Identification and characterization of functional Smad8 and Smad4 homologues from Echinococcus granulosus
Identification and characterization of functional Smad8 and Smad4 homologues from Echinococcus granulosus
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DOI：
10.1007/s00436-014-4040-4
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发表时间：
2014-07
影响因子：
2
通讯作者：
Chuanshan Zhang;Limin Wang;Hui Wang;Hongwei Pu;Le Yang;Jing Li;Junhua Wang;G. Lü;Xiaomei Lu;Wenbao Zhang;D. Vuitton;H. Wen;R. Lin
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文献类型：
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作者：
Chuanshan Zhang;Limin Wang;Hui Wang;Hongwei Pu;Le Yang;Jing Li;Junhua Wang;G. Lü;Xiaomei Lu;Wenbao Zhang;D. Vuitton;H. Wen;R. Lin
Smad家族蛋白是转化生长因子-β超家族的重要细胞介质。在本研究中，我们从囊型包虫病(CE)的病原体细粒棘球绦虫中鉴定了Smad8和Smad4同源蛋白的两个成员，Smad8和Smad4同源物(分别称为EgSmadE和EgSmadD)。系统发育分析表明，EgSmadE属于R-Smad亚家族的Smad1、5和8亚组，EgSmadD属于Co-Smad家族。此外，EgSmadE和EgSmadD与E的EmSmadE和EmSmadD有很高的同源性。多房肌分别为。EgSmadE和EgSmadD在幼虫期共表达，在激活的原头节中转录水平最高，其编码蛋白共定位于寄生虫的皮下层和被皮层。酵母双杂交和下拉分析表明，EgSmadE与EgSmadD呈正相互作用。此外，体外培养的Mv1Lu细胞(水貂肺上皮细胞)经人转化生长因子-β-1或人骨形成蛋白2处理后，其胞核内可见EgSmadE的表达，表明EgSmadE可转位至胞核。我们的研究表明，EgSmadE和EgSmadD可能参与了包虫病的生长、发育和寄生虫-宿主相互作用等关键生物学过程。
Smad family proteins are essential cellular mediators of the transforming growth factor-β superfamily. In the present study, we identified two members of the Smad proteins, Smad8 and Smad4 homologues (termed as EgSmadE and EgSmadD, respectively), fromEchinococcus granulosus, the causative agent of cystic echinococcosis (CE). Phylogenetic analysis placed EgSmadE in the Smad1, 5, and 8 subgroup of the R-Smad sub-family and EgSmadD in the Co-Smad family. Furthermore, EgSmadE and EgSmadD attained a high homology to EmSmadE and EmSmadD ofE. multilocularis, respectively. Both EgSmadE and EgSmadD were co-expressed in the larval stages and exhibited the highest transcript levels in activated protoscoleces, and their encoded proteins were co-localized in the sub-tegumental and tegumental layer of the parasite. As shown by yeast two-hybrid and pull-down analysis, EgSmadE displayed a positive binding interaction with EgSmadD. In addition, EgSmadE localized in the nuclei of Mv1Lu cells (mink lung epithelial cells) upon treatment with human TGF-β1 or human BMP2, indicating that EgSmadE is capable of being translocated into nucleus, in vitro. Our study suggests that EgSmadE and EgSmadD may take part in critical biological processes, including echinococcal growth, development, and parasite-host interaction.