Elemental composition of acidocalcisomes of Trypanosoma cruzi bloodstream trypomastigote forms

Corrêa, Alexandre F.S.; Andrade, Leonardo R.; Soares, Maurílio J.

doi:10.1007/s00436-002-0670-z

Cited by 18 publications

(8 citation statements)

References 39 publications

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“…Several acidocalcisome proteins of other trypanosomatids or with potential localization to acidocalcisomes were also investigated. Since iron has been detected in acidocalcisomes of T. cruzi [47] , Phytomonas spp. [48] , [49] , and Leishmania amazonensis [50] , we tagged a hypothetical protein (Tb927.3.800) with similarity to vacuolar iron transporters (VIT).…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of the Acidocalcisome, an Organelle Conserved from Bacteria to Human Cells

et al. 2014

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Acidocalcisomes are acidic organelles present in a diverse range of organisms from bacteria to human cells. In this study acidocalcisomes were purified from the model organism Trypanosoma brucei, and their protein composition was determined by mass spectrometry. The results, along with those that we previously reported, show that acidocalcisomes are rich in pumps and transporters, involved in phosphate and cation homeostasis, and calcium signaling. We validated the acidocalcisome localization of seven new, putative, acidocalcisome proteins (phosphate transporter, vacuolar H+-ATPase subunits a and d, vacuolar iron transporter, zinc transporter, polyamine transporter, and acid phosphatase), confirmed the presence of six previously characterized acidocalcisome proteins, and validated the localization of five novel proteins to different subcellular compartments by expressing them fused to epitope tags in their endogenous loci or by immunofluorescence microscopy with specific antibodies. Knockdown of several newly identified acidocalcisome proteins by RNA interference (RNAi) revealed that they are essential for the survival of the parasites. These results provide a comprehensive insight into the unique composition of acidocalcisomes of T. brucei, an important eukaryotic pathogen, and direct evidence that acidocalcisomes are especially adapted for the accumulation of polyphosphate.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of the Acidocalcisome, an Organelle Conserved from Bacteria to Human Cells

et al. 2014

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“…Using Xray microanalysis, oxygen, magnesium, phosphorus, sodium, potassium, zinc, and calcium were detected in acidocalcisomes of different stages of T. cruzi [4,5] while iron was also found in acidocalcisomes of the bloodstream forms [6]. T. cruzi acidocalcisomes have high levels of phosphorus in the form of inorganic pyrophosphate (PP i ) and polyphosphate (poly P) [7].…”

Section: Introductionmentioning

confidence: 99%

Phospholipid and glycolipid composition of acidocalcisomes of Trypanosoma cruzi

Salto

Kuhlenschmidt

et al. 2008

Molecular and Biochemical Parasitology

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Highly purified acidocalcisomes from Trypanosoma cruzi epimastigotes were obtained by differential centrifugation and iodixanol gradient ultracentrifugation. Lipid analysis of acidocalcisomes revealed the presence of low amounts of 3β-hydroxysterols and predominance of phospholipids. Alkylacyl phosphatidylinositol (16:0/18:2), diacyl phosphatidylinositol (18:0/18:2), diacyl phosphatidylcholine (16:0/18:2; 16:1/18:2; 16:2/18:2, 18:1/18:2, and 18:2/18:2), and diacyl phosphatidylethanolamine (16:0/18:2 and 16:1/18:2) were the only phospholipids characterized by electrospray ionization-mass spectrometry (ESI-MS). Incubation of epimastigotes with [ 3 H]-mannose and isolation of acidocalcisomes allowed the detection of a glycoinositolphospholipid (GIPL) in these organelles. The sugar content of the acidocalcisomal GIPL was similar to that of the GIPL present in a microsomal fraction but the amount of galactofuranose and inositol with respect to the other monosaccharides was lower, suggesting a different chemical structure. Taken together, these results indicate that acidocalcisomes of T. cruzi have a distinct lipid and carbohydrate composition.

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“…The low expression level observed in T. cruzi trypomastigotes may be related to the low endocytic activity observed for this stage [26], as opposed to the high endocytic activity found in T. brucei bloodstream trypomastigotes [27]. …”

Section: Discussionmentioning

confidence: 99%

Clathrin expression in Trypanosoma cruzi

et al. 2014

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BackgroundClathrin-mediated vesicular trafficking, the mechanism by which proteins and lipids are transported between membrane-bound organelles, accounts for a large proportion of import from the plasma membrane (endocytosis) and transport from the trans-Golgi network towards the endosomal system. Clathrin-mediated events are still poorly understood in the protozoan Trypanosoma cruzi, the causative agent of Chagas disease in Latin America. In this study, clathrin heavy (TcCHC) and light (TcCLC) chain gene expression and protein localization were investigated in different developmental forms of T. cruzi (epimastigotes, trypomastigotes and amastigotes), using both polyclonal and monoclonal antibodies raised against T. cruzi recombinant proteins.ResultsAnalysis by confocal microscopy revealed an accumulation of TcCHC and TcCLC at the cell anterior, where the flagellar pocket and Golgi complex are located. TcCLC partially colocalized with the Golgi marker TcRAB7-GFP and with ingested albumin, but did not colocalize with transferrin, a protein mostly ingested via uncoated vesicles at the cytostome/cytopharynx complex.ConclusionClathrin heavy and light chains are expressed in T. cruzi. Both proteins typically localize anterior to the kinetoplast, at the flagellar pocket and Golgi complex region. Our data also indicate that in T. cruzi epimastigotes clathrin-mediated endocytosis of albumin occurs at the flagellar pocket, while clathrin-independent endocytosis of transferrin occurs at the cytostome/cytopharynx complex.

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Elemental composition of acidocalcisomes of Trypanosoma cruzi bloodstream trypomastigote forms

Cited by 18 publications

References 39 publications

Proteomic Analysis of the Acidocalcisome, an Organelle Conserved from Bacteria to Human Cells

Proteomic Analysis of the Acidocalcisome, an Organelle Conserved from Bacteria to Human Cells

Phospholipid and glycolipid composition of acidocalcisomes of Trypanosoma cruzi

Clathrin expression in Trypanosoma cruzi

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