A merozoite-specific 22-kDa rhoptry protein of the coccidium Eimeria nieschulzi (Sporozoa, Coccidia) is exocytosed in the parasitophorous vacuole upon host cell invasion

1998 ◽  
Vol 84 (4) ◽  
pp. 291-296 ◽  
Author(s):  
B. Rick ◽  
J.-F. Dubremetz ◽  
R. Entzeroth
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Parasitophorous Vacuole ◽  
Host Cell Invasion ◽  
Eimeria Nieschulzi ◽  
Rhoptry Protein

Characterisation of NcGRA7 and NcSAG4 proteins: Immunolocalisation and their role in the host cell invasion by Neospora caninum tachyzoites

2010 ◽  
Vol 55 (4) ◽  
Author(s):  
Adriana Aguado-Martínez ◽  
Gema Álvarez-García ◽  
Gereon Schares ◽  
Verónica Risco-Castillo ◽  
Aurora Fernández-García ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Host Cell ◽  
Cell Invasion ◽  
Neospora Caninum ◽  
Parasitophorous Vacuole ◽  
Membrane Surface ◽  
Chronic Phase ◽  
Host Cell Invasion ◽  
Invasion Mechanisms ◽  
The Matrix

AbstractNeospora caninum negatively impacts bovine reproductive performance around the world. Addressing this problem requires a greater understanding of the parasite’s molecular biology. In this study, monoclonal antibodies against recombinant proteins were successfully developed and employed to characterise two different proteins of N. caninum: the acute phase-associated NcGRA7 and the chronic phase-associated NcSAG4. Immunofluorescence with the anti-rNcGRA7 monoclonal antibody suggested that NcGRA7 trafficks from tachyzoite dense granules to the matrix of the parasitophorous vacuole and parasite’s surroundings. Furthermore, NcGRA7 is also expressed in the bradyzoite stage and localised on the matrix of bradyzoite-positive vacuoles. NcGRA7 appears to be partially involved in the tachyzoite-invasion mechanisms, as an anti-rNcGRA7 monoclonal antibody partially inhibited in vitro tachyzoite-invasion. A monoclonal antibody specific for NcSAG4 confirmed this protein’s bradyzoitespecific expression both by western blot and immunofluorescence. However, some bradyzoite-positive vacuoles only weakly expressed NcSAG4, if it was expressed at all. The specificity of the anti-rNcSAG4 monoclonal antibody was confirmed by the recognition of the NcSAG4 in the membrane surface of Nc-1SAG4c transgenic tachyzoites, which constitutively expresses NcSAG4. Blocking NcSAG4 of Nc-1SAG4c tachyzoites with the monoclonal antibody did not affect host cell invasion. However, its implication on the host cell adhesion or host immune evasion should not be discarded.

scholarly journals First Characterization of theNeospora caninumDense Granule Protein GRA9

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Margret Leineweber ◽  
Katrin Spekker-Bosker ◽  
Vanessa Ince ◽  
Gereon Schares ◽  
Andrew Hemphill ◽  
...  
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Neospora Caninum ◽  
Parasitophorous Vacuole ◽  
Dense Granule ◽  
Immunogold Electron Microscopy ◽  
Host Cell Invasion ◽  
Dense Granules ◽  
Granule Protein

The obligate intracellular apicomplexan parasiteNeospora caninum (N. caninum)is closely related toToxoplasma gondii (T. gondii). The dense granules, which are present in all apicomplexan parasites, are important secretory organelles. Dense granule (GRA) proteins are released into the parasitophorous vacuole (PV) following host cell invasion and are known to play important roles in the maintenance of the host-parasite relationship and in the acquisition of nutrients. Here, we provide a detailed characterization of theN. caninumdense granule protein NcGRA9. The in silico genomic organization and key protein characteristics are described. Immunofluorescence-based localization studies revealed that NcGRA9 is located in the dense granules and is released into the interior of the PV following host cell invasion. Immunogold-electron microscopy confirmed the dense granule localization and showed that NcGRA9 is associated with the intravacuolar network. In addition, NcGRA9 is found in the “excreted secreted antigen” (ESA) fraction ofN. caninum. Furthermore, by analysing the distribution of truncated versions of NcGRA9, we provide evidence that the C-terminal region of this protein is essential for the targeting of NcGRA9 into the dense granules ofN. caninum, and the truncated proteins show reduced secretion.

scholarly journals Author response: The Plasmodium falciparum rhoptry protein RhopH3 plays essential roles in host cell invasion and nutrient uptake

2017 ◽  
Author(s):  
Emma S Sherling ◽  
Ellen Knuepfer ◽  
Joseph A Brzostowski ◽  
Louis H Miller ◽  
Michael J Blackman ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Nutrient Uptake ◽  
Cell Invasion ◽  
Author Response ◽  
Host Cell Invasion ◽  
Rhoptry Protein

Host cell invasion by Apicomplexa: an expression of the parasite's contractile system?

