scholarly journals Identification of novel inner membrane complex and apical annuli proteins of the malaria parasite Plasmodium falciparum

2021 ◽  
Author(s):  
Jan Stephan Wichers ◽  
Juliane Wunderlich ◽  
Dorothee Heincke ◽  
Samuel Pazicky ◽  
Jan Strauss ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Inner Membrane Complex

scholarly journals Plasmodium falciparum PhIL1 associated complex play an essential role in merozoite reorientation and invasion of host erythrocytes

2021 ◽  
Author(s):  
Ekta Saini ◽  
Pradeep Kumar Sheokand ◽  
Vaibhav Sharma ◽  
Prakhar Agrawal ◽  
Inderjeet Kaur ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Structural Protein ◽  
Initial Attachment ◽  
Interacting Protein ◽  
Human Malaria Parasite ◽  
Membrane Complex ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum ◽  
Inner Membrane Complex

Abstract The human malaria parasite, Plasmodium falciparum possess a unique gliding machinery referred as glideosome that powers its entry into the insect and vertebrate hosts. A number of parasite proteins including Photosensitized INA-labelled protein 1 (PhIL1) have been shown to associate with glideosome machinery. Here we describe a novel PhIL1 associated protein complex that co-exists with glideosome motor complex in the inner membrane complex of the merozoite. Furthermore, using experimental genetics approach we characterized the role(s) of three proteins associated with PhIL1: a glideosome associated protein- PfGAPM2, an IMC structural protein- PfALV5 and a previously uncharacterised protein - referred here as PfPhIP (PhIL1 Interacting Protein). Parasites lacking PfPhIP or PfGAPM2 were unable to invade the host RBCs. Additionally, the down regulation of PfPhIP resulted in significant defects in merozoite segmentation. Furthermore, the PfPhIP and PfGAPM2 depleted parasites revealed abrogation of reorientation/gliding, however initial attachment with host RBCs was not affected in these parasites. Together, the data presented here shows that proteins of the PhIL1 associated complex plays an important role in orientation of P. falciparum merozoites following initial attachment, which is crucial for formation of tight junction and hence invasion of host erythrocytes. The identification and characterization of PhIL1 associated complex opens new avenues for future anti-malarial drug development.

scholarly journals Identification of novel inner membrane complex and apical annuli proteins of the malaria parasite Plasmodium falciparum

2021 ◽  
Author(s):  
Jan Stephan Wichers ◽  
Juliane Wunderlich ◽  
Dorothee Heincke ◽  
Samuel Pazicky ◽  
Jan Strauss ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Spatial Association ◽  
Peptide Identification ◽  
Blood Stage ◽  
Asexual Blood Stage ◽  
Inner Membrane ◽  
Cell Functions ◽  
Membrane Complex ◽  
Inner Membrane Complex

ABSTRACTThe inner membrane complex (IMC) is a defining feature of apicomplexan parasites, which confers stability and shape to the cell, functions as a scaffolding compartment during the formation of daughter cells and plays an important role in motility and invasion during different life cycle stages of these single celled organisms. To explore the IMC proteome of the malaria parasite Plasmodium falciparum we applied a proximity-dependent biotin identification (BioID)-based proteomics approach, using the established IMC marker protein Photosensitized INA-Labelled protein 1 (PhIL1) as bait in asexual blood-stage parasites. Subsequent mass spectrometry-based peptide identification revealed enrichment of twelve known IMC proteins and several uncharacterized candidate proteins. We validated nine of these previously uncharacterized proteins by endogenous GFP-tagging. Six of these represent new IMC proteins, while three proteins have a distinct apical localization that most likely represent structures described as apical annuli in Toxoplasma gondii. Additionally, various Kelch13 interacting candidates were identified, suggesting an association of the Kelch13 compartment and the IMC in schizont and merozoite stages. This work extends the number of validated IMC proteins in the malaria parasite and reveals for the first time the existence of apical annuli proteins in P. falciparum. Additionally, it provides evidence for a spatial association between the Kelch13 compartment and the IMC in late blood-stage parasites.

Effects of Melatonin Derivatives on Human Malaria Parasite Plasmodium falciparum

2014 ◽  
Vol 8 (2) ◽  
pp. 102-108 ◽  
Author(s):  
Venkataramanujan Srinivasan ◽  
Rahimah Zakaria ◽  
Mahaneem Mohamed ◽  
Rozieyati Saleh
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Human Malaria Parasite ◽  
Human Malaria ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

scholarly journals Interactions between Merozoite Surface Proteins 1, 6, and 7 of the Malaria Parasite Plasmodium falciparum

2006 ◽  
Vol 281 (42) ◽  
pp. 31517-31527
Author(s):  
Christian W. Kauth ◽  
Ute Woehlbier ◽  
Michaela Kern ◽  
Zeleke Mekonnen ◽  
Rolf Lutz ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Surface Proteins ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

The plastid DNA of the malaria parasite Plasmodium falciparum is replicated by two mechanisms

2002 ◽  
Vol 45 (2) ◽  
pp. 533-542 ◽  
Author(s):  
D. H. Williamson ◽  
P. R. Preiser ◽  
P. W. Moore ◽  
S. McCready ◽  
M. Strath ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Parasite ◽  
Plastid Dna ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum
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