scholarly journals Identification and electrophysiological properties of a sphingosine‐dependent plasma membrane Ca 2+ channel in Trypanosoma cruzi

FEBS Journal ◽  
2019 ◽  
Vol 286 (19) ◽  
pp. 3909-3925 ◽  
Author(s):  
Jessica Rodriguez‐Duran ◽  
Andrea Pinto‐Martinez ◽  
Cecilia Castillo ◽  
Gustavo Benaim
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Electrophysiological Properties

Acetylenic fatty acids from Porcelia macrocarpa (Annonaceae) against trypomastigotes of Trypanosoma cruzi: Effect of octadec-9-ynoic acid in plasma membrane electric potential

2018 ◽  
Vol 78 ◽  
pp. 307-311 ◽  
Author(s):  
Vinicius S. Londero ◽  
Thais A. da Costa-Silva ◽  
Kaio S. Gomes ◽  
Daiane D. Ferreira ◽  
Juliana T. Mesquita ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Electric Potential ◽  
Acetylenic Fatty Acids

Participation of concanavalin A binding sites in the interaction between Trypanosoma cruzi and macrophages

1983 ◽  
Vol 62 (1) ◽  
pp. 287-299
Author(s):  
M.N. Meirelles ◽  
A. Martinez-Palomo ◽  
T. Souto-Padron ◽  
W. De Souza
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Trypanosoma Cruzi ◽  
Uniform Distribution ◽  
Concanavalin A ◽  
Binding Sites ◽  
Peritoneal Macrophages ◽  
Untreated Mouse ◽  
Mouse Peritoneal Macrophages

Untreated mouse peritoneal macrophages as well as macrophages treated with concanavalin A (ConA) were incubated in the presence of untreated or ConA-treated epimastigotes and trypomastigotes of Trypanosoma cruzi. Treatment of epimastigotes or trypomastigotes with ConA increased or decreased their uptake by macrophages, respectively. Treatment of their macrophages with ConA reduced by 70% and increased by five times the ingestion of epimastigotes and trypomastigotes, respectively. These results are discussed in relation to previous studies on the mobility of ConA receptors in the membrane of the parasite. Using fluorescein- or ferritin-labelled ConA we observed that ConA binding sites located on the plasma membrane of macrophages are internalized during endocytosis of T. cruzi, and observed in association with the membrane of the endocytic vacuole. Vacuoles without parasites showed a uniform distribution of ConA binding sites, while these sites were distributed in patches in vacuoles containing parasites. These results, in association with others previously reported, suggest the involvement of glycoproteins and/or glycolipids localized on the cell surface of T. cruzi and macrophages during the T. cruzi-macrophage interaction.

scholarly journals Characterization of the plasma-membrane calcium pump from Trypanosoma cruzi

1995 ◽  
Vol 306 (1) ◽  
pp. 299-303 ◽  
Author(s):  
G Benaim ◽  
S N J Moreno ◽  
G Hutchinson ◽  
V Cervino ◽  
T Hermoso ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Mammalian Cells ◽  
Membrane Vesicles ◽  
High Sensitivity ◽  
Bovine Brain ◽  
Calcium Pump ◽  
Plasma Membrane Vesicles ◽  
P Type

Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh, Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca(2+)-ATPases of different trypanosomatids differ from the Ca2+ pumps present in mammalian cells, Trypanosoma cruzi plasma-membrane Ca(2+)-ATPase shares several characteristics with the Ca2+ pumps present in other systems. This enzyme could be partially purified from epimastigote plasma-membrane vesicles using calmodulin-agarose affinity chromatography. The activity of the partially purified enzyme was stimulated by T. cruzi or bovine brain calmodulin. In addition, the enzyme cross-reacted with antiserum and monoclonal antibody 5F10 raised against human red-blood-cell Ca(2+)-ATPase, has a molecular mass of 140 kDa and forms Ca(2+)-dependent hydroxylamine-sensitive phosphorylated intermediates. These results, together with its high sensitivity to vanadate, indicate that this enzyme belongs to the P-type class of ionic pumps.

scholarly journals Lysosomal Fusion Is Essential for the Retention of Trypanosoma cruzi Inside Host Cells

2004 ◽  
Vol 200 (9) ◽  
pp. 1135-1143 ◽  
Author(s):  
Luciana O. Andrade ◽  
Norma W. Andrews
Keyword(s):  
Plasma Membrane ◽  
Life Cycle ◽  
Trypanosoma Cruzi ◽  
Parasitophorous Vacuole ◽  
Cell Types ◽  
Significant Fraction ◽  
Host Cells ◽  
Productive Infection ◽  
Kinase Inhibition

