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中国肝吸虫 Clonorchis sinensis 的一种 EF 手型 Ca(2+)-结合蛋白。

An EF-handed Ca(2+)-binding protein of Chinese liver fluke Clonorchis sinensis.

机构信息

Department of Environmental Medical Biology and Institute of Tropical Medicine, Yonsei University College of Medicine, Seoul, 120-752, South Korea.

出版信息

Parasitol Res. 2013 Dec;112(12):4121-8. doi: 10.1007/s00436-013-3603-0. Epub 2013 Sep 10.

Abstract

A cDNA clone encoding 8 kDa protein was retrieved from an EST pool of Chinese liver fluke Clonorchis sinensis. A deduced polypeptide of the cDNA clone was similar to 8 kDa Ca(2+)-binding proteins from other parasitic trematodes, and, thus, named as CsCa8, containing two EF-hand Ca(2+)-binding sites. Homology models predicted CsCa8 to be a single globular structure having four helices and molecular folds similar to Ca(2+)-binding state of other small Ca(2+)-binding proteins. Recombinant CsCa8 protein showed specific Ca(2+)-binding affinity and shifting in native gel mobility assay. Mouse immune sera raised against recombinant CsCa8 protein recognized native CsCa8 from adult C. sinensis worm extract. CsCa8 was localized in oral and ventral suckers, vitelline follicles and subtegumental tissues. These findings suggest that CsCa8 might be involved in cellular Ca(2+) signal transduction for muscle contraction and egg production.

摘要

从中华肝吸虫 Clonorchis sinensis 的 EST 池中检索到编码 8 kDa 蛋白的 cDNA 克隆。该 cDNA 克隆的推导多肽与来自其他寄生吸虫的 8 kDa Ca(2+)结合蛋白相似,因此命名为 CsCa8,含有两个 EF 手 Ca(2+)结合位点。同源性模型预测 CsCa8 为具有四个螺旋和分子折叠的单个球形结构,类似于其他小 Ca(2+)结合蛋白的 Ca(2+)结合状态。重组 CsCa8 蛋白表现出特异性的 Ca(2+)结合亲和力,并在天然凝胶迁移分析中发生迁移。针对重组 CsCa8 蛋白产生的小鼠免疫血清识别来自成年中华肝吸虫虫体提取物的天然 CsCa8。CsCa8 定位于口吸盘和腹吸盘、卵黄滤泡和皮下组织中。这些发现表明,CsCa8 可能参与肌肉收缩和产卵的细胞 Ca(2+)信号转导。

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