14-3-3 proteins in Schistosoma mansoni;: identification of a second epsilon isoform
14-3-3 proteins in Schistosoma mansoni;: identification of a second epsilon isoform
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DOI：
10.1016/s0020-7519(01)00323-x
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发表时间：
2002-06-01
影响因子：
4
通讯作者：
Pearce, EJ
中科院分区：
文献类型：
--
作者：
McGonigle, S;Loschiavo, M;Pearce, EJ
曼氏血吸虫14-3-3蛋白家族的一个新成员已被鉴定。序列分析表明，该蛋白是日本血吸虫14-3- 3A的直系同源物，属于A亚群。由于我们以前在S. mansoni，我们将原始蛋白质命名为14-3- 3 β-1，将第二种蛋白质命名为14-3- 3 β-2。曼氏血吸虫编码至少四种不同的14-3-3同种型：两种Zeta蛋白和14-3-3蛋白1和蛋白2，它们是zeta样同种型。系统发育分析表明，早期的分歧的p14 - 3 - 3异构体，和p14 -3-3蛋白是最古老的非p14 -3-3蛋白尚未确定。曼氏血吸虫14-3- 3 α-1、14-3- 3 β-2和蛋白1以类似的方式在阶段特异性表达，在尾蚴和童虫中不存在，而在肺期和成年雄性和雌性蠕虫中丰富。在检查的任何生命周期阶段均未检测到蛋白2转录物。所有三种检测到的14-3-3同种型在感染期间引起免疫应答，其中最大的应答针对蛋白1。与S. mansoni受体激酶-1（SmRK 1）和人Raf激酶的结果显示，三种14-3-3同种型表现出对靶蛋白结合的偏好。虽然所有三种亚型都与两种靶点结合，但14-3-3蛋白1与Raf的相互作用最强，而14-3- 3 - 3 -1亚型优先结合SmRK 1。这些结果表明，个别14-3-3蛋白可能已经进化到发挥异构体特异性的作用，在S。在其宿主体内的曼森氏菌(C)2002年澳大利亚寄生虫学会由Elsevier Science Ltd.出版，版权所有。
A now member of the 14-3-3 protein family in Schistosoma mansoni has been identified. Sequence analysis demonstrated that this protein is a member of the epsilon sub-group and is the orthologue of Schistosoma japonicum 14-3-3epsilon. Since we had previously identified a 14-3-3epsilon protein from S. mansoni, we termed the original protein 14-3-3epsilon-1 and this second epsilon protein 14-3-3epsilon-2. Schistosoma mansoni encodes at least four different 14-3-3 isoforms: the two epsilon proteins and 14-3-3 protein 1 and protein 2, which are zeta-like isoforms. Phylogenetic analysis demonstrated the early divergence of the epsilon isoforms, and that schistosome proteins 1 and 2 are among the oldest non-epsilon 14-3-3 proteins yet identified. Schistosoma mansoni 14-3-3epsilon-1, 14-3-3epsilon-2, and protein 1 are stage specifically expressed in a similar manner, being absent in cercariae and schistosomula, and abundant in lung stage and adult male and female worms. Protein 2 transcript was not detected at any of the life cycle stages examined. All three detected 14-3-3 isoforms elicit an immune response during infection, with the greatest response directed against protein 1. Binding studies with S. mansoni receptor kinase-1 (SmRK1) and human Raf kinase revealed that the three 14-3-3 isoforms exhibit a preference for target protein binding. Although all three isoforms do bind to both targets, 14-3-3 protein 1 interacts most strongly with Raf, whereas the 14-3-3epsilon-1 isoform binds SmRK1 preferentially. These results suggest that the individual 14-3-3 proteins may have evolved to play isoform-specific roles in the development and survival of S. mansoni within its host. (C) 2002 Australian Society for Parasitology Inc. Published by Elsevier Science Ltd. All rights reserved.