Trypanosoma brucei transferrin receptor: functional replacement of the GPI anchor with a transmembrane domain
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...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
12 January 2021
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| In: |
Molecular and biochemical parasitology
Year: 2021, Volume: 242, Pages: 1-5 |
| ISSN: | 1872-9428 |
| DOI: | 10.1016/j.molbiopara.2021.111361 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.molbiopara.2021.111361 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0166685121000128 
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| Author Notes: | Mostafa Kabiri, Dietmar Steverding |
MARC
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| 520 | |a 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. | ||
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