Abstract
ABSTRACTThe intraerythrocytic developmental cycle of Plasmodium falciparum is completed with the release of up to 32 invasive daughter cells, the merozoites, into the blood stream. Before release, the final step of merozoite development is the assembly of the cortical pellicle, a multi-layered membrane structure. This unique apicomplexan feature includes the inner membrane complex (IMC) and the parasite's plasma membrane. A dynamic ring structure, referred to as the basal complex, is part of the IMC and helps to divide organelles and abscises in the maturing daughter cells. Here, we analyze the dynamics of the basal complex of P. falciparum. We report on a novel transmembrane protein of the basal complex termed BTP1, which is specific to the genus Plasmodium. It colocalizes with the known basal complex marker protein MORN1 and shows distinct dynamics as well as localization when compared to other IMC proteins during schizogony. Using a parasite plasma membrane marker cell line, we correlate dynamics of the basal complex with the acquisition of the maternal membrane. We show that plasma membrane invagination and IMC propagation are interlinked during the final steps of cell division.
Highlights
Apicomplexans are a clade of single-cell eukaryotes, the majority of which are obligate intracellular parasites (Cavelier-Smith, 1993)
Apicomplexan parasites multiply within their host cell (Fig. 1A) through internal budding, resulting in either two daughter cells or multiple progeny
We report on the dynamics of the basal complex in P. falciparum merozoites using a newly identified protein (PFF0570c) termed basal complex transmembrane protein 1 (BTP1), which is unique to the genus Plasmodium
Summary
Apicomplexans are a clade of single-cell eukaryotes, the majority of which are obligate intracellular parasites (Cavelier-Smith, 1993). In Toxoplasma gondii, the apical and the basal end of the IMC, termed apical cap and basal complex respectively, represent two specialized cytoskeletal structures that are characterized by specific sets of proteins. The protein has no homologs outside of the genus of Plasmodium and appears to be a recent Plasmodium-specific evolutionary innovation, like the recently described IMC membrane matrix protein MAL13P1.228, which marks transversal structures in the pre-sexual stages of the parasite (Kono et al, 2012).
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