Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity

被引:45
作者
Takai, T
Mineki, R
Nakazawa, T
Takaoka, M
Yasueda, H
Murayama, K
Okumura, K
Ogawa, H
机构
[1] Juntendo Univ, Sch Med, Atopy Allergy Res Ctr, Bunkyo Ku, Tokyo 1138421, Japan
[2] Juntendo Univ, Sch Med, Div Biochem Analysis,Cent Lab Med Sci, Bunkyo Ku, Tokyo 1138421, Japan
[3] Saitama Inst Publ Hlth, Kamiokubo, Saitama 3380824, Japan
[4] Natl Sagamihara Hosp, Clin Res Ctr, Sagamihara, Kanagawa 2288522, Japan
[5] Juntendo Univ, Sch Med, Dept Immunol, Bunkyo Ku, Tokyo 1138421, Japan
[6] Juntendo Univ, Sch Med, Dept Dermatol, Bunkyo Ku, Tokyo 1138421, Japan
关键词
recombinant major house dust mite group 1; allergen; maturation; prosequence; N-glycosylation; cysteine protease; IgE-binding;
D O I
10.1016/S0014-5793(02)03534-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 motion effective inhibition of proteolytic activity of pro-Der p 1 was suggested. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:265 / 272
页数:8
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