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

FEBS Letters

Takaoka, Masatoshi³  Murayama, Kimie¹  Okumura, Ko⁴  Nakazawa, Takuya⁴  Ogawa, Hideoki⁴  Yasueda, Hiroshi²  Takai, Toshiro⁴  Mineki, Reiko¹ 

[1] Division of Biochemical Analysis, Central Laboratory of Medical Sciences, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan;Clinical Research Center, National Sagamihara Hospital, 18-1 Sakuradai, Sagamihara, Kanagawa 228-8522, Japan;Saitama Institute of Public Health, 639-1, Kamiokubo, Saitama 338-0824, Japan;Atopy (Allergy) Research Center, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan

关键词: Recombinant major house dust mite group 1 allergen;    Maturation;    Prosequence;    N-Glycosylation;    Cysteine protease;    IgE-binding;   

DOI  :  10.1016/S0014-5793(02)03534-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 motif on effective inhibition of proteolytic activity of pro-Der p 1 was suggested.

【 授权许可】

Unknown