Back to search

Article

Nutrient stress dramatically increases malaria parasite <i>clag2</i> copy number to increase host cell permeability and enable pathogen survival

2025-06-23

Abstract excerpt

To grow and replicate in erythrocytes, malaria parasites must increase the host cell’s permeability to a broad range of nutrients. The plasmodial surface anion channel (PSAC) mediates this increased permeability and has been linked to CLAG3, a protein encoded by a multigene family conserved in Plasmodium spp. Surprisingly, an CLAG3 knockout parasite produced in P. falciparum exhibits incomplete reductions in PSA...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
121b3226-f5fc-507b-adf7-ec28a5e4c42d
DOI
10.1101/2025.06.23.661025
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Nutrient stress dramatically increases malaria parasite <i>clag2</i> copy number to increase host cell permeability and enable pathogen survivalDOI 10.1101/2025.06.23.661025
Partially Overlapping Contributions of Clag Paralogs to Nutrient Uptake Channels in <em>P</em>. <em>falciparum</em>Semantic proximity
CLAG3 Self-Associates in Malaria Parasites and Quantitatively Determines Nutrient Uptake Channels at the Host MembraneSemantic proximity
Complex nutrient channel phenotypes despite Mendelian inheritance in a Plasmodium falciparum genetic cross.Semantic proximity
Solute Restriction Reveals an Essential Role for clag3-Associated Channels in Malaria Parasite Nutrient AcquisitionSemantic proximity
Malaria parasite clag3 genes determine channel-mediated nutrient uptake by infected red blood cells.Semantic proximity
A CLAG3 mutation in an amphipathic transmembrane domain alters malaria parasite nutrient channels and confers leupeptin resistance.Semantic proximity
Phylogenetic profiles of all membrane transport proteins of the malaria parasite highlight new drug targetsSemantic proximity
MMV687794 blocks <i>Plasmodium falciparum</i> invasion of red blood cells by targeting a Surface-associated Lipid-Interacting Rhoptry Protein, <i>Pf</i> SLIRPSemantic proximity
An essential dual-function complex mediates erythrocyte invasion and channel-mediated nutrient uptake in malaria parasitesSemantic proximity
Iron transport pathways in the human malaria parasite <i>Plasmodium falciparum</i> revealed by RNA-sequencingSemantic proximity
TransLeish: Identification of membrane transporters essential for survival of intracellular <i>Leishmania</i> parasites in a systematic gene deletion screenSemantic proximity
Novel Ion Channel Genes in Malaria ParasitesSemantic proximity
Select a neighboring publication to make it the new centre.