Trypanosoma brucei transferrin receptor

• Verfasst von: Kabiri, Mostafa [VerfasserIn]
• Verfasst von: Steverding, Dietmar [VerfasserIn]
• Titel: Trypanosoma brucei transferrin receptor
• Titelzusatz: functional replacement of the GPI anchor with a transmembrane domain
• Verf.angabe: Mostafa Kabiri, Dietmar Steverding
• E-Jahr: 2021
• Jahr: 12 January 2021
• Umfang: 5 S.
• Fussnoten: Gesehen am 21.12.2021
• Titel Quelle: Enthalten in: Molecular and biochemical parasitology
• Ort Quelle: Amsterdam : Elsevier, 1980
• Jahr Quelle: 2021
• Band/Heft Quelle: 242(2021), Artikel-ID 111361, Seite 1-5
• ISSN Quelle: 1872-9428
• DOI: doi:10.1016/j.molbiopara.2021.111361
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: GPI-anchor
• Sach-SW: Transferrin receptor
• Sach-SW: Transmembrane domain
• K10plus-PPN: 1782654275

Abstract

The transferrin receptor of Trypanosoma brucei (TbTfR) is a heterodimer of a glycosylphosphatidylinositol (GPI)-anchored ESAG6 subunit and an ESAG7 subunit. To investigate whether the GPI-anchor is essential for the function of the TbTfR, an ESAG6 with a transmembrane domain instead of a GPI-anchor (ESAG6tmd) was inducibly expressed in bloodstream form trypanosomes. It is shown that the ESAG6tmd is able to dimerise with ESAG7 to form a TbTfR that can bind transferrin. Fractionation experiments clearly demonstrated that the transmembrane-anchored TbTfR is exclusively associated with the membrane fraction. No difference in the uptake of transferrin was observed between trypanosomes inducibly expressing a transmembrane-anchored TbTfR and trypanosomes inducibly expressing a GPI-anchored TbTfR. Differences in glycosylation pattern of ESAG6tmd and native ESAG6 may indicate different intracellular trafficking of transmembrane- and GPI-anchored TbTfRs. The findings suggest that the GPI-anchor is not essential for the function of the TbTfR in bloodstream forms of T. brucei.