scholarly journals The Dynamic Roles of the Inner Membrane Complex in the Multiple Stages of the Malaria Parasite

2021 ◽  
Vol 10 ◽  
Author(s):  
Josie Liane Ferreira ◽  
Dorothee Heincke ◽  
Jan Stephan Wichers ◽  
Benjamin Liffner ◽  
Danny W. Wilson ◽  
...  
Keyword(s):  
De Novo ◽  
Morphological Changes ◽  
Protein Composition ◽  
Cell Types ◽  
Structural Element ◽  
Inner Membrane ◽  
Cell Functions ◽  
Membrane Complex ◽  
Inner Membrane Complex ◽  
And Function

Apicomplexan parasites, such as human malaria parasites, have complex lifecycles encompassing multiple and diverse environmental niches. Invading, replicating, and escaping from different cell types, along with exploiting each intracellular niche, necessitate large and dynamic changes in parasite morphology and cellular architecture. The inner membrane complex (IMC) is a unique structural element that is intricately involved with these distinct morphological changes. The IMC is a double membrane organelle that forms de novo and is located beneath the plasma membrane of these single-celled organisms. In Plasmodium spp. parasites it has three major purposes: it confers stability and shape to the cell, functions as an important scaffolding compartment during the formation of daughter cells, and plays a major role in motility and invasion. Recent years have revealed greater insights into the architecture, protein composition and function of the IMC. Here, we discuss the multiple roles of the IMC in each parasite lifecycle stage as well as insights into its sub-compartmentalization, biogenesis, disassembly and regulation during stage conversion of P. falciparum.

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 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

scholarly journals The action of digitonin on rat liver mitochondria. Electron microscopy

1968 ◽  
Vol 107 (3) ◽  
pp. 377-380 ◽  
Author(s):  
Donald J. Morton ◽  
Charles Hoppel ◽  
Cecil Cooper
Keyword(s):  
Outer Membrane ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Inner Membrane ◽  
Lamellar Structures ◽  
Membrane Complex ◽  
Condensed Form ◽  
Intact Mitochondrion ◽  
Inner Membrane Complex

1. Rat liver mitochondria were examined in the electron microscope by using negative staining in the presence of 0·3m-sucrose. The intact outer membrane does not appear to be freely permeable to the stain. Where the stain penetrated through a tear it was seen that the inner membrane had randomly oriented grooves, many of which contained round structures varying between 200 and 900å in diameter. Laminar structures containing two to five layers of approx. 50å each were found at the periphery. 2. When the outer membrane was removed by treating the mitochondria with digitonin several types of inner-membrane complexes were formed and they showed a general correlation with those observed in sectioned samples of the same preparations. The main types were: (a) a condensed form looking very much like the intact mitochondrion without the outer membrane (this still showed the grooves, some of which contained the round structures, and the laminar whirls at the edges); (b) a more transparent form containing tubules of uniform width and various lengths (some of these appeared to terminate in a hole at the surface of the inner membrane); (c) a large torn sac, probably the inner membrane, containing some tubules and vesicles. 3. When the inner-membrane complex was further treated with digitonin it was disrupted and the resulting material consisted of pieces of membrane, doughnut-shaped units and lamellar structures. Most of these pieces varied in size between 500 and 1000å.

scholarly journals Rab11A-Controlled Assembly of the Inner Membrane Complex Is Required for Completion of Apicomplexan Cytokinesis

2009 ◽  
Vol 5 (1) ◽  
pp. e1000270 ◽  
Author(s):  
Carolina Agop-Nersesian ◽  
Bernina Naissant ◽  
Fathia Ben Rached ◽  
Manuel Rauch ◽  
Angelika Kretzschmar ◽  
...  
Keyword(s):  
Inner Membrane ◽  
Controlled Assembly ◽  
Membrane Complex ◽  
Inner Membrane Complex
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