Contacting domains segregate a lipid transporter from a solute transporter in the malarial host–parasite interface
| Autor: | Tatyana Tenkova-Heuser, Christopher K. E. Bleck, John E. Heuser, Daniel E. Goldberg, Eva S. Istvan, Joshua Zimmerberg, Robyn Roth, Matthias Garten, Josh R. Beck |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Cytoplasm Erythrocytes Science Plasmodium falciparum Protozoan Proteins General Physics and Astronomy Membrane trafficking General Biochemistry Genetics and Molecular Biology Article Host-Parasite Interactions 03 medical and health sciences 0302 clinical medicine Organelle parasitic diseases Extracellular Parasite hosting Humans Malaria Falciparum lcsh:Science Multidisciplinary Chemistry Intracellular parasite Cell Membrane Membrane Transport Proteins Transporter Biological Transport Membrane structure and assembly General Chemistry Intracellular Membranes Lipids Transport protein Cell biology Parasite biology Protein Transport 030104 developmental biology Membrane Vacuoles lcsh:Q 030217 neurology & neurosurgery |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | The malaria parasite interfaces with its host erythrocyte (RBC) using a unique organelle, the parasitophorous vacuole (PV). The mechanism(s) are obscure by which its limiting membrane, the parasitophorous vacuolar membrane (PVM), collaborates with the parasite plasma membrane (PPM) to support the transport of proteins, lipids, nutrients, and metabolites between the cytoplasm of the parasite and the cytoplasm of the RBC. Here, we demonstrate that the PV has structure characterized by micrometer-sized regions of especially close apposition between the PVM and the PPM. To determine if these contact sites are involved in any sort of transport, we localize the PVM nutrient-permeable and protein export channel EXP2, as well as the PPM lipid transporter PfNCR1. We find that EXP2 is excluded from, but PfNCR1 is included within these regions of close apposition. We conclude that the host-parasite interface is structured to segregate those transporters of hydrophilic and hydrophobic substrates. While membrane contact sites between intracellular organelles are abundant, little is known about the contacts between membranes that delimit extracellular junctions within cells, such as intracellular parasites. Here authors demonstrate the segregation of a lipid transporter from a solute transporter in the malarial host-parasite interface. |
| Databáze: | OpenAIRE |
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