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 Daughter Cell Assembly in the Protozoan ParasiteToxoplasma gondii

2002 ◽  
Vol 13 (2) ◽  
pp. 593-606 ◽  
Author(s):  
Ke Hu ◽  
Tara Mann ◽  
Boris Striepen ◽  
Con J. M. Beckers ◽  
David S. Roos ◽  
...  
Keyword(s):  
Cell Division ◽  
Fluorescent Protein ◽  
Molecular Genetic ◽  
Inner Membrane ◽  
Apicomplexan Parasites ◽  
Membrane Complex ◽  
Ideal System ◽  
Animal Pathogens ◽  
Inner Membrane Complex

The phylum Apicomplexa includes thousands of species of obligate intracellular parasites, many of which are significant human and/or animal pathogens. Parasites in this phylum replicate by assembling daughters within the mother, using a cytoskeletal and membranous scaffolding termed the inner membrane complex. Most apicomplexan parasites, including Plasmodium sp. (which cause malaria), package many daughters within a single mother during mitosis, whereas Toxoplasma gondii typically packages only two. The comparatively simple pattern of T. gondii cell division, combined with its molecular genetic and cell biological accessibility, makes this an ideal system to study parasite cell division. A recombinant fusion between the fluorescent protein reporter YFP and the inner membrane complex protein IMC1 has been exploited to examine daughter scaffold formation in T. gondii.Time-lapse video microscopy permits the entire cell cycle of these parasites to be visualized in vivo. In addition to replication via endodyogeny (packaging two parasites at a time), T. gondii is also capable of forming multiple daughters, suggesting fundamental similarities between cell division in T. gondii and other apicomplexan parasites.

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 A De novo Peptide from a High Throughput Peptide Library Blocks Myosin A -MTIP Complex Formation in Plasmodium falciparum

2020 ◽  
Vol 21 (17) ◽  
pp. 6158
Author(s):  
Zill e Anam ◽  
Nishant Joshi ◽  
Sakshi Gupta ◽  
Preeti Yadav ◽  
Ayushi Chaurasiya ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
De Novo ◽  
Peptide Library ◽  
Tail Domain ◽  
Interacting Protein ◽  
Membrane Complex ◽  
Inner Membrane Complex ◽  
De Novo Peptide

Apicomplexan parasites, through their motor machinery, produce the required propulsive force critical for host cell-entry. The conserved components of this so-called glideosome machinery are myosin A and myosin A Tail Interacting Protein (MTIP). MTIP tethers myosin A to the inner membrane complex of the parasite through 20 amino acid-long C-terminal end of myosin A that makes direct contacts with MTIP, allowing the invasion of Plasmodium falciparum in erythrocytes. Here, we discovered through screening a peptide library, a de-novo peptide ZA1 that binds the myosin A tail domain. We demonstrated that ZA1 bound strongly to myosin A tail and was able to disrupt the native myosin A tail MTIP complex both in vitro and in vivo. We then showed that a shortened peptide derived from ZA1, named ZA1S, was able to bind myosin A and block parasite invasion. Overall, our study identified a novel anti-malarial peptide that could be used in combination with other antimalarials for blocking the invasion of Plasmodium falciparum.

scholarly journals The ZIP Code of Vesicle Trafficking in Apicomplexa: SEC1/Munc18 and SNARE Proteins

mBio ◽  
2020 ◽  
Vol 11 (5) ◽  
Author(s):  
Hugo Bisio ◽  
Rouaa Ben Chaabene ◽  
Ricarda Sabitzki ◽  
Bohumil Maco ◽  
Jean Baptiste Marq ◽  
...  
Keyword(s):  
Host Cell ◽  
Critical Role ◽  
Vesicular Trafficking ◽  
Snare Proteins ◽  
Organelle Biogenesis ◽  
Inner Membrane ◽  
Content Type ◽  
Membrane Complex ◽  
Inner Membrane Complex ◽  
Zip Code

ABSTRACT Apicomplexans are obligate intracellular parasites harboring three sets of unique secretory organelles termed micronemes, rhoptries, and dense granules that are dedicated to the establishment of infection in the host cell. Apicomplexans rely on the endolysosomal system to generate the secretory organelles and to ingest and digest host cell proteins. These parasites also possess a metabolically relevant secondary endosymbiotic organelle, the apicoplast, which relies on vesicular trafficking for correct incorporation of nuclear-encoded proteins into the organelle. Here, we demonstrate that the trafficking and destination of vesicles to the unique and specialized parasite compartments depend on SNARE proteins that interact with tethering factors. Specifically, all secreted proteins depend on the function of SLY1 at the Golgi. In addition to a critical role in trafficking of endocytosed host proteins, TgVps45 is implicated in the biogenesis of the inner membrane complex (alveoli) in both Toxoplasma gondii and Plasmodium falciparum, likely acting in a coordinated manner with Stx16 and Stx6. Finally, Stx12 localizes to the endosomal-like compartment and is involved in the trafficking of proteins to the apical secretory organelles rhoptries and micronemes as well as to the apicoplast. IMPORTANCE The phylum of Apicomplexa groups medically relevant parasites such as those responsible for malaria and toxoplasmosis. As members of the Alveolata superphylum, these protozoans possess specialized organelles in addition to those found in all members of the eukaryotic kingdom. Vesicular trafficking is the major route of communication between membranous organelles. Neither the molecular mechanism that allows communication between organelles nor the vesicular fusion events that underlie it are completely understood in Apicomplexa. Here, we assessed the function of SEC1/Munc18 and SNARE proteins to identify factors involved in the trafficking of vesicles between these various organelles. We show that SEC1/Munc18 in interaction with SNARE proteins allows targeting of vesicles to the inner membrane complex, prerhoptries, micronemes, apicoplast, and vacuolar compartment from the endoplasmic reticulum, Golgi apparatus, or endosomal-like compartment. These data provide an exciting look at the “ZIP code” of vesicular trafficking in apicomplexans, essential for precise organelle biogenesis, homeostasis, and inheritance.

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