ORCID Profile
0000-0002-0050-7771
Current Organisation
University of East Anglia
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Publisher: Wiley
Date: 28-10-1996
DOI: 10.1016/0014-5793(96)01073-3
Abstract: Uptake of host transferrin (Tf) in Trypanosoma brucei is mediated by a heterodimeric, glycosyl-phosphatidylinositol-anchored receptor. After endocytosis, Tf is delivered to lysosomes where it is proteolytically degraded. So far, the sequence of events leading to ligand dissociation and degradation is undefined. We now show by Triton X-114 phase separation that iron-free Tf (apo-Tf) dissociates from the receptor at pH 5.0. The low affinity of apo-Tf for its receptor at pH 5.0 is confirmed by an apparent dissociation constant of 1.1 microM. The implications of this result on the mechanism of intracellular processing of Tf in trypanosomes are discussed.
Publisher: Elsevier BV
Date: 10-2008
DOI: 10.1016/J.EXPPARA.2008.07.004
Abstract: The transferrin receptor of the parasite Trypanosoma brucei is a heterodimeric protein complex encoded by the 2 expression site-associated genes (ESAGs) 6 and 7. ESAG6 is a heterogeneously glycosylated protein of 50-60kDa modified by a glycosylphosphatidylinositol anchor at the C-terminus, while ESAG7 is a 40-42kDa glycoprotein carrying an unmodified C-terminus. In order to determine whether glycosylation is necessary for dimer formation and ligand binding, the receptor was expressed in insect cells in the presence of tunicamycin. When insect cells were infected with recombinant ESAG6/ESAG7 double expressor baculovirus and grown in the presence of tunicamycin, non-glycosylated forms of ESAG6 and ESAG7 of 46 and 36kDa, respectively, were synthesized. The non-glycosylated ESAG6 and ESAG7 were capable of forming a heterodimer and of binding transferrin. This results shows that glycosylation is not necessary for synthesis of a functional T. brucei transferrin receptor.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Dietmar Steverding.