Invariant surface proteins in bloodstream forms of Trypanosoma brucei

Overath, Peter; Chaudhri, M.; Steverding, Dietmar; Ziegelbauer, Karl

doi:10.1016/0169-4758(94)90393-x

Cited by 76 publications

(55 citation statements)

References 37 publications

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“…One of the most important characteristics of the salivarian trypanosomes is their capacity to modify their surface coat during the course of infection (Overath et al 1994). The African trypanosomes variant surface coat (VSG) is reported to be a single 10-15 nm thick coat of glycoproteins with a MW Fig.…”

Section: Discussionmentioning

confidence: 99%

Specific antibody levels and antigenic recognition of Wistar rats inoculated with distinct isolates of Trypanosoma evansi

Queiroz

Legey

Xavier

et al. 2001

Mem. Inst. Oswaldo Cruz

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Section: Discussionmentioning

confidence: 99%

Specific antibody levels and antigenic recognition of Wistar rats inoculated with distinct isolates of Trypanosoma evansi

Queiroz

Legey

Xavier

et al. 2001

Mem. Inst. Oswaldo Cruz

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“…As 90% of the total surface glycoprotein in trypanosomes is the variant surface glycoprotein (VSG), and hence VSG is the overwhelming mannose-containing surface macromolecule, uptake of the mannose-binding lectin concanavalin A (ConA) mainly reports on VSG endocytosis (Overath et al, 1994;Cross, 1996;Mehlert et al, 2002;Allen et al, 2003). To address a possible role for Rab28 in surface protein endocytosis, we monitored ConA accumulation in T. brucei Rab28…”

Section: Rab28 Function In Endocytosis 3773mentioning

confidence: 99%

Rab28 function in trypanosomes: interactions with retromer and ESCRT pathways

Lumb

Leung

DuBois

et al. 2011

Journal of Cell Science

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SummaryEarly endosomal cargo is typically targeted to either a degradative or recycling pathway. Despite established functions for the retromer and ESCRT complexes at late endosomes/multivesicular bodies, the mechanisms integrating and coordinating these functions remain largely unknown. Rab family GTPases are key membrane trafficking organizers and could contribute. Here, in the unicellular organism Trypanosoma brucei, we demonstrate that Rab28 locates to the endosomal pathway and partially colocalizes with Vps23, an ESCRT I component. Rab28 is required for turnover of endocytosed proteins and for lysosomal delivery of protein cargo. Using RNA interference we find that in Rab28-depleted cells, protein levels of ESCRT I (Vps23/28) and retromer (Vps26) are also decreased, suggesting that Rab28 is an important regulator of these factors. We suggest that Rab28 coordinates the activity of retromer-dependent trafficking and ESCRT-mediated degradative pathways.

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“…The cisternae contain biotinylated VSG taken up by endocytosis from the cell surface (Overath et al, 1994;our unpublished data). A common feature of endosomal cisternae are coated, budding structures at their rims (Figure 4, A and B, arrows) but occasionally also on their planar face ( Figure 4C, arrow), which could be labeled by anti-clathrin antibodies.…”

Section: Clathrin-coated Vesicles Depleted In Vsg Bud From Endosomesmentioning

confidence: 99%

“…First, this and related flagellates abundantly express GPI-anchored proteins. T. brucei is covered by a dense coat of the GPIanchored variant surface glycoprotein (VSG), which comprises 10% of the total cellular protein (Overath et al, 1994;Cross, 1996). Sorting is effective, because the concentration of VSG at the cell surface is 50 times higher than in the endoplasmic reticulum (ER) (Grü nfelder et al, 2002), where the protein is synthesized and the lipid anchor is attached.…”

Section: Introductionmentioning

confidence: 99%

Endocytosis of a Glycosylphosphatidylinositol-anchored Protein via Clathrin-coated Vesicles, Sorting by Default in Endosomes, and Exocytosis via RAB11-positive Carriers

Grünfelder

Engstler

Weise

et al. 2003

MBoC

124

168

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Recently, proteins linked to glycosylphosphatidylinositol (GPI) residues have received considerable attention both for their association with lipid microdomains and for their specific transport between cellular membranes. Basic features of trafficking of GPI-anchored proteins or glycolipids may be explored in flagellated protozoan parasites, which offer the advantage that their surface is dominated by these components. In Trypanosoma brucei, the GPI-anchored variant surface glycoprotein (VSG) is efficiently sorted at multiple intracellular levels, leading to a 50-fold higher membrane concentration at the cell surface compared with the endoplasmic reticulum. We have studied the membrane and VSG flow at an invagination of the plasma membrane, the flagellar pocket, the sole region for endoand exocytosis in this organism. VSG enters trypanosomes in large clathrin-coated vesicles (135 nm in diameter), which deliver their cargo to endosomes. In the lumen of cisternal endosomes, VSG is concentrated by default, because a distinct class of small clathrin-coated vesicles (50 -60 nm in diameter) budding from the cisternae is depleted in VSG. TbRAB11-positive cisternal endosomes, containing VSG, fragment by an unknown process giving rise to intensely TbRAB11-as well as VSG-positive, disk-like carriers (154 nm in diameter, 34 nm in thickness), which are shown to fuse with the flagellar pocket membrane, thereby recycling VSG back to the cell surface.

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Invariant surface proteins in bloodstream forms of Trypanosoma brucei

Cited by 76 publications

References 37 publications

Specific antibody levels and antigenic recognition of Wistar rats inoculated with distinct isolates of Trypanosoma evansi

Specific antibody levels and antigenic recognition of Wistar rats inoculated with distinct isolates of Trypanosoma evansi

Rab28 function in trypanosomes: interactions with retromer and ESCRT pathways

Endocytosis of a Glycosylphosphatidylinositol-anchored Protein via Clathrin-coated Vesicles, Sorting by Default in Endosomes, and Exocytosis via RAB11-positive Carriers

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