Biochemical characterization of highly active Trypanosoma brucei gambiense glycerol kinase, a promising drug target

2013 ◽  
Vol 154 (1) ◽  
pp. 77-84 ◽  
Author(s):  
E. O. Balogun ◽  
D. K. Inaoka ◽  
T. Shiba ◽  
Y. Kido ◽  
T. Nara ◽  
...  
2012 ◽  
Vol 194 (19) ◽  
pp. 5434-5443 ◽  
Author(s):  
H. Tomita ◽  
Y. Yokooji ◽  
T. Ishibashi ◽  
T. Imanaka ◽  
H. Atomi

2011 ◽  
Vol 108 (1) ◽  
pp. 33-46 ◽  
Author(s):  
Cristina Pagliano ◽  
Fabiana Chimirri ◽  
Guido Saracco ◽  
Francesco Marsano ◽  
James Barber

2013 ◽  
Vol 288 (20) ◽  
pp. 14428-14437 ◽  
Author(s):  
Marco A. Sanchez

Pyruvate export is an essential physiological process for the bloodstream form of Trypanosoma brucei as the parasite would otherwise accumulate this end product of glucose metabolism to toxic levels. In the studies reported here, genetic complementation in Saccharomyces cerevisiae has been employed to identify a gene (TbPT0) that encodes this vital pyruvate transporter from T. brucei. Expression of TbPT0 in S. cerevisiae reveals that TbPT0 is a high affinity pyruvate transporter. TbPT0 belongs to a clustered multigene family consisting of five members, whose expression is up-regulated in the bloodstream form. Interestingly, TbPT family permeases are related to polytopic proteins from plants but not to characterized monocarboxylate transporters from mammals. Remarkably, inhibition of the TbPT gene family expression in bloodstream parasites by RNAi is lethal, confirming the physiological relevance of these transporters. The discovery of TbPT0 reveals for the first time the identity of the essential pyruvate transporter and provides a potential drug target against the mammalian life cycle stage of T. brucei.


PLoS ONE ◽  
2016 ◽  
Vol 11 (11) ◽  
pp. e0167350 ◽  
Author(s):  
Aygun Israyilova ◽  
Silvia Buroni ◽  
Federico Forneris ◽  
Viola Camilla Scoffone ◽  
Namiq Q. Shixaliyev ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document