TY  - JOUR
A1  - Broster Reix, Christine E.
A1  - Florimond, Célia
A1  - Cayrel, Anne
A1  - Mailhé, Amélie
A1  - Agnero-Rigot, Corentin
A1  - Landrein, Nicolas
A1  - Dacheux, Denis
A1  - Havlicek, Katharina
A1  - Bonhivers, Mélanie
A1  - Morriswood, Brooke
A1  - Robinson, Derrick R.
T1  - Bhalin, an essential cytoskeleton-associated protein of Trypanosoma brucei linking TbBILBO1 of the flagellar pocket collar with the hook complex
JF  - Microorganisms
N2  - Background: In most trypanosomes, endo and exocytosis only occur at a unique organelle called the flagellar pocket (FP) and the flagellum exits the cell via the FP. Investigations of essential cytoskeleton-associated structures located at this site have revealed a number of essential proteins. The protein TbBILBO1 is located at the neck of the FP in a structure called the flagellar pocket collar (FPC) and is essential for biogenesis of the FPC and parasite survival. TbMORN1 is a protein that is present on a closely linked structure called the hook complex (HC) and is located anterior to and overlapping the collar. TbMORN1 is essential in the bloodstream form of T. brucei. We now describe the location and function of BHALIN, an essential, new FPC-HC protein. Methodology/Principal Findings: Here, we show that a newly characterised protein, BHALIN (BILBO1 Hook Associated LINker protein), is localised to both the FPC and HC and has a TbBILBO1 binding domain, which was confirmed in vitro. Knockdown of BHALIN by RNAi in the bloodstream form parasites led to cell death, indicating an essential role in cell viability. Conclusions/Significance: Our results demonstrate the essential role of a newly characterised hook complex protein, BHALIN, that influences flagellar pocket organisation and function in bloodstream form T. brucei parasites.
KW  - trypanosoma
KW  - flagellar pocket
KW  - hook complex
KW  - endocytosis
KW  - cytoskeleton
KW  - protozoan
KW  - flagellar pocket collar
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-250301
SN  - 2076-2607
VL  - 9
IS  - 11
ER  - 
TY  - JOUR
A1  - Link, Fabian
A1  - Borges, Alyssa R.
A1  - Jones, Nicola G.
A1  - Engstler, Markus
T1  - To the Surface and Back: Exo- and Endocytic Pathways in Trypanosoma brucei
JF  - Frontiers in Cell and Developmental Biology
N2  - Trypanosoma brucei is one of only a few unicellular pathogens that thrives extracellularly in the vertebrate host. Consequently, the cell surface plays a critical role in both immune recognition and immune evasion. The variant surface glycoprotein (VSG) coats the entire surface of the parasite and acts as a flexible shield to protect invariant proteins against immune recognition. Antigenic variation of the VSG coat is the major virulence mechanism of trypanosomes. In addition, incessant motility of the parasite contributes to its immune evasion, as the resulting fluid flow on the cell surface drags immunocomplexes toward the flagellar pocket, where they are internalized. The flagellar pocket is the sole site of endo- and exocytosis in this organism. After internalization, VSG is rapidly recycled back to the surface, whereas host antibodies are thought to be transported to the lysosome for degradation. For this essential step to work, effective machineries for both sorting and recycling of VSGs must have evolved in trypanosomes. Our understanding of the mechanisms behind VSG recycling and VSG secretion, is by far not complete. This review provides an overview of the trypanosome secretory and endosomal pathways. Longstanding questions are pinpointed that, with the advent of novel technologies, might be answered in the near future.
KW  - cell surface
KW  - African trypanosomes
KW  - endocytosis
KW  - exocytosis
KW  - membrane recycling
KW  - Rab
KW  - clathrin
Y1  - 2021
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-244682
SN  - 2296-634X
VL  - 9
ER  -