Correction: BILBO1 Is a Scaffold Protein of the Flagellar Pocket Collar in the Pathogen Trypanosoma brucei

Florimond, Célia; Sahin, Annelise; Vidilaseris, Keni; Dong, Gang; Landrein, Nicolas; Dacheux, Denis; Albisetti, Anna; Byard, Edward H.; Bonhivers, Mélanie; Robinson, Derrick R.

doi:10.1371/journal.ppat.1004844

Cited by 3 publications

(13 citation statements)

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“…As protein expression in heterologous cells can help to decipher localizations 20 , we used this strategy to first prove the specificity of our antibodies. U-2 OS cells do not possess any TcoClec orthologs and are well-suited for heterologous expression of trypanosomal proteins 21 22 23 . From Figure 2, it can be seen that our antibodies react only with transfected cells, whereas the control marker (calnexin) is detected in all cells.…”

Section: Resultsmentioning

confidence: 99%

“…Exponentially growing cells were transfected with 250 ng DNA (TcoClec or control) using Lipofectamine 2000 in OPTIMEM (Invitrogen) according to the manufacturer's instructions and processed for IFA 24 h post-transfection. To control transfection efficiency, the pcDNA3.1 Bilbo plasmid was used 22 . A transfection without DNA was used as negative control.…”

Section: Methodsmentioning

confidence: 99%

“…For whole-cell and « shaving » experiments, trypanosomes were fixed with paraformaldehyde (PFA, 3%) as described elsewhere 22 .…”

Section: Methodsmentioning

confidence: 99%

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A multigene family encoding surface glycoproteins in Trypanosoma congolense

2017

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Trypanosoma congolense, the causative agent of the most important livestock disease in Africa, expresses specific surface proteins involved in its parasitic lifestyle. Unfortunately, the complete repertoire of such molecules is far from being deciphered. As these membrane components are exposed to the host environment, they could be used as therapeutic or diagnostic targets. By mining the T. congolense genome database, we identified a novel family of lectin-like glycoproteins (TcoClecs). These molecules are predicted to have a transmembrane domain, a tandem repeat amino acid motif, a signal peptide and a C-type lectin-like domain (CTLD). This paper depicts several experimental arguments in favor of a surface localization in bloodstream forms of T. congolense. A TcoClec gene was heterologously expressed in U-2 OS cells and the product could be partially found at the plasma membrane. TcoClecs were also localized at the surface of T. congolense bloodstream forms. The signal was suppressed when the cells were treated with a detergent to remove the plasma membrane or with trypsin to « shave » the parasites and remove their external proteins. This suggests that TcoClecs could be potential diagnostic or therapeutic antigens of African animal trypanosomiasis. The potential role of these proteins in T. congolense as well as in other trypanosomatids is discussed.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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A multigene family encoding surface glycoproteins in Trypanosoma congolense

2017

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“…In T. brucei the FP is essential for survival and this has been demonstrated through studies of an FP-linked cytoskeleton component called the flagellar pocket collar (FPC). The FPC is a cytoskeletal structure that circumvents the neck of the FP at the site where the flagellum exits the cell (13,(20)(21)(22)(23)(24)(25)(26). The FPC forms a cytoskeletal boundary or interface at the site of contact between the pellicular, flagellar and FP membranes (13,20,(23)(24)(25)(26).…”

Section: Introductionmentioning

confidence: 99%

“…The FPC is a cytoskeletal structure that circumvents the neck of the FP at the site where the flagellum exits the cell (13,(20)(21)(22)(23)(24)(25)(26). The FPC forms a cytoskeletal boundary or interface at the site of contact between the pellicular, flagellar and FP membranes (13,20,(23)(24)(25)(26). To (which was not certified by peer review) is the author/funder.…”

Section: Introductionmentioning

confidence: 99%

Intrabody induced cell death by targeting theT. bruceicytoskeletal proteinTbBILBO1

Broster-Reix

Ramanantsalama

Primo

et al. 2021

Preprint

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Trypanosoma brucei belongs to a genus of protists that cause life-threatening and economically important diseases of human and animal populations in Sub-Saharan Africa. T. brucei cells are covered in surface glycoproteins some of which are used to escape the host immune system. Exo-/endocytotic trafficking of these and other molecules occurs via a single copy organelle called the flagellar pocket (FP). The FP is maintained and enclosed around the flagellum by the flagellar pocket collar (FPC). To date, the most important cytoskeletal component of the FPC is an essential, calcium-binding, polymer-forming protein called TbBILBO1. In searching for novel immune-tools to study this protein, we raised nanobodies against TbBILBO1. Nanobodies (Nb) that were selected according to their binding properties to TbBILBO1, were tested as immunofluorescence tools, and expressed as intrabodies (INb). One of them, Nb48, proved to be the most robust nanobody and intrabody. We further demonstrate that inducible, cytoplasmic expression of INb48 was lethal to these parasites, producing abnormal phenotypes resembling those of TbBILBO1 RNAi knockdown.; Our results validate the feasibility of generating functional single-domain antibody derived intrabodies to target trypanosome cytoskeleton proteins.

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TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

et al. 2022

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The flagellar pocket (FP) of the pathogen Trypanosoma brucei is an important single copy structure that is formed by the invagination of the pellicular membrane. It is the unique site of endo- and exocytosis and is required for parasite pathogenicity. The FP consists of distinct structural sub-domains with the least explored being the flagellar pocket collar (FPC). TbBILBO1 is the first-described FPC protein of Trypanosoma brucei. It is essential for parasite survival, FP and FPC biogenesis. In this work, we characterize TbKINX1B, a novel TbBILBO1 partner. We demonstrate that TbKINX1B is located on the basal bodies, the microtubule quartet (a set of four microtubules) and the FPC in T. brucei. Down-regulation of TbKINX1B by RNA interference in bloodstream forms is lethal, inducing an overall disturbance in the endomembrane network. In procyclic forms, the RNAi knockdown of TbKINX1B leads to a minor phenotype with a small number of cells displaying epimastigote-like morphologies, with a misplaced kinetoplast. Our results characterize TbKINX1B as the first putative kinesin to be localized both at the basal bodies and the FPC with a potential role in transporting cargo along with the microtubule quartet.

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Correction: BILBO1 Is a Scaffold Protein of the Flagellar Pocket Collar in the Pathogen Trypanosoma brucei

Cited by 3 publications

References 1 publication

A multigene family encoding surface glycoproteins in Trypanosoma congolense

A multigene family encoding surface glycoproteins in Trypanosoma congolense

Intrabody induced cell death by targeting theT. bruceicytoskeletal proteinTbBILBO1

TbKINX1B: a novel BILBO1 partner and an essential protein in bloodstream form Trypanosoma brucei

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