain, and bromelain, while non-allergens of the family, e.g. calpain, and cysteine protease B do not show mannosylation in their carbohydrate patterns, staphopain B is also a cysteine protease protein, like Der p 1, but is an amannosylated antigen
physiological function
sinonasal epithelial exposure to house dust mite antigen enzyme Der p 1 decreases expression of tight junction proteins, representing a potential mechanism for increased permeability and presentation of antigens across the sinonasal epithelial layer. Enzyme Der p 1-exposed human sinonasal cells show a marked decrease in transepithelial resistance when compared to control cells, with decreased expression of tight junction proteins claudin-1 and junction adhesion molecule-A (JAM-A). Epithelial permeability is highly dependent upon the integrity of tight junctions, cell-cell adhesion complexes located at the apical aspect of the lateral membrane of polarized epithelial cells. Importance of Der p 1 cysteine protease activity directed against airway epithelia
physiological function
stimulation with natural Der p 1 causes an increase in thymic stromal lymphopoietin, TSLP, cytokine secretion by human lung epithelia in a carbohydrate-dependent manner. TSLP may drive denditic cell maturation in support of allergic hypersensitivity reactions
physiological function
the enzyme is 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. 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
physiological function
Der p 7 elicits strong IgE antibody and T-cell responses in mite allergic patients. Sensitization to house dust mite allergens is strongly correlated with asthma. The allergen function may contribute to allergenicity, e.g. the protease activity of Group 1 mite allergens, and the interaction with the innate immune system by Group 2 mite allergens
physiological function
the isozymes have allergenic potential in humans
physiological function
high enzyme concentration in mites faecal pellets can be airborne and, when inhaled, can cause perennial rhinitis and bronchial asthma in humans
additional information
activation mechanism analysis of the two other serine proteases, Der p 6 (chymotrypsin-like) and Der p 9 (collagenase)zymogen by mite protease Der p 1, overview
additional information
-
activation mechanism analysis of the two other serine proteases, Der p 6 (chymotrypsin-like) and Der p 9 (collagenase)zymogen by mite protease Der p 1, overview
additional information
the enzyme is a group 1 mite allergen
additional information
the enzyme is bound by the mannose receptor of dendritic cells, the recombinant enzyme binds stronger due to its higher degree of mannans compared to the native enzyme
additional information
the Group 7 as well as the Group 2 mite allergens are structurally similar to different proteins in the TLR pathway
additional information
binding properties of in tobacco plant-produced I-rDer p 1 versus the IgE of patients sera are comparable to those obtained on Der p 1 preparation immobilized on a microarray
additional information
-
binding properties of in tobacco plant-produced I-rDer p 1 versus the IgE of patients sera are comparable to those obtained on Der p 1 preparation immobilized on a microarray
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PEPT1_DERPT
320
0
36104
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000 - 18000
-
recombinant form without N-glycosylation, gel filtration
22200
x * 22200, about, mature Der p 7, sequence calculation, x * 24000-31000, SDS-PAGE
24000
-
x * 24000, mature mutant enzyme N52Q, SDS-PAGE under non-reducing conditions
25000
35000
-
x * 35000, recombinant ProDer p1 (Escherichia coli), SDS-PAGE
36000 - 60000
-
smear from 36 to 60 kDa, SDS-PAGE, recombinant Der p 1, expressed in Pichia pastoris
55000
-
average molecular weight, gel filtration, recombinant Der p 1, expressed in Pichia pastoris
additional information
-
recombinant Der p 1 and Der p 1 purified from Dermatophagoides pteronyssinus show differences in glycosylation
25000
-
gel filtration, Der p 1 purified from Dermatophagoides pteronyssinus
25000
x * 25000, about, recombinant I-Der p 1, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
Der p 7 has an elongated structure with two 4-stranded anti-parallel beta-sheets which wrap around a long C-terminal helix, NMR analysis of His-tagged Der p 7, overview
?
-
x * 24000, mature mutant enzyme N52Q, SDS-PAGE under non-reducing conditions
?
-
x * 40000-50000, mature mutant enzyme N52Q, SDS-PAGE under non-reducing conditions
?
-
x * 35000-45000, mature wild-type enzyme, SDS-PAGE under non-reducing conditions
?
-
x * 35000-45000, mature wild-type enzyme under reducing conditions
?