Parasitology ◽  
1983 ◽  
Vol 87 (2) ◽  
pp. 199-209 ◽  
Author(s):  
D. G. Russell
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Parasitophorous Vacuole ◽  
Membrane Receptors ◽  
Host Cell Invasion ◽  
Contractile System ◽  
Transmission Electron ◽  
Electron Microscopes ◽  
The One ◽  
Host Parasite

SUMMARYRecent studies on the motility of coccidian sporozoites have demonstrated a membrane-associated contractile system capable of moving certain intramembraneous components down the parasite surface propelling it forwards. The properties of this system resemble recorded observations on host cell invasion. In this study the invasive behaviour ofEimeria tenellaandE. acervulinahas been examined, with reference to the above findings, by light microscope and scanning and transmission electron microscopes. Known inhibitors of motility prevent invasion, though attachment appears unaffected. Invasion itself consists of 3 phases; attachment and orientation, induction of a parasitophorous vacuole and translocation of the parasite into the vacuole. Ultrastructural examination reveals a close membrane/membrane association maintained throughout invasion. From these results it is suggested that the parasite enters the parasitophorous vacuole by ‘capping’ the host/parasite junction down its body, so locomoting into the host cell. Such a model has two main advantages; it requires no additional modifications to either cell, and the specificity of membrane receptors would enable the one membrane-associated contractile system to be responsible for locomotion, antibody capping and host cell invasion.

scholarly journals Phosphorylation of Rhoptry Protein RhopH3 Is Critical for Host Cell Invasion by the Malaria Parasite

mBio ◽  
2020 ◽  
Vol 11 (5) ◽  
Author(s):  
Roseleen Ekka ◽  
Ankit Gupta ◽  
Sonika Bhatnagar ◽  
Pawan Malhotra ◽  
Pushkar Sharma
Keyword(s):  
Host Cell ◽  
Cell Invasion ◽  
Blood Cells ◽  
Malaria Infection ◽  
Malaria Parasite ◽  
Host Cell Invasion ◽  
Human Malaria Parasite ◽  
Content Type ◽  
Rhoptry Protein

ABSTRACT Merozoites formed after asexual division of the malaria parasite invade the host red blood cells (RBCs), which is critical for initiating malaria infection. The process of invasion involves specialized organelles like micronemes and rhoptries that discharge key proteins involved in interaction with host RBC receptors. RhopH complex comprises at least three proteins, which include RhopH3. RhopH3 is critical for the process of red blood cell (RBC) invasion as well as intraerythrocytic development of human malaria parasite Plasmodium falciparum. It is phosphorylated at serine 804 (S804) in the parasite; however, it is unclear if phosphorylation regulates its function. To address this, a CRISPR-CAS9-based approach was used to mutate S804 to alanine (A) in P. falciparum. Using this phosphomutant (R3_S804A) of RhopH3, we demonstrate that the phosphorylation of S804 is critical for host RBC invasion by the parasite but not for its intraerythrocytic development. Importantly, the phosphorylation of RhopH3 regulates its localization to the rhoptries and discharge from the parasite, which is critical for RBC invasion. We also identified P. falciparum CDPK1 (PfCDPK1) as a possible candidate kinase for RhopH3-S804 phosphorylation and found that it regulates RhopH3 secretion from the parasite. These findings provide novel insights into the role of phosphorylation in rhoptry release and invasion, which is poorly understood. IMPORTANCE Host cell invasion by the malaria parasite is critical for establishing infection in human host and is dependent on discharge of key ligands from organelles like rhoptry and microneme, and these ligands interact with host RBC receptors. In the present study, we demonstrate that phosphorylation of a key rhoptry protein, RhopH3, is critical for host invasion. Phosphorylation regulates its localization to rhoptries and discharge from the parasite.

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