Cyclophilin 19 secreted in the host cell cytosol by Trypanosoma cruzi promotes ROS production required for parasite growth

2020 ◽  
Author(s):  
Gregory Pedroso Santos ◽  
Fernanda Midori Abukawa ◽  
Normanda Souza‐Melo ◽  
Laura Maria Alcântara ◽  
Paula Bittencourt‐Cunha ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Parasite Growth ◽  
Ros Production ◽  
Cell Cytosol ◽  
Host Cell Cytosol

scholarly journals Trypanosoma cruzi Differentiates and Multiplies within Chimeric Parasitophorous Vacuoles in Macrophages Coinfected with Leishmania amazonensis

2016 ◽  
Vol 84 (5) ◽  
pp. 1603-1614 ◽  
Author(s):  
Carina Carraro Pessoa ◽  
Éden Ramalho Ferreira ◽  
Ethel Bayer-Santos ◽  
Michel Rabinovitch ◽  
Renato Arruda Mortara ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Biology ◽  
Mammalian Cells ◽  
Leishmania Amazonensis ◽  
Content Type ◽  
Multidimensional Imaging ◽  
Protozoan Infections ◽  
Cell Cytosol ◽  
Host Cell Cytosol

The trypanosomatidsLeishmania amazonensisandTrypanosoma cruziare excellent models for the study of the cell biology of intracellular protozoan infections. After their uptake by mammalian cells, the parasitic protozoan flagellatesL. amazonensisandT. cruzilodge within acidified parasitophorous vacuoles (PVs). However, whereasL. amazonensisdevelops in spacious, phagolysosome-like PVs that may enclose numerous parasites,T. cruziis transiently hosted within smaller vacuoles from which it soon escapes to the host cell cytosol. To investigate if parasite-specific vacuoles are required for the survival and differentiation ofT. cruzi, we constructed chimeric vacuoles by infection ofL. amazonensisamastigote-infected macrophages withT. cruziepimastigotes (EPIs) or metacyclic trypomastigotes (MTs). These chimeric vacuoles, easily observed by microscopy, allowed the entry and fate ofT. cruziinL. amazonensisPVs to be dynamically recorded by multidimensional imaging of coinfected cells. We found that althoughT. cruziEPIs remained motile and conserved their morphology in chimeric vacuoles,T. cruziMTs differentiated into amastigote-like forms capable of multiplying. These results demonstrate that the large adaptive vacuoles ofL. amazonensisare permissive toT. cruzisurvival and differentiation and that noninfective EPIs are spared from destruction within the chimeric PVs. We conclude thatT. cruzidifferentiation can take place inLeishmania-containing vacuoles, suggesting this occurs prior to their escape into the host cell cytosol.

scholarly journals Differential Expression and Characterization of a Member of the Mucin-Associated Surface Protein Family Secreted by Trypanosoma cruzi

2011 ◽  
Vol 79 (10) ◽  
pp. 3993-4001 ◽  
Author(s):  
Luis Miguel De Pablos ◽  
Gloria González González ◽  
Jennifer Solano Parada ◽  
Víctor Seco Hidalgo ◽  
Isabel María Díaz Lozano ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Surface Protein ◽  
Surface Proteins ◽  
Host Cells ◽  
Content Type ◽  
The Family ◽  
Cell Cytosol ◽  
Host Cell Cytosol

ABSTRACTWe describe the characterization, purification, expression, and location of a 52-kDa protein secreted during interaction between the metacyclic form ofTrypanosoma cruziand its target host cell. The protein, which we have named MASP52, belongs to the family of mucin-associated surface proteins (MASPs). The highest levels of expression of both the protein and mRNA occur during the metacyclic and bloodstream trypomastigote stages, the forms that infect the vertebrate host cells. The protein is located in the plasma membrane and in the flagellar pockets of the epimastigote, metacyclic, and trypomastigote forms and is secreted into the medium at the point of contact between the parasite and the cell membrane, as well as into the host-cell cytosol during the amastigote stage. IgG antibodies specific against a synthetic peptide corresponding to the catalytic zone of MASP52 significantly reduce the parasite's capacity to infect the host cells. Furthermore, when the protein is adsorbed onto inert particles of bentonite and incubated with a nonphagocytic cell culture, the particles are able to induce endocytosis in the cells, which seems to demonstrate that MASP52 plays a role in a process whereby the trypomastigote forms of the parasite invade the host cell.

scholarly journals Host Cell Lipid Bodies Triggered by Trypanosoma cruzi Infection and Enhanced by the Uptake of Apoptotic Cells Are Associated With Prostaglandin E2 Generation and Increased Parasite Growth

2011 ◽  
Vol 204 (6) ◽  
pp. 951-961 ◽  
Author(s):  
Heloisa D’Avila ◽  
Célio G. Freire-de-Lima ◽  
Natalia R. Roque ◽  
Livia Teixeira ◽  
Christina Barja-Fidalgo ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Prostaglandin E2 ◽  
Host Cell ◽  
Parasite Growth ◽  
Apoptotic Cells ◽  
Lipid Bodies ◽  
Cell Lipid ◽  
Cruzi Infection

Parasitophorous vacuoles of Leishmania mexicana acquire macromolecules from the host cell cytosol via two independent routes

