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

来源：

FEBS LETTERS | 2002年 / 531卷 / 02期

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

页码：265 / 272

页数：8

共 49 条

[1] ISOLATION OF CYSTEINE PROTEASE IN THE CRUDE MITE EXTRACT, DERMATOPHAGOIDES-FARINAE [J].