Literature summary for 3.4.22.65 extracted from

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 (2010), Int. Arch. Allergy Immunol., 153, 141-151.

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Application

Application	Comment	Organism
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	Dermatophagoides pteronyssinus

Cloned(Commentary)

Cloned (Comment)	Organism
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	Dermatophagoides pteronyssinus

Protein Variants

Protein Variants	Comment	Organism
C132V	site-directed mutagenesis, Der p 1 catalytic site mutant	Dermatophagoides pteronyssinus
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	Dermatophagoides pteronyssinus

Organism

Organism	UniProt	Comment	Textmining
Dermatophagoides pteronyssinus	P49273	-	-

Purification (Commentary)

Purification (Comment)	Organism
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	Dermatophagoides pteronyssinus

Renatured (Commentary)

Renatured (Comment)	Organism
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	Dermatophagoides pteronyssinus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Z-Phe-Arg-4-methylcoumarin 7-amide + H2O	-	Dermatophagoides pteronyssinus	Z-Phe-Arg + 7-amino-4-methylcoumarin	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Dermatophagoides pteronyssinus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Dermatophagoides pteronyssinus

General Information

General Information	Comment	Organism
physiological function	the isozymes have allergenic potential in humans	Dermatophagoides pteronyssinus

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Release 2023.1 (January 2023)