Contacting domains segregate a lipid transporter from a solute transporter in the malarial host–parasite interface

Matthias Garten, Josh R. Beck, Robyn Roth, Tatyana Tenkova-Heuser, John Heuser, Eva S. Istvan, Christopher K. E. Bleck, Daniel E. Goldberg () and Joshua Zimmerberg ()
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Matthias Garten: Section on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health
Josh R. Beck: Iowa State University
Robyn Roth: Washington University School of Medicine
Tatyana Tenkova-Heuser: Section on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health
John Heuser: Section on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health
Eva S. Istvan: Washington University School of Medicine
Christopher K. E. Bleck: Electron Microscopy Core Facility, National Heart, Lung and Blood Institute, National Institutes of Health
Daniel E. Goldberg: Washington University School of Medicine
Joshua Zimmerberg: Section on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-17506-9

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