scholarly journals A cell-body groove housing the new flagellum tip suggests an adaptation of cellular morphogenesis for parasitism in the bloodstream form of Trypanosoma brucei

2013 ◽  
Vol 126 (24) ◽  
pp. 5748-5757 ◽  
Author(s):  
Louise Hughes ◽  
Katie Towers ◽  
Tobias Starborg ◽  
Keith Gull ◽  
Sue Vaughan
Keyword(s):  
Trypanosoma Brucei ◽  
Cell Body ◽  
Bloodstream Form ◽  
Cellular Morphogenesis ◽  
A Cell

Synthesis of a cell-permeable analogue of a glycosylphosphatidylinositol (GPI) intermediate that is toxic to the living bloodstream form of Trypanosoma brucei

2005 ◽  
Vol 46 (43) ◽  
pp. 7419-7421 ◽  
Author(s):  
Arthur Crossman ◽  
Terry K. Smith ◽  
Michael A.J. Ferguson ◽  
John S. Brimacombe
Keyword(s):  
Trypanosoma Brucei ◽  
Bloodstream Form ◽  
A Cell

scholarly journals Flagellar adhesion in Trypanosoma brucei relies on interactions between different skeletal structures in the flagellum and cell body

2013 ◽  
Vol 127 (1) ◽  
pp. 204-215 ◽  
Author(s):  
B. Rotureau ◽  
T. Blisnick ◽  
I. Subota ◽  
D. Julkowska ◽  
N. Cayet ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Cell Body ◽  
Skeletal Structures

scholarly journals The endoplasmic reticulum-associated mRNA-binding proteins ERBP1 and ERBP2 interact in bloodstream-form Trypanosoma brucei

2019 ◽  
Author(s):  
Kathrin Bajak ◽  
Kevin Leiss ◽  
Christine Clayton ◽  
Esteban Erben
Keyword(s):  
Endoplasmic Reticulum ◽  
Ribosomal Protein ◽  
Trypanosoma Brucei ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Bloodstream Form ◽  
Control Of Gene Expression ◽  
Mrna Binding Proteins ◽  
Mrna Binding

AbstractKinetoplastids rely heavily on post-transcriptional mechanisms for control of gene expression, and on RNA-binding proteins that regulate mRNA splicing, translation and decay. Trypanosoma brucei ERBP1 (Tb927.10.14150) and ERBP2 (Tb927.9.9550) were previously identified as mRNA binding proteins that lack canonical RNA-binding domains. We here show that ERBP1 is associated with the endoplasmic reticulum, like ERBP2, and that the two proteins interact in vivo. Loss of ERBP1 from bloodstream-form T. brucei initially resulted in a growth defect but proliferation was restored after more prolonged cultivation. Results from a pull-down of tagged ERBP1 suggest that it preferentially binds to ribosomal protein mRNAs. The ERBP1 sequence resembles that of Saccharomyces cerevisiae Bfr1, which also localises to the endoplasmic reticulum and binds to ribosomal protein mRNAs. However, unlike Bfr1, ERBP1 does not bind to mRNAs encoding secreted proteins, and it is also not recruited to stress granules after starvation.

A gene from the variant surface glycoprotein expression site encodes one of several transmembrane adenylate cyclases located on the flagellum of Trypanosoma brucei

1992 ◽  
Vol 12 (3) ◽  
pp. 1218-1225
Author(s):  
P Paindavoine ◽  
S Rolin ◽  
S Van Assel ◽  
M Geuskens ◽  
J C Jauniaux ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Trypanosoma Brucei ◽  
Membrane Fraction ◽  
Transcription Unit ◽  
Bloodstream Form ◽  
Surface Glycoprotein ◽  
Yeast Cells ◽  
Variant Surface Glycoprotein ◽  
Polycistronic Transcription ◽  
Expression Site

