scholarly journals Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum

2012 ◽  
Vol 178 (1) ◽  
pp. 61-73 ◽  
Author(s):  
Jürgen Bosch ◽  
Matthew H. Paige ◽  
Akhil B. Vaidya ◽  
Lawrence W. Bergman ◽  
Wim G.J. Hol
Keyword(s):  
Crystal Structure ◽  
Plasmodium Falciparum ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Inner Membrane Complex

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.

Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes

2012 ◽  
Vol 125 (8) ◽  
pp. 2053-2063 ◽  
Author(s):  
M. K. Dearnley ◽  
J. A. Yeoman ◽  
E. Hanssen ◽  
S. Kenny ◽  
L. Turnbull ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Inner Membrane Complex ◽  
And Function

scholarly journals Tracking Glideosome-Associated Protein 50 Reveals the Development and Organization of the Inner Membrane Complex of Plasmodium falciparum

2011 ◽  
Vol 10 (4) ◽  
pp. 556-564 ◽  
Author(s):  
Jeffrey A. Yeoman ◽  
Eric Hanssen ◽  
Alexander G. Maier ◽  
Nectarios Klonis ◽  
Bohumil Maco ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Fluorescent Protein ◽  
Early Stage ◽  
Tail Domain ◽  
Structured Illumination Microscopy ◽  
Membrane Anchor ◽  
Inner Membrane ◽  
Content Type ◽  
Membrane Complex ◽  
Inner Membrane Complex

ABSTRACT The most deadly of the human malaria parasites, Plasmodium falciparum , has different stages specialized for invasion of hepatocytes, erythrocytes, and the mosquito gut wall. In each case, host cell invasion is powered by an actin-myosin motor complex that is linked to an inner membrane complex (IMC) via a membrane anchor called the glideosome-associated protein 50 (PfGAP50). We generated P. falciparum transfectants expressing green fluorescent protein (GFP) chimeras of PfGAP50 (PfGAP50-GFP). Using immunoprecipitation and fluorescence photobleaching, we show that C-terminally tagged PfGAP50-GFP can form a complex with endogenous copies of the linker protein PfGAP45 and the myosin A tail domain-interacting protein (MTIP). Full-length PfGAP50-GFP is located in the endoplasmic reticulum in early-stage parasites and then redistributes to apical caps during the formation of daughter merozoites. In the final stage of schizogony, the PfGAP50-GFP profile extends further around the merozoite surface. Three-dimensional (3D) structured illumination microscopy reveals the early-stage IMC as a doubly punctured flat ellipsoid that separates to form claw-shaped apposed structures. A GFP fusion of PfGAP50 lacking the C-terminal membrane anchor is misdirected to the parasitophorous vacuole. Replacement of the acid phosphatase homology domain of PfGAP50 with GFP appears to allow correct trafficking of the chimera but confers a growth disadvantage.

scholarly journals Disrupting assembly of the inner membrane complex blocks Plasmodium falciparum sexual stage development

2017 ◽  
Vol 13 (10) ◽  
pp. e1006659 ◽  
Author(s):  
Molly Parkyn Schneider ◽  
Boyin Liu ◽  
Philipp Glock ◽  
Annika Suttie ◽  
Emma McHugh ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Sexual Stage ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Stage Development ◽  
Inner Membrane Complex

scholarly journals Raft microdomain localized in the luminal leaflet of inner membrane complex of living Toxoplasma gondii

2021 ◽  
Vol 100 (2) ◽  
pp. 151149
Author(s):  
Rikako Konishi ◽  
Yuna Kurokawa ◽  
Kanna Tomioku ◽  
Tatsunori Masatani ◽  
Xuenan Xuan ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Inner Membrane Complex

scholarly journals Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii

2004 ◽  
Vol 165 (3) ◽  
pp. 383-393 ◽  
Author(s):  
Elizabeth Gaskins ◽  
Stacey Gilk ◽  
Nicolette DeVore ◽  
Tara Mann ◽  
Gary Ward ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Protein Complex ◽  
Integral Membrane Protein ◽  
Gliding Motility ◽  
Host Cells ◽  
Inner Membrane ◽  
Apicomplexan Parasites ◽  
Membrane Complex ◽  
Inner Membrane Complex ◽  
Two Stages

Apicomplexan parasites exhibit a unique form of substrate-dependent motility, gliding motility, which is essential during their invasion of host cells and during their spread between host cells. This process is dependent on actin filaments and myosin that are both located between the plasma membrane and two underlying membranes of the inner membrane complex. We have identified a protein complex in the apicomplexan parasite Toxoplasma gondii that contains the class XIV myosin required for gliding motility, TgMyoA, its associated light chain, TgMLC1, and two novel proteins, TgGAP45 and TgGAP50. We have localized this complex to the inner membrane complex of Toxoplasma, where it is anchored in the membrane by TgGAP50, an integral membrane glycoprotein. Assembly of the protein complex is spatially controlled and occurs in two stages. These results provide the first molecular description of an integral membrane protein as a specific receptor for a myosin motor, and further our understanding of the motile apparatus underlying gliding motility in apicomplexan parasites.

scholarly journals Gliding Associated Proteins Play Essential Roles during the Formation of the Inner Membrane Complex of Toxoplasma gondii

2016 ◽  
Vol 12 (2) ◽  
pp. e1005403 ◽  
Author(s):  
Clare R. Harding ◽  
Saskia Egarter ◽  
Matthew Gow ◽  
Elena Jiménez-Ruiz ◽  
David J. P. Ferguson ◽  
...  
Keyword(s):  
Toxoplasma Gondii ◽  
Inner Membrane ◽  
Membrane Complex ◽  
Associated Proteins ◽  
Inner Membrane Complex
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