Substitution of Pro165 in Transmembrane 4 of PfCRT Abolishes Lysosome Acidification Function in Stably Transfected HEK-293F Cells
Microbiology Research Journal International · pp. 45–55 · Published 27 Dec 2021
10.9734/mrji/2021/v31i1030352Abstract
The Plasmodium falciparum chloroquine resistance transporter (PfCRT) is localised on the parasite digestive vacuole, an organelle that maintains an acidic lumen. Here we demonstrated the isolation of HEK-293F cells stably expressing wild type 3D7 and mutant Pfcrt alleles. Immuno-fluorescence staining of HEK-293F transfectants confirms the localization of Pfcrt alleles to the lysosomal vesicles. Moreover, cells expressing mut-PfCRTETSE showed greater lysosomal acidification as demonstrated by the dramatic increase in the accumulation of two weak bases, acridine orange and CytiPainter LysoOrange dyes. Furthermore, HEK-293 cells stably expressing mut-PfCRTETSE with a single substitution of proline 165 in transmembrane 4 completely inhibited the accumulation of weak bases. Taken together, our results demonstrate the role of Pro165 in PfCRT lysosomal acidification function in HEK-293F cells.
Cited by 0
No indexed citations yet.
Related research
- Molecular Determinants of Artemisinin Resistance in k13 Gene of Plasmodium falciparum — shares topic coverage
- Mathematical Model of Malaria for Co-infection of Plasmodium vivax and Plasmodium falciparum in India — shares topic coverage
- Sentinel surveillance of the WHO-Validated Pfkelch13 C580Y Artemisinin Resistance Marker in Plasmodium falciparum Isolates from Bangui, Central African Republic — shares topic coverage
Article metrics
Real usage data collected on this platform.
0
Page views
0
PDF downloads
0
Outbound clicks
0
Citations
Views by country
Approximate, from request IP at view time — not citizenship or institution. Countries with fewer than 5 views are grouped as "Other".
No views recorded yet.
Traffic sources
Referring site, by host.
No traffic recorded yet.
Views and downloads exclude known bots/crawlers. Citations combines this platform's own DOI-resolved index with each external source's own reported total — see Cited by above for individually listed citing works. Last refreshed 0 seconds ago.