Trypomastigotes, the highly motile infective forms of Trypanosoma cruzi, are capable of infecting several cell types. Invasion occurs either by direct recruitment and fusion of lysosomes at the plasma membrane, or through invagination of the plasma membrane followed by intracellular fusion with lysosomes. The lysosome-like parasitophorous vacuole is subsequently disrupted, releasing the parasites for replication in the cytosol. The role of this early residence within lysosomes in the intracellular cycle of T. cruzi has remained unclear. For several other cytosolic pathogens, survival inside host cells depends on an early escape from phagosomes before lysosomal fusion. Here, we show that when lysosome-mediated T. cruzi invasion is blocked through phosophoinositide 3-kinase inhibition, a significant fraction of the internalized parasites are not subsequently retained inside host cells for a productive infection. A direct correlation was observed between the lysosomal fusion rates after invasion and the intracellular retention of trypomastigotes. Thus, formation of a parasitophorous vacuole with lysosomal properties is essential for preventing these highly motile parasites from exiting host cells and for allowing completion of the intracellular life cycle.

scholarly journals Trypanosoma cruzi modulates gene expression of plasma membrane repair-related proteins

Acta Tropica ◽  
2017 ◽  
Vol 174 ◽  
pp. 153-157 ◽  
Author(s):  
Rebecca Tavares e Silva Brígido ◽  
Paula Cristina Brígido Tavares ◽  
Marlus Alves dos Santos ◽  
Júlia de Gouveia Santos ◽  
Maria Aparecida de Souza ◽  
...  
Keyword(s):  
Gene Expression ◽  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Membrane Repair ◽  
Plasma Membrane Repair ◽  
Related Proteins

Antimicrobial peptides isolated from Phyllomedusa nordestina (Amphibia) alter the permeability of plasma membrane of Leishmania and Trypanosoma cruzi

2013 ◽  
Vol 135 (4) ◽  
pp. 655-660 ◽  
Author(s):  
Erika Gracielle Pinto ◽  
Daniel C. Pimenta ◽  
Marta Maria Antoniazzi ◽  
Carlos Jared ◽  
Andre Gustavo Tempone
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Antimicrobial Peptides

scholarly journals Role for a P-type H+-ATPase in the acidification of the endocytic pathway of Trypanosoma cruzi

2005 ◽  
Vol 392 (3) ◽  
pp. 467-474 ◽  
Author(s):  
Mauricio Vieira ◽  
Peter Rohloff ◽  
Shuhong Luo ◽  
Narcisa L. Cunha-E-Silva ◽  
Wanderley De Souza ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Trypanosoma Cruzi ◽  
Subcellular Fractionation ◽  
Etiologic Agent ◽  
Proton Pumping ◽  
Endocytic Pathway ◽  
Immunogold Electron Microscopy ◽  
Intermediate Form ◽  
Confocal Immunofluorescence Microscopy ◽  
P Type

Previous studies in Trypanosoma cruzi, the etiologic agent of Chagas disease, have resulted in the cloning and sequencing of a pair of tandemly linked genes (TcHA1 and TcHA2) that encode P (phospho-intermediate form)-type H+-ATPases with homology to fungal and plant proton-pumping ATPases. In the present study, we demonstrate that these pumps are present in the plasma membrane and intracellular compartments of three different stages of T. cruzi. The main intracellular compartment containing these ATPases in epimastigotes was identified as the reservosome. This identification was achieved by immunofluorescence assays and immunoelectron microscopy showing their co-localization with cruzipain, and by subcellular fractionation and detection of their activity. ATP-dependent proton transport by isolated reservosomes was sensitive to vanadate and insensitive to bafilomycin A1, which is in agreement with the localization of P-type H+-ATPases in these organelles. Analysis by confocal immunofluorescence microscopy revealed that epitope–tagged TcHA1-Ty1 and TcHA2-Ty1 gene products are localized in the reservosomes, whereas the TcHA1-Ty1 gene product is additionally present in the plasma membrane. Immunogold electron microscopy showed the presence of the H+-ATPases in other compartments of the endocytic pathway such as the cytostome and endosomal vesicles, suggesting that in contrast with most cells investigated until now, the endocytic pathway of T. cruzi is acidified by a P-type H+-ATPase.

A proton pumping pyrophosphatase in the Golgi apparatus and plasma membrane vesicles of Trypanosoma cruzi

2002 ◽  
Vol 120 (2) ◽  
pp. 205-213 ◽  
Author(s):  
Rosa Martinez ◽  
Youhong Wang ◽  
Gustavo Benaim ◽  
Marlene Benchimol ◽  
Wanderley de Souza ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Trypanosoma Cruzi ◽  
Membrane Vesicles ◽  
Proton Pumping ◽  
Plasma Membrane Vesicles
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