Hemolytic activity and developmental expression of pore-forming peptide, clonorin

被引:29
作者
Lee, JY
Cho, PY
Kim, TY
Kang, SY
Song, KY
Hong, SJ [1 ]
机构
[1] Chung Ang Univ, Coll Med, Dept Parasitol, Seoul 156756, South Korea
[2] Chung Ang Univ, Coll Med, Dept Pathol, Seoul 156756, South Korea
基金
新加坡国家研究基金会;
关键词
Clonorchis sinensis; pore-forming peptide; intestine; stage-specific; hemolytic; clonorin;
D O I
10.1016/S0006-291X(02)02062-4
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
Peptides pore-forming in cell membrane have been identified from a wide range of animals. A putative pore-forming peptide deduced from a cDNA clone of Clonorchis sinensis (clonorin) was predicted to consist of four amphipathic alpha-helices. Clonorin contained six invariably conserved cysteine residues, identified to form three disulfide bonds. These predicted structural features are highly homologous with pore-forming peptides, the amoebapores. Recombinant clonorin showed hemolytic activity toward rabbit erythrocytes. The hemolytic activity of C. sinensis extract increased dose-dependently and was inhibited by anti-clonorin immune sera. The clonorin was expressed developmentally in juvenile and adult flukes and localized in the intestinal epithelium of adult flukes. It is proposed that, through lysing host cellular components, clonorin could enhance proteolytic digestion in the intestine of C. sinensis. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:1238 / 1244
页数:7
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