Yang Baoling, Wang Xiaofeng, Jiang Ning, Sang Xiaoyu, Feng Ying, Chen Ran, Wang Xinyi, Chen Qijun
Key Laboratory of Livestock Infectious Diseases in Northeast China, Ministry of Education, Key Laboratory of Zoonosis, Shenyang Agricultural University, Shenyang, China.
College of Food Science and Technology, Shenyang Agricultural University, Shenyang, China.
Front Microbiol. 2020 Nov 13;11:611190. doi: 10.3389/fmicb.2020.611190. eCollection 2020.
extensively remodels host cells by translocating numerous proteins into the cytoplasm of red blood cells (RBCs) after invasion. Among these exported proteins, members of the helical interspersed subtelomeric (PHIST) family are crucial for host cell remodeling and host-parasite interactions, and thereby contribute to malaria pathogenesis. Herein, we explored the function of PF3D7_1372300, a member of the PHIST/PHISTa-like subfamily. PF3D7_1372300 was highly transcribed and expressed during the blood stage of , and distributed throughout RBCs, but most abundant at the erythrocyte membrane. Specific interaction of PF3D7_1372300 with the cytoplasmic tail of erythrocyte membrane protein 1 (PfEMP1) was revealed by immunofluorescence assay, intermolecular interaction assays. The interaction sites of PF3D7_1372300 with PfEMP1 ATS domain were found involved more than 30 amino acids (aa) at several positions. The findings deepen our understanding of host-parasite interactions and malaria pathogenesis.
入侵后，通过将大量蛋白质转运到红细胞（RBC）的细胞质中，广泛重塑宿主细胞。在这些输出蛋白中，螺旋状散布亚端粒（PHIST）家族成员对于宿主细胞重塑和宿主-寄生虫相互作用至关重要，从而导致疟疾发病机制。在此，我们探究了PHIST/PHISTa样亚家族成员PF3D7_1372300的功能。PF3D7_1372300在疟原虫血液阶段高度转录和表达，并分布于整个红细胞，但在红细胞膜上最为丰富。免疫荧光测定、分子间相互作用测定揭示了PF3D7_1372300与红细胞膜蛋白1（PfEMP1）细胞质尾的特异性相互作用。发现PF3D7_1372300与PfEMP1 ATS结构域的相互作用位点在几个位置涉及30多个氨基酸（aa）。这些发现加深了我们对宿主-寄生虫相互作用和疟疾发病机制的理解。