-
x * 35000, recombinant ProDer p1 (Escherichia coli), SDS-PAGE
?
x * 22200, about, mature Der p 7, sequence calculation, x * 24000-31000, SDS-PAGE
?
x * 25000, about, recombinant I-Der p 1, sequence calculation
monomer
-
crystal structure: analysis of the accessible surface area upon dimerization, dimer corresponds most probably to the inactive form
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
analysis of the glycosylation pattern and comparison to other allergens, mannosylation appears to be a dominant feature among allergens, overview. The main dominant sugars on these allergens are 1-2, 1-3 and 1-6 mannose, the sugar part of the enzyme is recognized by lectins from Datura stramonium lectin, Arachis hypogaea, and Sambucus nigra. Sodium periodate deglycosylation of natural and recombinant enzyme Der p 1 resulting in a significant decrease in the uptake of both Der p 1 preparations into dendritic cells. The recombinant enzyme shows a higher degree of mannans compared to the native enzyme
proteolytic modification
the Der p 1 enzyme propeptide of 80 amino acids plays an essential role in zymogen folding as an intramolecular chaperone and in the inhibition of its own enzymatic activity
glycoprotein
proteolytic modification
glycoprotein
-
N-glycosylation of the prosequences decelerated the maturation. Systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen
glycoprotein
different levels of glycosylation or isozymes
proteolytic modification
-
contribution of the N-terminal region of the Der p 1 prosequence including the N-glycosylation site, Asn(-65), on effective inhibition of proteolytic activity in pro-Der p 1
proteolytic modification
-
the Der p 1 propiece is a potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4°C, 45% monomethyl polyethylene glycole 5000 or 2000 in 50 mM sodium acetate (pH 5.5), 1.9 A resolution, typical papain-family fold, exhibits a magnesium binding site
recombinant Der p 7-MBP fusion protein, mixing of 0.001 ml of 27 mg/mL protein in 25 mM HEPES, pH 7.4, 75 mM NaCl, and 5 mM maltose, with 00.001 ml of reservoir solution containing 42.5 mM Tris pH 8.5, 12.75% PEG 4000, 85 mM lithium sulfate, and 7.5% glycerol, 4°C, 1 week, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C132V
site-directed mutagenesis, Der p 1 catalytic site mutant
N52Q
additional information
N52Q
mutant with disrupted N-glycosylation motif in the prodomain
N52Q
-
mutant with disrupted N-glycosylation motif in the prodomain, decreases the productivity and accelerates the maturation
N52Q
-
mutant with disrupted N-glycosylation motif in the prodomain, lower productivity
N52Q
-
molecular weight identical with that of natural allergen
additional information
construction of a chimeric allergen R8, derived from the major allergen group 1 of house dust mites species, Dermatophagoides farinae and Dermatophagoides pteronyssinus
additional information
-
hybrid molecules from parts of Der p 1 and Der p2 are constructed
additional information
development of chimeras assembling Der p 1 and Der p 2 allergens. Mutations in the Der p 1 catalytic site are also engineered
additional information
-
development of chimeras assembling Der p 1 and Der p 2 allergens. Mutations in the Der p 1 catalytic site are also engineered
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged chimeric allergen R8 from Nicotiana benthamiana leaves by affinity chromatography to homogeneity under denaturing conditions
ammonium sulfate precipitation, gel filtration, ion exchange chromatography
-
culture supernatants recovered, buffer exchange by gel filtration, equilibration with 100 mM sodium acetate buffer (pH 4)
-
dialysis, cationic exchange on SP-Sepharose, recombinant Der p 1 dialysis, benzamidine column, dialysis
immunoaffinity chromatography using immobilized 4C1 anti-Der p 1 monoclonal antibody
-
proform secreted in Pichia pastoris culture supernatant and converted into their prosequence-removed mature form, anion exchange column and gel filtration
-
recombinant Der p 7-MBP fusion protein Der p 7 from Escherichia coli Rosetta2(DE3) pLacI cells by amylose affinity chromatography and gel filtration. Recombinant His6-tagged Der p 7 from Escherichia coli Rosetta2(DE3) pLacI cells by alternating nickel affinity and anion exchange chromatography
recombinant His-tagged fusion proteins by nickel affinity chromatography using a His-Trap column under denaturing conditions with 20 m M sodium phosphate, pH 7.0, 0.5 M NaCl, 0.05% Tween 20, 8 M urea, 1 mM DTT, 0.03 M imidazole as binding buffer, and 20 mM sodium phosphate, pH 7.8, 0.05% Tween 20, 8 M urea, 1 mM DTT, 1 M imidazole as elution buffer
