Identification of a piroplasm protein of Theileria orientalis that binds to bovine erythrocyte band 3
Identification of a piroplasm protein of Theileria orientalis that binds to bovine erythrocyte band 3
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DOI：
10.1016/j.molbiopara.2004.05.012
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发表时间：
2004-10-01
影响因子：
1.5
通讯作者：
Sugimoto, C
中科院分区：
文献类型：
--
作者：
Kim, JY;Yokoyama, N;Sugimoto, C
东方泰勒虫感染牛并引起各种疾病症状，包括贫血和黄疸。红细胞阶段是这些症状的原因，但这些阶段涉及的分子事件尚未完全阐明。在这项研究中，我们确定了东方锥虫的cDNA编码的多肽相关的身份，微小泰勒虫的微管蛋白。通过间接荧光抗体试验分析其重组产物（ToMRP），发现其特异性表达于侵入后的早期红细胞阶段。这种表达在红细胞内发育的中间阶段消失。然后，在寄生虫通过二分裂分裂成二分体或四分体形式之后以及这些形式从宿主红细胞释放之前的晚期阶段，其表达再次出现。体外红细胞结合试验表明，ToMRP与红细胞膜的Triton X不溶性部分，但不与完整的红细胞。共沉淀和Western印迹分析表明，ToMRP结合带3，牛红细胞的膜组件。这些观察结果表明，ToMRP可能参与寄生虫的出口和/或侵入宿主红细胞通过与红细胞的膜骨架中的蛋白质相互作用，从而改变细胞的结构和功能。(C)2004 Elsevier B. V.保留所有权利。
Theileria orientalis infects cattle and causes various disease symptoms, including anaemia and icterus. The erythrocytic stages are responsible for these symptoms but the molecular events involved in these stages have not yet been fully elucidated. In this study, we identified a T orientalis cDNA that encodes a polypeptide related to identity to the microneme-rhoptry protein of Theileria parva. Analysis of its recombinant product (ToMRP) by indirect fluorescent-antibody test revealed that it is specifically expressed at the early erythrocytic stage after invasion. This expression disappears during the intermediate stages of intra-erythrocytic development. Its expression then reappears at the late stages after the parasite has divided by binary fission into diad or tetrad forms and before these forms are released from the host erythrocyte. In vitro erythrocyte binding assays showed that ToMRP associates with the Triton X-insoluble fraction of erythrocytes membrane but not with intact erythrocytes. Cosedimentation and Western blot analyses revealed that ToMRP binds to band 3, a membrane component of bovine erythrocytes. These observations suggest that ToMRP may be involved in the parasite's egress from and/or invasion into the host erythrocytes by interacting with a protein in the membrane skeleton of the erythrocyte and thereby modifying the structure and function of the cell. (C) 2004 Elsevier B.V. All rights reserved.