1999 ◽  
Vol 112 (5) ◽  
pp. 681-693
Author(s):  
U.E. Schaible ◽  
P.H. Schlesinger ◽  
T.H. Steinberg ◽  
W.F. Mangel ◽  
T. Kobayashi ◽  
...  
Keyword(s):  
Host Cell ◽  
Lucifer Yellow ◽  
Cysteine Proteinase ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Infected Cells ◽  
Lysobisphosphatidic Acid ◽  
Cell Cytosol ◽  
Host Cell Cytosol

The intracellular parasite Leishmania survives and proliferates in host macrophages. In this study we show that parasitophorous vacuoles of L. mexicana gain access to cytosolic material via two different routes. (1) Small anionic molecules such as Lucifer Yellow are rapidly transported into the vacuoles by an active transport mechanism that is sensitive to inhibitors of the host cell's organic anion transporter. (2) Larger molecules such as fluorescent dextrans introduced into the host cell cytosol are also delivered to parasitophorous vacuoles. This transport is slower and sensitive to modulators of autophagy. Infected macrophages were examined by two novel assays to visualize and quantify this process. Immunoelectron microscopy of cells loaded with digoxigenin-dextran revealed label in multivesicular endosomes, which appeared to fuse with parasitophorous vacuoles. The inner membranes of the multivesicular vesicles label strongly with antibodies against lysobisphosphatidic acid, suggesting that they represent a point of confluence between the endosomal and autophagosomal pathways. Although the rate of autophagous transfer was comparable in infected and uninfected cells, infected cells retained hydrolyzed cysteine proteinase substrate to a greater degree. These data suggest that L. mexicana-containing vacuoles have access to potential nutrients in the host cell cytosol via at least two independent mechanisms.

scholarly journals Type II Secretion Substrates ofLegionella pneumophilaTranslocate Out of the Pathogen-Occupied Vacuole via a Semipermeable Membrane

mBio ◽  
2017 ◽  
Vol 8 (3) ◽  
Author(s):  
Hilary K. Truchan ◽  
Harry D. Christman ◽  
Richard C. White ◽  
Nakisha S. Rutledge ◽  
Nicholas P. Cianciotto
Keyword(s):  
Host Cell ◽  
Infected Host ◽  
Type Ii Secretion ◽  
Dependent Manner ◽  
Type Ii ◽  
Murine Macrophages ◽  
Intracellular Infection ◽  
Infected Host Cell ◽  
Cell Cytosol ◽  
Host Cell Cytosol

ABSTRACTLegionella pneumophilareplicates in macrophages in a host-derived phagosome, termed theLegionella-containing vacuole (LCV). While the translocation of type IV secretion (T4S) effectors into the macrophage cytosol is well established, the location of type II secretion (T2S) substrates in the infected host cell is unknown. Here, we show that the T2S substrate ProA, a metalloprotease, translocates into the cytosol of human macrophages, where it associates with the LCV membrane (LCVM). Translocation is detected as early as 10 h postinoculation (p.i.), which is approximately the midpoint of the intracellular life cycle. However, it is detected as early as 6 h p.i. if ProA is hyperexpressed, indicating that translocation depends on the timing of ProA expression and that any other factors necessary for translocation are in place by that time point. Translocation occurs with allL. pneumophilastrains tested and in amoebae, natural hosts forL. pneumophila. It was absent in murine bone marrow-derived macrophages and murine macrophage cell lines. The ChiA chitinase also associated with the cytoplasmic face of the LCVM at 6 h p.i. and in a T2S-dependent manner. Galectin-3 and galectin-8, eukaryotic proteins whose localization is influenced by damage to host membranes, appeared within the LCV of infected human but not murine macrophages beginning at 6 h p.i. Thus, we hypothesize that ProA and ChiA are first secreted into the vacuolar lumen by the activity of the T2S and subsequently traffic into the macrophage cytosol via a novel mechanism that involves a semipermeable LCVM.IMPORTANCEInfection of macrophages and amoebae plays a central role in the pathogenesis ofL. pneumophila, the agent of Legionnaires’ disease. We have previously demonstrated that the T2S system ofL. pneumophilagreatly contributes to intracellular infection. However, the location of T2S substrates within the infected host cell is unknown. This report presents the first evidence of aL. pneumophilaT2S substrate in the host cell cytosol and, therefore, the first evidence of a non-T4S effector trafficking out of the LCV. We also provide the first indication that the LCV is not completely intact but is instead semipermeable and that this occurs in human but not murine macrophages. Given this permeability, we hypothesize that other T2S substrates and LCV lumenal contents can escape into the host cell cytosol. Thus, these substrates may represent a battery of previously unidentified effectors that can interact with host factors and contribute to intracellular infection byL. pneumophila.

scholarly journals PfVPS45 Is Required for Host Cell Cytosol Uptake by Malaria Blood Stage Parasites

2019 ◽  
Vol 25 (1) ◽  
pp. 166-173.e5 ◽  
Author(s):  
Ernst Jonscher ◽  
Sven Flemming ◽  
Marius Schmitt ◽  
Ricarda Sabitzki ◽  
Nick Reichard ◽  
...  
Keyword(s):  
Host Cell ◽  
Blood Stage ◽  
Cell Cytosol ◽  
Host Cell Cytosol
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