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of C-terminally His6-tagged chimeric allergen R8, derived from the major allergen group 1 of house dust mites species, Dermatophagoides farinae and Dermatophagoides pteronyssinus, in leaves of Nicotiana benthamiana via transfection with Agrobacterium tumefaciens strain GV3101
Der p 1.0124 (according to the IUIS-WHO Allergen Nomenclature Subcommittee)
-
expression and maturation of prepro-Der p 1 and its mutants in Pichia pastoris. Maturation systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen
-
expression of Der p 7-MBP fusion protein and His6-tagged Der p 7 in Escherichia coli Rosetta2(DE3) pLacI cells
expression of His-tagged fusion proteins encompassing Der p 2 with either mature or proDer p 1 in Escherichia coli strain BL21 (DE3) and Origami2 (DE3), or in Pichia pastoris strain GS115 or X33. Four fusion proteins are expressed in Escherichia coli as inclusion bodies, whereas only chimeras comprising proDer p 1 are obtained in yeast
I-Der p 1 gene, cDNA isolation, DNA and amino acid sequence determination and analysis, detection of 11 polymorphisms to the sequence of peptidase 1, DERP1, UniProt ID P08176, sequence comparison, PVX-mediated expression of immunologically active mature form I-rDer p 1 in Nicotiana benthamiana plants using a Agrobacterium tumefaciens strain GV3101-mediated transfection strategy, the recombinant enzyme comprises the N-terminal 222 amino acids which corresponds to the mature form of I-Der p 1 after proteolytic cleavage, the C-terminus is expressed as FLAG-tagged protein
preparation described elsewhere, proform secreted in Pichia pastoris culture supernatant and converted into their prosequence-removed mature form, recombinant protein exhibits cysteine protease activity but no serine protease activity
-
recombinant proforms secreted into culture supernatant of Pichia pastoris cells and converted into prosequence-removed mature form Der p 1-WT
-
the propiece of Der p 1 is PCR cloned and expressed in Escherichia coli
-
wild-type and mutant enzyme N52Q, expression in Pichia pastoris
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged chimeric allergen R8 from Nicotiana benthamiana leaves after purification by affinity chromatography under denaturing conditions, refolding by dialysis against decreasing concentrations of urea
recombinant His-tagged fusion proteins encompassing Der p 2 with either mature or proDer p 1 from Escherichia coli inclusion bodies with purification via denaturating nickel affinity chromatography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is a target for design and development of specific inhibitors for treatment of allergic asthma
diagnostics
medicine
diagnostics
-
maturation systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen
diagnostics
-
suspension-cultured BY-2 tobacco cells represent a low cost and environmentally safe expression system suitable to produce recombinant allergens from Dermatophagoides pteronyssinus under a form appropriate for diagnostic and therapeutic purposes
diagnostics
possible development of diagnostic allergy tests based on in planta produced allergens using Der 1 p as prototype
medicine
affects individuals with allergy, resulting in rhinitis, asthma and/or atopic dermatitits
medicine
-
allergen is associated with allergic diseases such as bronchial asthma, rhinitis, and atopic dermatitis
medicine
-
induces biological responses in a human airway-derived epithelial cell line
medicine
-
mimotopes identify conformational B-cell epitopes on the house dust mite allergen Der p 1. These mimotopes are potential candidates for the directed induction of blocking antibodies and epitope-specific immunotherapy of mite allergy
medicine
chimeras assembling Der p 1 and Der p 2 allergens are potential candidate vaccines against house dust mite allergy. But significant solubility and stability issues can limit the application of such chimeras for immunotherapy or diagnostic
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pernas, M.; Sanchez-Ramos, I.; Sanchez-Monge, R.; Lombardero, M.; Arteaga, C.; Castanera, P.; Salcedo, G.
Der p 1 and Der f 1, the highly related and major allergens from house dust mites, are differentially affected by a plant cystatin
Clin. Exp. Allergy
30
972-978
2000
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Takai, T.; Mineki, R.; Nakazawa, T.; Takaoka, M.; Yasueda, H.; Murayama, K.; Okumura, K.; Ogawa, H.
Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity
FEBS Lett.
531
265-272
2002
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Thomas, W.R.; Stewart, G.A.; Simpson, R.J.; Chua, K.Y.; Plozza, T.M.; Dilworth, R.J.; Nisbet, A.; Turner, K.J.
Cloning and expression of DNA coding for the major house dust mite allergen Der p 1 in Escherichia coli
Int. Arch. Allergy Appl. Immunol.
