AUTHOR=Yang Baoling , Wang Xiaofeng , Jiang Ning , Sang Xiaoyu , Feng Ying , Chen Ran , Wang Xinyi , Chen Qijun 

TITLE=Interaction Analysis of a Plasmodium falciparum PHISTa-like Protein and PfEMP1 Proteins

JOURNAL=Frontiers in Microbiology

VOLUME=11

YEAR=2020

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2020.611190

DOI=10.3389/fmicb.2020.611190

ISSN=1664-302X

ABSTRACT=<p><italic>Plasmodium falciparum</italic> 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 <italic>Plasmodium</italic> 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 <italic>P. falciparum</italic>, and distributed throughout RBCs, but most abundant at the erythrocyte membrane. Specific interaction of PF3D7_1372300 with the cytoplasmic tail of <italic>P. falciparum</italic> erythrocyte membrane protein 1 (PfEMP1) was revealed by immunofluorescence assay, <italic>in vitro</italic> 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.</p>