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Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity
Author(s) -
Takai Toshiro,
Mineki Reiko,
Nakazawa Takuya,
Takaoka Masatoshi,
Yasueda Hiroshi,
Murayama Kimie,
Okumura Ko,
Ogawa Hideoki
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03534-2
Subject(s) - pichia pastoris , recombinant dna , chemistry , glycosylation , cysteine protease , cleavage (geology) , protease , biochemistry , microbiology and biotechnology , cysteine , biology , enzyme , paleontology , fracture (geology) , gene
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.