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

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

doi:10.3389/fmicb.2020.611190

Abstract

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

Highlights

Malaria is a globally distributed disease that poses a serious threat to public health (Chiodini, 2018)
P. falciparum exports a large number of proteins into erythrocytes, some of which form a complex network with host proteins, while others are transferred onto the infected red blood cell surface (Maier et al, 2008; Prajapati and Singh, 2013; Oberli et al, 2014; Warncke et al, 2016)
For the malaria parasite P. falciparum to thrive inside human erythrocytes, it must modulate host cells, and this involves networks of protein-protein interactions

Summary

Introduction

Malaria is a globally distributed disease that poses a serious threat to public health (Chiodini, 2018). P. falciparum exports a large number of proteins into erythrocytes, some of which form a complex network with host proteins, while others are transferred onto the infected red blood cell (iRBC) surface (Maier et al, 2008; Prajapati and Singh, 2013; Oberli et al, 2014; Warncke et al, 2016). At this stage, P. falciparum remodels human erythrocytes, which results in structural and physiological alterations and increased rigidity of the erythrocyte membrane. These changes help the parasite to evade host immune

Methods

Results

Conclusion