BILBO1 Is a Scaffold Protein of the Flagellar Pocket Collar in the Pathogen

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Trypanosoma brucei avoids destruction by, in part, changing its surface glycoprotein coat, which is trafficked onto the cell surface via an invagination of the cell surface called the flagellar pocket. The pocket is essential for pathogenicity. The distal membrane of the pocket is anchored to a cytoskeleton structure called the flagellar pocket collar (FPC). The FPC is a ring/horseshoe shaped structure, which itself is attached to the single copy flagellum of the parasite. How the “ring” shape of the collar is formed is not understood. Moreover, the only known protein component of the FPC is the protein BILBO1. BILBO1 is modular and has a distinct N-terminal domain, two EF-hand calcium-binding domains and a large C-terminal coiled-coil domain. Here we demonstrate that mutating the EF hand domains prevent calcium binding and that the coiled-coil domain is not only sufficient to target to the collar, but can also form polymers in mammalian cells. Mutating either or both calcium-binding domains of BILBO1 influences polymer formation and type when expressed in mammalian and trypanosome cells. Our premise is that BILBO1 has intrinsic polymer forming properties that are essential for the flagellar pocket collar making the pocket a target for intervention.

Vyšlo v časopise: BILBO1 Is a Scaffold Protein of the Flagellar Pocket Collar in the Pathogen. PLoS Pathog 11(3): e32767. doi:10.1371/journal.ppat.1004654
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004654

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