Abstract
BackgroundDuring development in human erythrocytes, Plasmodium falciparum parasites display a remarkable number of adhesive proteins on their plasma membrane. In the invasive merozoites, these include members of the PfMSP1 and PfAMA1/RON complexes, which facilitate contact between merozoites and red blood cells. In gametocytes, sexual precursor cells mediating parasite transmission to the mosquito vector, plasma membrane-associated proteins primarily belong to the PfCCp and 6-cys families with roles in fertilization. This study describes a newly identified WD40-repeat protein unique to Plasmodium species that associates with adhesion protein complexes of both merozoites and gametocytes.MethodsThe WD40-repeat protein-like protein PfWLP1 was identified via co-immunoprecipitation assays followed by mass spectrometry and characterized using biochemical and immunohistochemistry methods. Reverse genetics were employed for functional analysis.ResultsPfWLP1 is expressed both in schizonts and gametocytes. In mature schizonts, the protein localizes underneath the merozoite micronemes and interacts with PfAMA1, while in gametocytes PfWLP1 primarily accumulates underneath the plasma membrane and associates with PfCCp1 and Pfs230. Reverse genetics failed to disrupt the pfwlp1 gene, while haemagglutinin-tagging was feasible, suggesting a crucial function for PfWLP1 during blood stage replication.ConclusionsThis is the first report on a plasmodial WD40-repeat protein associating with cell adhesion proteins. Since WD40 domains are known to mediate protein–protein contact by serving as a rigid scaffold for protein interactions, the presented data suggest that PfWLP1 supports the stability of adhesion protein complexes of the plasmodial blood stages.Electronic supplementary materialThe online version of this article (doi:10.1186/s12936-015-0967-x) contains supplementary material, which is available to authorized users.
Highlights
During development in human erythrocytes, Plasmodium falciparum parasites display a remarkable number of adhesive proteins on their plasma membrane
Most of the adhesive proteins found on the surface of the invasive merozoites involved in binding to the red blood cell (RBC) prior to infection are known to assemble as complexes, e.g., the merozoite surface protein 1 (MSP1) complex or the apical membrane antigen 1 (AMA1)/Rhoptry neck (RON)-complex
It was shown that AMA1, a transmembrane protein of the micronemal membrane, upon merozoite attachment to the RBC relocates to the plasma membrane and interacts with RON proteins that have been secreted and inserted into the RBC membrane
Summary
During development in human erythrocytes, Plasmodium falciparum parasites display a remarkable number of adhesive proteins on their plasma membrane. Protein complexes are formed by two or more non-covalently bound proteins mutually supportive in distinct For intracellular pathogens, such as malaria parasites, recognition, adhesion and invasion of host cells are essential steps during infection and are often mediated von Bohl et al Malar J (2015) 14:435 by protein–protein interactions. Most of the adhesive proteins found on the surface of the invasive merozoites involved in binding to the red blood cell (RBC) prior to infection are known to assemble as complexes, e.g., the merozoite surface protein 1 (MSP1) complex or the apical membrane antigen 1 (AMA1)/Rhoptry neck (RON)-complex (reviewed in [1,2,3]). RON2 functions as an anchor on the RBC membrane, interacting with the parasite transmembrane protein AMA1 and thereby forming the tight junction ([5, 6], reviewed in [7])
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