85
127-129
1988
Dermatophagoides pteronyssinus (P08176)
Gough, L.; Schulz, O.; Sewell, H.F.; Shakib, F.
The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response
J. Exp. Med.
190
1897-1902
1999
Dermatophagoides pteronyssinus
Schulz, O.; Sutton, B.J.; Beavil, R.L.; Shi, J.; Sewell, H.F.; Gould, H.J.; Laing, P.; Shakib, F.
Cleavage of the low-affinity receptor for human IgE (CD23) by a mite cysteine protease: nature of the cleaved fragment in relation to the structure and function of CD23
Eur. J. Immunol.
27
584-588
1997
Dermatophagoides pteronyssinus
Schulz, O.; Laing, P.; Sewell, H.F.; Shakib, F.
Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23)
Eur. J. Immunol.
25
3191-3194
1995
Dermatophagoides pteronyssinus
Shakib, F.; Gough, L.
The proteolytic activity of Der p 1 selectively enhances IgE synthesis: a link between allergenicity and cysteine protease activity
Clin. Exp. Allergy
30
751-752
2000
Dermatophagoides pteronyssinus
John, R.J.; Rusznak, C.; Ramjee, M.; Lamont, A.G.; Abrahamson, M.; Hewitt, E.L.
Functional effects of the inhibition of the cysteine protease activity of the major house dust mite allergen Der p 1 by a novel peptide-based inhibitor
Clin. Exp. Allergy
30
784-793
2000
Dermatophagoides pteronyssinus
Takai, T.; Kato, T.; Sakata, Y.; Yasueda, H.; Izuhara, K.; Okumura, K.; Ogawa, H.
Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity
Biochem. Biophys. Res. Commun.
328
944-952
2005
Dermatophagoides pteronyssinus
Kauffman Henk , K.H.; Tamm Michae, T.M.; Timmerman J. Andre , T.J.; Borger Pete, B.P.
House dust mite major allergens Der p 1 and Der p 5 activate human airway-derived epithelial cells by protease-dependent and protease-independent mechanisms
Clin. Mol. Allergy
4
5-5
2006
Dermatophagoides pteronyssinus
Takai, T.; Kato, T.; Ota, M.; Yasueda, H.; Kuhara, T.; Okumura, K.; Ogawa, H.
Recombinant Der p 1 and Der f 1 with in vitro enzymatic activity to cleave human CD23, CD25 and alpha1-antitrypsin, and in vivo IgE-eliciting activity in mice
Int. Arch. Allergy Immunol.
137
194-200
2005
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Takai, T.; Mizuuchi, E.; Kikuchi, Y.; Nagamune, T.; Okumura, K.; Ogawa, H.
Glycosylation of recombinant proforms of major house dust mite allergens Der p 1 and Der f 1 decelerates the speed of maturation
Int. Arch. Allergy Immunol.
139
181-187
2006
Dermatophagoides pteronyssinus
Wong, C.K.; Li, M.L.; Wang, C.B.; Ip, W.K.; Tian, Y.P.; Lam, C.W.
House dust mite allergen Der p 1 elevates the release of inflammatory cytokines and expression of adhesion molecules in co-culture of human eosinophils and bronchial epithelial cells
Int. Immunol.
18
1327-1335
2006
Dermatophagoides pteronyssinus
Takai, T.; Kato, T.; Yasueda, H.; Okumura, K.; Ogawa, H.
Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: Major conformational IgE epitopes blocked by prodomains
J. Allergy Clin. Immunol.
115
555-563
2005
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Pichavant, M.; Charbonnier, A.; Taront, S.; Brichet, A.; Wallaert, B.; Pestel, J.; Tonnel, A.; Gosset, P.
Asthmatic bronchial epithelium activated by the proteolytic allergen Der p 1 increases selective dendritic cell recruitment
J. Allergy Clin. Immunol.
115
771-778
2005
Dermatophagoides pteronyssinus
de Halleux, S.; Stura, E.; VanderElst, L.; Carlier, V.; Jacquemin, M.; Saint-Remy, J.
Three-dimensional structure and IgE-binding properties of mature fully active Der p 1, a clinically relevant major allergen
J. Allergy Clin. Immunol.
117
571-576
2006
Dermatophagoides pteronyssinus, Dermatophagoides pteronyssinus (P08176)
Adam, E.; Hansen, K.K.; Astudillo, O.F.; Coulon, L.; Bex, F.; Duhant, X.; Jaumotte, E.; Hollenberg, M.D.; Jacquet, A.
