Trypanosoma brucei rhodesiense: Membrane Glycoproteins Localized Primarily in Endosomes and Lysosomes of Bloodstream Forms

Brickman, Marla J.; Balber, Andrew E.

doi:10.1006/expr.1993.1041

Cited by 38 publications

(24 citation statements)

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“…Most of the untreated trypanosomes showed staining for rhodamine-labeled dextran (a bulk-phase endocytic marker) and p67 (a lysosomal membrane marker) in one to two vesicles located between the kinetoplast and the nucleus (Figure 4a and b), corresponding to the typical endosomal-lysosomal localization in trypanosomes. 10 VIP treatment progressively increased the number of dextran-containing and p67 þ vesicles, and B75% of trypanosomes had more than three lysosome-like vesicles after 4 h of treatment. This correlates with the increased cell complexity induced by VIP ( Figure 1c).…”

Section: Resultsmentioning

confidence: 97%

Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death

et al. 2008

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Trypanosoma brucei is the causative agent of African sleeping sickness. Available treatments are ineffective, toxic and susceptible to resistance by the parasite. Here we show that various endogenous neuropeptides act as potent antitrypanosome agents. Neuropeptides exerted their trypanolytic activity through an unusual mechanism that involves peptide uptake by the parasite, disruption of lysosome integrity and cytosolic accumulation of glycolytic enzymes. This promotes an energetic metabolism failure that initiates an autophagic-like cell death. Neuropeptide-based treatment improved clinical signs in a chronic model of trypanosomiasis by reducing the parasite burden in various target organs. Of physiological importance is the fact that hosts respond to trypanosome infection producing neuropeptides as part of their natural innate defense. From a therapeutic point of view, targeting of intracellular compartments by neuropeptides suppose a new promising strategy for the treatment of trypanosomiasis.

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Section: Resultsmentioning

confidence: 97%

Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death

et al. 2008

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“…5). We employed the uptake of tomato lectin at 37°C for 1 min as a marker for the flagellar pocket and early endosomes [36], Rab7 as a marker for the late endosomal compartment [37], [38] and the CB1 epitope of the lysosomal membrane glycoprotein p67 as a marker of the lysosomal compartment [39], [40]. There was some degree of colocalization of TbMyo1 with all of these compartments but a full overlap of the two signals was not observed with the possible exception of some of the smaller Rab7 positive compartments (see arrows Fig.…”

Section: Resultsmentioning

confidence: 99%

Identification and Characterization of an Unusual Class I Myosin Involved in Vesicle Traffic in Trypanosoma brucei

et al. 2010

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Myosins are a multimember family of motor proteins with diverse functions in eukaryotic cells. African trypanosomes possess only two candidate myosins and thus represent a useful system for functional analysis of these motors. One of these candidates is an unusual class I myosin (TbMyo1) that is expressed at similar levels but organized differently during the life cycle of Trypanosoma brucei. This myosin localizes to the polarized endocytic pathway in bloodstream forms of the parasite. This organization is actin dependent. Knock down of TbMyo1 results in a significant reduction in endocytic activity, a cessation in cell division and eventually cell death. A striking morphological feature in these cells is an enlargement of the flagellar pocket, which is consistent with an imbalance in traffic to and from the surface. In contrast TbMyo1 is distributed throughout procyclic forms of the tsetse vector and a loss of ∼90% of the protein has no obvious effects on growth or morphology. These results reveal a life cycle stage specific requirement for this myosin in essential endocytic traffic and represent the first description of the involvement of a motor protein in vesicle traffic in these parasites.

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“…Rabbit antiserum against T. brucei aldolase was kindly provided by Prof. Christine Clayton, ZMBH, Heidelberg, Germany. The monoclonal antibodies against T. brucei major lysosomal glycoprotein (CB1‐gp; clone CB1) [16] and against the procyclic acidic repetitive protein (PARP; clone TBRP1/247) were purchased from Cedarlane.…”

Section: Methodsmentioning

confidence: 99%

Ribonucleotide reductase is regulated via the R2 subunit during the life cycle of Trypanosoma brucei

2000

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We have examined the occurrence of the R1 and R2 subunits of ribonucleotide reductase during the life cycle of Trypanosoma brucei. Whereas the R1 protein is present throughout the life cycle, the R2 protein is not found in cell cycle-arrested short stumpy trypanosomes. RT-PCR/hybridization analysis revealed almost equal amounts of the R1 and R2 mRNAs in all life cycle stages of the parasite. The data indicate that ribonucleotide reductase of African trypanosomes is developmentally controlled by post-transcriptional regulation of the R2 subunit.z 2000 Federation of European Biochemical Societies.

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Trypanosoma brucei rhodesiense: Membrane Glycoproteins Localized Primarily in Endosomes and Lysosomes of Bloodstream Forms

Cited by 38 publications

References 0 publications

Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death

Neuropeptides kill African trypanosomes by targeting intracellular compartments and inducing autophagic-like cell death

Identification and Characterization of an Unusual Class I Myosin Involved in Vesicle Traffic in Trypanosoma brucei

Ribonucleotide reductase is regulated via the R2 subunit during the life cycle of Trypanosoma brucei

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