Evidence map›Paper›PMID 32732874›Full record

ArticleNature communications2020

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, Joshua Zimmerberg

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Unpacking boxes: identification of novel inhibitors of malaria parasite invasion.International journal for parasitology. Drugs and drug resistance · 2026
    Article
  3. Article
  4. bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. TheScience advances · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  12. Article
  13. The role of cholesterol in invasion and growth of malaria parasites.Frontiers in cellular and infection microbiology · 2022
    Review
  14. Review
  15. Designing antimalarials that break into cells to lock down parasites.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. Review
  18. Frontiers in cell and developmental biology · 2021
    Review
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Matthias GartenSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA.ORCID http://orcid.org/0000-0002-8660-1039
Josh R BeckDepartment of Biomedical Sciences, Iowa State University, Ames, IA, 50011, USA.ORCID http://orcid.org/0000-0001-6196-8689
Robyn RothDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO, 63110, USA.
Tatyana Tenkova-HeuserSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA.
John HeuserSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA.
Eva S IstvanDepartments of Medicine and Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, 63110, USA.ORCID http://orcid.org/0000-0002-8666-3248
Christopher K E BleckElectron Microscopy Core Facility, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.ORCID http://orcid.org/0000-0003-1029-3444
Daniel E GoldbergDepartments of Medicine and Molecular Microbiology, Washington University School of Medicine, St. Louis, MO, 63110, USA. dgoldberg@wustl.edu.ORCID http://orcid.org/0000-0003-3529-8399
Joshua ZimmerbergSection on Integrative Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA. zimmerbj@mail.nih.gov.ORCID http://orcid.org/0000-0002-1707-3789
National Institutes of Health · USWashington University in St. Louis · USIowa State University · US

Funding

Membrane Remodeling in Viral Infection, Parasite Replication, and Traumatic Brain InjuryZIAHD001409 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI ZIMMERBERG, JOSHUA · 2009 to 2025
$29.9M
Erythrocyte Subversion by Malaria Parasite Exported EffectorsR00HL133453 · NHLBI · IOWA STATE UNIVERSITY · PI BECK, JOSH RYAN · 2017 to 2019
$747k
Erythrocyte Subversion by Malaria Parasite Exported EffectorsK99HL133453 · NHLBI · WASHINGTON UNIVERSITY · PI BECK, JOSH RYAN · 2016 to 2017
$166k
NHLBI NIH HHS K99 HL133453NHLBI NIH HHS R00 HL133453
6 · The paper itself

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.

Indexed as

LipidsBiological TransportCell MembraneCytoplasmErythrocytesHost-Parasite InteractionsHumansIntracellular MembranesMalaria, FalciparumMembrane Transport ProteinsPlasmodium falciparumProtein TransportProtozoan ProteinsVacuolesLipidsMembrane Transport ProteinsProtozoan Proteins

Identifiers

PMID32732874
PMCPMC7393353
OpenAlexW3046894614

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.