Laboratórios de Protozoologia e de Bioinformática, Departamento de Microbiologia, Imunologia e Parasitologia, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, Florianópolis, SC, Brasil.
Mem Inst Oswaldo Cruz. 2012 Sep;107(6):713-9. doi: 10.1590/s0074-02762012000600002.
Protein tyrosine phosphatases (PTPs) play an essential role in the regulation of cell differentiation in pathogenic trypanosomatids. In this study, we describe a PTP expressed by the non-pathogenic protozoan Trypanosoma rangeli (TrPTP2). The gene for this PTP is orthologous to the T. brucei TbPTP1 and Trypanosoma cruzi (TcPTP2) genes. Cloning and expression of the TrPTP2 and TcPTP2 proteins allowed anti-PTP2 monoclonal antibodies to be generated in BALB/c mice. When expressed by T. rangeli epimastigotes and trypomastigotes, native TrPTP2 is detected as a ~65 kDa protein associated with the parasite's flagellum. Given that the flagellum is an important structure for cell differentiation in trypanosomatids, the presence of a protein responsible for tyrosine dephosphorylation in the T. rangeli flagellum could represent an interesting mechanism of regulation in this structure.
蛋白酪氨酸磷酸酶（PTPs）在致病性原生动物细胞分化的调控中起着至关重要的作用。在这项研究中，我们描述了一种由非致病性原生动物锥虫（Trypanosoma rangeli）表达的 PTP（TrPTP2）。该 PTP 的基因与布鲁斯氏锥虫（TbPTP1）和克氏锥虫（TcPTP2）基因同源。TrPTP2 和 TcPTP2 蛋白的克隆和表达使我们能够在 BALB/c 小鼠中产生抗 PTP2 的单克隆抗体。当表达在锥虫的前鞭毛体和动基体时，天然的 TrPTP2 被检测为一种与寄生虫鞭毛相关的~65 kDa 蛋白。鉴于鞭毛是原生动物细胞分化的重要结构，鞭毛中存在负责酪氨酸去磷酸化的蛋白可能代表了该结构中一种有趣的调控机制。