The house dust mite allergen Der p 1, unlike Der p 3, stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism
J. Biol. Chem.
281
6910-6923
2006
Dermatophagoides pteronyssinus
Zhang, J.; Hamilton, J.M.; Garrod, D.R.; Robinson, C.
Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases
Allergy
62
1302-1309
2007
Dermatophagoides pteronyssinus
Meno Kar, M.K.; Thorsted Peter , T.P.; Ipsen Henri, I.H.; Kristensen Ol, K.O.; Larsen Jorgen , L.J.; Spangfort Michael , S.M.; Gajhede Michae, G.M.; Lund Kaar, L.K.
The metal binding site of the major house dust mite allergen Der p 1
J. Allergy Clin. Immunol.
118
971-971
2006
Dermatophagoides pteronyssinus (P08176)
Deb, R.; Shakib, F.; Reid, K.; Clark, H.
Major house dust mite allergens Dermatophagoides pteronyssinus 1 and Dermatophagoides farinae 1 degrade and inactivate lung surfactant proteins A and D
J. Biol. Chem.
282
36808-36819
2007
Dermatophagoides pteronyssinus
Kikuchi, Y.; Takai, T.; Kuhara, T.; Ota, M.; Kato, T.; Hatanaka, H.; Ichikawa, S.; Tokura, T.; Akiba, H.; Mitsuishi, K.; Ikeda, S.; Okumura, K.; Ogawa, H.
Crucial commitment of proteolytic activity of a purified recombinant major house dust mite allergen Der p1 to sensitization toward IgE and IgG responses
J. Immunol.
177
1609-1617
2006
Dermatophagoides pteronyssinus
Szalai, K.; Fuhrmann, J.; Pavkov, T.; Scheidl, M.; Wallmann, J.; Braemswig, K.H.; Vrtala, S.; Scheiner, O.; Keller, W.; Saint-Remy, J.M.; Neumann, D.; Pali-Schoell, I.; Jensen-Jarolim, E.
Mimotopes identify conformational B-cell epitopes on the two major house dust mite allergens Der p 1 and Der p 2
Mol. Immunol.
45
1308-1317
2008
Dermatophagoides pteronyssinus
Lienard, D.; Tran Dinh, O.; van Oort, E.; Van Overtvelt, L.; Bonneau, C.; Wambre, E.; Bardor, M.; Cosette, P.; Didier-Laurent, A.; de Borne, F.D.; Delon, R.; van Ree, R.; Moingeon, P.; Faye, L.; Gomord, V.
Suspension-cultured BY-2 tobacco cells produce and mature immunologically active house dust mite allergens
Plant Biotechnol. J.
5
93-108
2007
Dermatophagoides pteronyssinus
Zhang, J.; Saint-Remy, J.M.; Garrod, D.R.; Robinson, C.
Comparative enzymology of native and recombinant house dust mite allergen Der p 1
Allergy
64
469-477
2009
Dermatophagoides pteronyssinus
Walgraffe, D.; Matteotti, C.; El Bakkoury, M.; Garcia, L.; Marchand, C.; Bullens, D.; Vandenbranden, M.; Jacquet, A.
A hypoallergenic variant of Der p 1 as a candidate for mite allergy vaccines
J. Allergy Clin. Immunol.
123
1150-1156
2009
Dermatophagoides pteronyssinus
Maneechotesuwan, K.; Wamanuttajinda, V.; Kasetsinsombat, K.; Huabprasert, S.; Yaikwawong, M.; Barnes, P.J.; Wongkajornsilp, A.
Der p 1 suppresses indoleamine 2, 3-dioxygenase in dendritic cells from house dust mite-sensitive patients with asthma
J. Allergy Clin. Immunol.
123
239-248
2009
Dermatophagoides pteronyssinus
Chruszcz, M.; Chapman, M.D.; Vailes, L.D.; Stura, E.A.; Saint-Remy, J.M.; Minor, W.; Pomes, A.
Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding
J. Mol. Biol.
386
520-530
2009
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Spertini, F.; Berney, M.; Foradini, F.; Roulet, C.A.
Major mite allergen Der f 1 concentration is reduced in buildings with improved energy performance
Allergy
65
623-629
2010
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Asturias, J.A.; Ibarrola, I.; Arilla, M.C.; Vidal, C.; Ferrer, A.; Gamboa, P.M.; Vinuela, J.E.; Sanz, M.L.; Andreu, C.; Martinez, A.
