Abstract
Recombinant pro-Der p 1 expressed in yeast Pichia pastoris was convertible into the prosequence-removed mature Der p 1 with full activities of cysteine protease and IgE-binding with or without N-glycosylation of the mature sequence as well as pro-Der f 1. The active recombinant variants will be the basis for various future studies. The major N-terminus of pro-Der p 1 with low proteolytic activity was the putative signal-cleavage site, while that of pro-Der f 1 contained not only the equivalent site but also 21 residues downstream, and pro-Der f 1 retained significant activity. Contribution of the N-terminal region of the Der p 1 prosequence including an N-glycosylation motif on effective inhibition of proteolytic activity of pro-Der p 1 was suggested.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allergens / genetics
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Allergens / immunology
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Allergens / metabolism*
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Amino Acid Sequence
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Antigens, Dermatophagoides / genetics
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Antigens, Dermatophagoides / immunology
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Antigens, Dermatophagoides / metabolism*
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Arthropod Proteins
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Cloning, Molecular
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Cysteine Endopeptidases / metabolism
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Enzyme Inhibitors / pharmacology
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Immunoglobulin E / immunology
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Molecular Sequence Data
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Pichia / genetics
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Protein Precursors / genetics
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Protein Precursors / metabolism
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Recombinant Proteins / metabolism
Substances
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Allergens
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Antigens, Dermatophagoides
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Arthropod Proteins
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Enzyme Inhibitors
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Protein Precursors
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Recombinant Proteins
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Immunoglobulin E
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Cysteine Endopeptidases
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Dermatophagoides farinae antigen f 1
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Dermatophagoides pteronyssinus antigen p 1