Theileria annulata subtelomere-encoded variable secreted protein-TA05560 interacts with bovine RNA binding motif protein 39 (RBM39)

文献类型: 外文期刊

第一作者: Ma, Quanying

作者: Ma, Quanying;Teng, Guixiang;Wang, Xiaoqiang;Han, Yuan;Fu, Yong;Li, Zhi;Liu, Junlong

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关键词: Theileria annulata; Subtelomere-encoded variable secreted protein; Schizont stage; TaNM1 cells

期刊名称:ACTA TROPICA ( 影响因子:2.7; 五年影响因子:2.7 )

ISSN: 0001-706X

年卷期: 2024 年 252 卷

页码:

收录情况: SCI

摘要: Theileria annulata is the only eukaryotic pathogen able to transform bovine leukocytes, including B cells, macrophages and dendritic cells. T. annulata-transformed cells exhibit several cancer-like phenotypes, such as hyperproliferation, immortalization and dissemination. Although several parasite factors involved in bovine cell transformation have been explored, the roles of subtelomere-encoded variable secreted proteins (SVSPs) of the parasite in host-cell interactions are largely unknown. In the present study, the target molecule TA05560, a member of the SVSP multigene family of T. annulata, was identified at the mRNA level during different life cycles through a quantitative real -time PCR assay, and the subcellular distribution of TA05560 was examined via confocal microscopy. The results showed that the parasite molecule TA05560 was transcribed mainly in the schizont stage of T. annulata infection, and the protein was distributed in the nucleus and cytoplasm of the parasitized cells. The potential host cell proteins that interact with TA05560 were screened using the yeast twohybrid system, and the direct interaction between TA05560 and its prey protein, Bos taurus RNA binding motif protein 39 (RBM39) was further identified in HEK293T cells by using confocal microscopy, coimmunoprecipitation and bimolecular fluorescence complementation assays. Moreover, the interaction between TA05560 and its host protein was observed in T. annulata-infected cells via confocal microscopy. Therefore, our study is the first to show that the T. annulata-secreted TA05560 protein directly binds to both the exogenous and endogenous host cell molecule RBM39, laying the foundation for exploring host-parasite interactions and understanding the transformation mechanisms induced by T. annulata and other transforming parasites.

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