VIDILASERIS, Keni; LANDREIN, Nicolas; PIVOVAROVA, Yulia; LESIGANG, Johannes; AEKSIRI, Niran; ROBINSON, Derrick; BONHIVERS, Melanie; DONG, Gang

doi:10.1074/jbc.RA119.010768

LANDREIN, Nicolas
Microbiologie Fondamentale et Pathogénicité [MFP]

PIVOVAROVA, Yulia

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Article de revue

Ce document a été publié dans

Journal of Biological Chemistry. 2020, vol. 295, n° 6, p. 1489-1499

Résumé en anglais

Trypanosoma brucei is a protist parasite causing sleeping sickness and nagana in sub-Saharan Africa. T. brucei has a single flagellum whose base contains a bulblike invagination of the plasma membrane called the flagellar pocket (FP). Around the neck of the FP on its cytoplasmic face is a structure called the flagellar pocket collar (FPC), which is essential for FP biogenesis. BILBO1 was the first characterized component of the FPC in trypanosomes. BILBO1's N-terminal domain (NTD) plays an essential role in T. brucei FPC biogenesis and is thus vital for the parasite's survival. Here, we report a 1.6-Å resolution crystal structure of TbBILBO1-NTD, which revealed a conserved horseshoe-like hydrophobic pocket formed by an unusually long loop. Results from mutagenesis experiments suggested that another FPC protein, FPC4, interacts with TbBILBO1 by mainly contacting its three conserved aromatic residues Trp-71, Tyr-87, and Phe-89 at the center of this pocket. Our findings disclose the binding site of TbFPC4 on TbBILBO1-NTD, which may provide a basis for rational drug design targeting BILBO1 to combat T. brucei infections.< Réduire

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https://oskar-bordeaux.fr/handle/20.500.12278/182399

DOI

http://dx.doi.org/10.1074/jbc.RA119.010768

Project ANR

Alliance française contre les maladies parasitaires - ANR-11-LABX-0024

Unités de recherche

MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234

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Crystal structure of the N-terminal domain of the trypanosome flagellar protein BILBO1 reveals a ubiquitin fold with a long structured loop for protein binding

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