Interaction between the flagellar pocket collar and the hook complex via a novel microtubule-binding protein in Trypanosoma brucei.

Autor: Anna Albisetti, Célia Florimond, Nicolas Landrein, Keni Vidilaseris, Marie Eggenspieler, Johannes Lesigang, Gang Dong, Derrick Roy Robinson, Mélanie Bonhivers

Publikováno v: PLoS Pathogens, Vol 13, Iss 11, p e1006710 (2017)

Trypanosoma brucei belongs to a group of unicellular, flagellated parasites that are responsible for human African trypanosomiasis. An essential aspect of parasite pathogenicity is cytoskeleton remodelling, which occurs during the life cycle of the p

Externí odkaz: https://doaj.org/article/1c883b8988a746d1884e7028529545a9

BILBO1 is a scaffold protein of the flagellar pocket collar in the pathogen Trypanosoma brucei.

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

Publikováno v: PLoS Pathogens, Vol 11, Iss 3, p e1004654 (2015)

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

Externí odkaz: https://doaj.org/article/9f36e33b67ef408494190715810d4588

Functional and structural asymmetry suggest a unifying principle for catalysis in integral membrane-bound pyrophosphatases

Autor: Jannik Strauss, Craig Wilkinson, Keni Vidilaseris, Orquidea Ribeiro, Jianing Liu, James Hillier, Anssi Malinen, Bernadette Gehl, Lars J.C. Jeuken, Arwen R. Pearson, Adrian Goldman

Membrane-bound pyrophosphatases (M-PPases) are homodimeric primary ion pumps that couple the transport of Na+- and/or H+across membranes to the hydrolysis of pyrophosphate. Their role in the virulence of protist pathogens likePlasmodium falciparummak

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9efa3c66a8e72459e22659b204477a74
https://doi.org/10.1101/2022.11.07.515396

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

Autor: Keni Vidilaseris, Gang Dong, Nicolas Landrein, Johannes Lesigang, Derrick R. Robinson, Niran Aeksiri, Mélanie Bonhivers, Yulia Pivovarova

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, 295 (6), pp.1489-1499. ⟨10.1074/jbc.RA119.010768⟩
J Biol Chem
'Journal of Biological Chemistry ', vol: 295, pages: 1489-1499 (2020)

International audience; 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 pock

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cb63aa6873387238d984c336f5afc19
https://hal.archives-ouvertes.fr/hal-02482599/document

Asymmetry in catalysis by Thermotoga maritima membrane-bound pyrophosphatase demonstrated by a nonphosphorus allosteric inhibitor

Autor: Ayman Khattab, Paula Kiuru, Teppo O. Leino, Alexandros Kiriazis, Jari Yli-Kauhaluoma, Henri Xhaard, Ainoleena Turku, Adrian Goldman, Seppo Meri, Niklas G. Johansson, Gustav Boije af Gennäs, Keni Vidilaseris

Publikováno v: 'Science Advances ', vol: 5, pages: eaav7574-1-eaav7574-12 (2019)

Membrane-bound pyrophosphatases are homodimeric integral membrane proteins that hydrolyze pyrophosphate into orthophosphates, coupled to the active transport of protons or sodium ions across membranes. They are important in the life cycle of bacteria

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4b4e5dd74119289ae3cd225d57d2610
http://hdl.handle.net/10138/303494