Journal
PEERJ
Volume 5, Issue -, Pages -Publisher
PEERJ INC
DOI: 10.7717/peerj.3128
Keywords
Apicoplast; Acyl-carrier protein (ACP-GFP); P. falciparum; Glutathione peroxidase like thioredoxin peroxidase (PfTPx(Gl)); Protein trafficking
Categories
Funding
- Science and Engineering Research Board (SERB) [SB/YS/LS-354/2013]
- Board of Research in Nuclear Sciences (BRNS) [2013/37B/18/BRNS]
Ask authors/readers for more resources
The secretory pathway in Plasmodium falciparum has evolved to transport proteins to the host cell membrane and to an endosymbiotic organelle, the apicoplast. The latter can latter can occur via the ER or the ER-Golgi route. Here, we study these three routes using proteins Erythrocyte Membrane Protein-1 (PfEMP1), Acyl Carrier Protein (ACP) and glutathione peroxidase-like thioredoxin peroxidase (PfTPx(Gl)) and inhibitors of vesicular transport. As expected,the G protein-dependent vesicular. fusion inphibitor AlF4- and microtubule destabilizing drug vinblastine block the trafficking of PfEMP- 1 a protein secreted to the. host cell membrane. However, while both PfITx(Gl) and ACP are targeted to the apicoplast, only ACP trafficking remains unaffected by these treatments. This implies that. G protein-dependent vesicles do not play a role in classical apicoplast protein targeting. Unlike the soluble protein ACP, we show that localized to the outermost membrane of the apicoplast. Thus, the parasite apicoplast acquires proteins via two different pathways:first, the vesicular trafficking pathway appears to handle not only secretory Proteins, but an apicoplast membrane PfTPx(Gl); second, trafficking of apicoplast luminal proteins appear to be independent , of G protein-coupled vesicles.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available