The bloodstream form of Trypanosoma brucei contains transcripts of at least four genes showing partial sequence homology to the genes for eucaryotic adenylate and guanylate cyclases (S. Alexandre, P. Paindavoine, P. Tebabi, A. Pays, S. Halleux, M. Steinert, and E. Pays, Mol. Biochem. Parasitol. 43:279-288, 1990). One of these genes, termed ESAG 4, belongs to the polycistronic transcription unit of the variant surface glycoprotein (VSG) gene. Whereas ESAG 4 is transcribed only in the bloodstream form of the parasite, the three other genes, GRESAG 4.1, 4.2, and 4.3, are also expressed in procyclic (insect) forms. These genes differ primarily in a region presumed to encode a large extracellular domain. We show here that ESAG 4-related glycoproteins of about 150 kDa can be found in the trypanosome membrane, that they are detected, by light and electron gold immunocytochemistry, only at the surface of the flagellum, and that the products of at least two of these genes, ESAG 4 and GRESAG 4.1, can complement a Saccharomyces cerevisiae mutant for adenylate cyclase. The recombinant cyclases are associated with the yeast membrane fraction and differ with respect to their activation by calcium: while the GRESAG 4.1 and yeast cyclases are inhibited by calcium, the ESAG 4 cyclase is stimulated. ESAG 4 thus most probably encodes the calcium-activated cyclase that has been found to be expressed only in the bloodstream form of T. brucei (S. Rolin, S. Halleux, J. Van Sande, J. E. Dumont, E. Pays, and M. Steinert. Exp. Parasitol. 71:350-352, 1990). Our data suggest that the trypanosome cyclases are not properly regulated in yeast cells.

scholarly journals Precision Calcium Imaging of Dense Neural Populations via a Cell-Body-Targeted Calcium Indicator

Neuron ◽  
2020 ◽  
Vol 107 (3) ◽  
pp. 470-486.e11 ◽  
Author(s):  
Or A. Shemesh ◽  
Changyang Linghu ◽  
Kiryl D. Piatkevich ◽  
Daniel Goodwin ◽  
Orhan Tunc Celiker ◽  
...  
Keyword(s):  
Cell Body ◽  
Calcium Imaging ◽  
Calcium Indicator ◽  
Neural Populations ◽  
A Cell

scholarly journals Kinetic study of the plasma-membrane potential in procyclic and bloodstream forms of Trypanosoma brucei brucei using the fluorescent probe bisoxonol

1996 ◽  
Vol 314 (2) ◽  
pp. 595-601 ◽  
Author(s):  
Fabienne DEFRISE-QUERTAIN ◽  
Chantal FRASER-L'HOSTIS ◽  
Danièle CORAL ◽  
Jacques DESHUSSES
Keyword(s):  
Plasma Membrane ◽  
Membrane Potential ◽  
Trypanosoma Brucei ◽  
Cultured Cells ◽  
Bloodstream Form ◽  
Metabolic Inhibitors ◽  
Trypanosoma Brucei Brucei ◽  
Plasma Membrane Potential ◽  
Regulation Mechanisms ◽  
K Concentration

The characteristics of the plasma-membrane potential of procyclic and bloodstream forms of Trypanosoma brucei brucei (cultured cells) were investigated using the fluorescent anionic probe bisoxonol. Observation of a stable and representative plasma-membrane potential in the resting state required careful washing, centrifugation and maintenance of the cells at room temperature before measurement. Bloodstream forms were more prone to depolarization during washing at 4 °C than procyclic cells. The higher fluorescence observed in the presence of long slender cells than in the presence of procyclic cells shows that the plasma-membrane potential is more negative in the insect form. Healthy dilute cells can sustain their plasma-membrane potential for hours in the presence of external glucose. The presence of a high K+ concentration in the medium did not promote by itself the depolarization of either type of cell. Study of bisoxonol fluorescence as a function of time allowed us to follow the kinetics of the action of metabolic inhibitors in the presence of various ions. o-Vanadate (1 mM) was found to depolarize bloodstream-form cells rapidly but only in a phosphate-free NaCl buffer. Omeprazole and strophanthidin also specifically depolarized bloodstream-form trypanosomes. However, NN´-dicyclohexylcarbodi-imide depolarized both types of cell, but more rapidly for bloodstream-form cells. Bloodstream-form trypanosomes appear to use mainly a vanadate-sensitive Na+ pump to maintain their Na+-diffusion gradient. However, most of the ATPase inhibitors tested had little or no effect on the plasma-membrane potential of procyclics suggesting that this form of trypanosome may rely on several regulation mechanisms.

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