Citation

BibTex format

@article{Tiengwe:2016:10.1111/cmi.12605,
author = {Tiengwe, C and Muratore, KA and Bangs, JD},
doi = {10.1111/cmi.12605},
journal = {Cellular Microbiology},
pages = {1673--1688},
title = {Surface proteins, ERAD and antigenic variation in Trypanosoma brucei},
url = {http://dx.doi.org/10.1111/cmi.12605},
volume = {18},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Variant surface glycoprotein (VSG) is central to antigenic variation in African trypanosomes. Although much prior work documents that VSG is efficiently synthesized and exported to the cell surface, it was recently claimed that 2–3 fold more is synthesized than required, the excess being eliminated by ERAssociated Degradation (ERAD) (Field et al., 2010). We now reinvestigate VSG turnover and find no evidence for rapid degradation, consistent with a model whereby VSG synthesis is precisely regulated to match requirements for a functional surface coat on each daughter cell. However, using a mutated version of the ESAG7 subunit of the transferrin receptor (E7:Ty) we confirm functional ERAD in trypanosomes. E7:Ty fails to assemble into transferrin receptors and accumulates in the ER, consistent with retention of misfolded protein, and its turnover is selectively rescued by the proteasomal inhibitor MG132. We also show that ER accumulation of E7:Ty does not induce an unfolded protein response. These data, along with the presence of ERAD orthologues in the Trypanosoma brucei genome, confirm ERAD in trypanosomes. We discuss scenarios in which ERAD could be critical to bloodstream parasites, and how these may have contributed to the evolution of antigenic variation in trypanosomes.
AU - Tiengwe,C
AU - Muratore,KA
AU - Bangs,JD
DO - 10.1111/cmi.12605
EP - 1688
PY - 2016///
SN - 1462-5814
SP - 1673
TI - Surface proteins, ERAD and antigenic variation in Trypanosoma brucei
T2 - Cellular Microbiology
UR - http://dx.doi.org/10.1111/cmi.12605
UR - http://hdl.handle.net/10044/1/59681
VL - 18
ER -

Contact us

Dr. Calvin Tiengwe
Dept. of Life Sciences,
503 Sir Ernst Chain Building,
Imperial College London,
SW7 2AZ, UK

c.tiengwe@imperial.ac.uk 

Funding