Engineering of major house dust mite allergens Der p 1 and Der p 2 for allergen-specific immunotherapy
Clin. Exp. Allergy
39
1088-1098
2009
Dermatophagoides pteronyssinus
Horlock, C.; Shakib, F.; Jones, N.S.; Sewell, H.F.; Ghaemmaghami, A.M.
Differential protein expression by dendritic cells from atopic and non-atopic individuals after stimulation by the major house dust mite allergen Der p 1
Int. Arch. Allergy Immunol.
150
237-251
2009
Dermatophagoides pteronyssinus
Takai, T.; Kato, T.; Hatanaka, H.; Inui, K.; Nakazawa, T.; Ichikawa, S.; Mitsuishi, K.; Ogawa, H.; Okumura, K.
Modulation of allergenicity of major house dust mite allergens Der f 1 and Der p 1 by interaction with an endogenous ligand
J. Immunol.
183
7958-7965
2009
Dermatophagoides farinae, Dermatophagoides pteronyssinus
Bussieres, L.; Bordas-Le Floch, V.; Bulder, I.; Chabre, H.; Nony, E.; Lautrette, A.; Berrouet, C.; Nguefeu, Y.; Horiot, S.; Baron-Bodo, V.; Van Overtvelt, L.; De Conti, A.M.; Schlegel, A.; Maguet, N.; Mouz, N.; Lemoine, P.; Batard, T.; Moingeon, P.
Recombinant fusion proteins assembling Der p 1 and Der p 2 allergens from Dermatophagoides pteronyssinus
Int. Arch. Allergy Immunol.
153
141-151
2010
Dermatophagoides pteronyssinus (P49273), Dermatophagoides pteronyssinus
Mueller, G.A.; Edwards, L.L.; Aloor, J.J.; Fessler, M.B.; Glesner, J.; Pomes, A.; Chapman, M.D.; London, R.E.; Pedersen, L.C.
The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins
J. Allergy Clin. Immunol.
125
909-917.e4
2010
Dermatophagoides pteronyssinus (P49273)
Herman, J.; Thelen, N.; Smargiasso, N.; Mailleux, A.C.; Luxen, A.; Cloes, M.; De Pauw, E.; Chevigne, A.; Galleni, M.; Dumez, M.E.
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
Biochim. Biophys. Acta
1840
1117-1124
2014
Dermatophagoides pteronyssinus (P08176), Dermatophagoides pteronyssinus
Li, C.; Jiang, Y.; Guo, W.; Liu, Z.
Production of a chimeric allergen derived from the major allergen group 1 of house dust mite species in Nicotiana benthamiana
Hum. Immunol.
74
531-537
2013
Dermatophagoides pteronyssinus (P08176), Dermatophagoides farinae (Q58A71)
Henriquez, O.A.; Den Beste, K.; Hoddeson, E.K.; Parkos, C.A.; Nusrat, A.; Wise, S.K.
House dust mite allergen Der p 1 effects on sinonasal epithelial tight junctions
Int. Forum Allergy Rhinol.
3
630-635
2013
Dermatophagoides pteronyssinus (P08176)
Newton, G.K.; Perrior, T.R.; Jenkins, K.; Major, M.R.; Key, R.E.; Stewart, M.R.; Firth-Clark, S.; Lloyd, S.M.; Zhang, J.; Francis-Newton, N.J.; Richardson, J.P.; Chen, J.; Lai, P.; Garrod, D.R.; Robinson, C.
The discovery of potent, selective, and reversible inhibitors of the house dust mite peptidase allergen Der p 1: an innovative approach to the treatment of allergic asthma
J. Med. Chem.
57
9447-9462
2014
Dermatophagoides pteronyssinus (P08176)
Al-Ghouleh, A.; Johal, R.; Sharquie, I.; Emara, M.; Harrington, H.; Shakib, F.; Ghaemmaghami, A.
The glycosylation pattern of common allergens: The recognition and uptake of Der p 1 by epithelial and dendritic cells is carbohydrate dependent
PLoS ONE
7
e33929
2012
Dermatophagoides pteronyssinus (P08176)
Marconi, G.; Albertini, E.; Mari, A.; Palazzo, P.; Porceddu, A.; Raggi, L.; Bolis, L.; Lancioni, H.; Palomba, A.; Lucentini, L.; Lanfaloni, L.; Marcucci, F.; Falcinelli, M.; Panara, F.
In planta expression of a mature Der p 1 allergen isolated from an Italian strain of Dermatophagoides pteronyssinus
Transgenic Res.
21
523-535
2012
Dermatophagoides pteronyssinus (B5AYU7), Dermatophagoides pteronyssinus
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