Evidence map›Paper›PMID 26916885›Full record

ArticleCellular microbiology2016

Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton.

Alexander Oberli, Laura Zurbrügg, Sebastian Rusch, Françoise Brand, Madeleine E Butler, Jemma L Day, Erin E Cutts, Thomas Lavstsen, Ioannis Vakonakis, Hans-Peter Beck

Abstract read
In one paragraph

Article in Cellular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023
    Review
  2. TheFrontiers in molecular biosciences · 2023
    Review
  3. Identification of ExportedMicroorganisms · 2022
    Article
  4. Article
  5. Article
  6. Interaction Analysis of aFrontiers in microbiology · 2020
    Article
  7. Article
  8. Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019
    Review
  9. Review
  10. Article
  11. Erythrocyte Membrane Makeover byFrontiers in microbiology · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. eLife · 2017
    Article
  18. Article
  19. Article
  20. 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

10 authors.

Alexander OberliSwiss Tropical and Public Health Institute, Basel, Switzerland.
Laura ZurbrüggSwiss Tropical and Public Health Institute, Basel, Switzerland.
Sebastian RuschSwiss Tropical and Public Health Institute, Basel, Switzerland.
Françoise BrandSwiss Tropical and Public Health Institute, Basel, Switzerland.
Madeleine E ButlerDepartment of Biochemistry, University of Oxford, Oxford, UK.
Jemma L DayDepartment of Biochemistry, University of Oxford, Oxford, UK.
Erin E CuttsDepartment of Biochemistry, University of Oxford, Oxford, UK.
Thomas LavstsenCentre for Medical Parasitology, Department of International Health, Immunology, and Microbiology, University of Copenhagen, Copenhagen, Denmark.
Ioannis VakonakisDepartment of Biochemistry, University of Oxford, Oxford, UK.
Hans-Peter BeckSwiss Tropical and Public Health Institute, Basel, Switzerland. hans-peter.beck@unibas.ch.

Funding

Medical Research Council MR/N009274/1Wellcome Trust
6 · The paper itself

Abstract

Adherence of Plasmodium falciparum-infected erythrocytes to host endothelium is conferred through the parasite-derived virulence factor P. falciparum erythrocyte membrane protein 1 (PfEMP1), the major contributor to malaria severity. PfEMP1 located at knob structures on the erythrocyte surface is anchored to the cytoskeleton, and the Plasmodium helical interspersed subtelomeric (PHIST) gene family plays a role in many host cell modifications including binding the intracellular domain of PfEMP1. Here, we show that conditional reduction of the PHIST protein PFE1605w strongly reduces adhesion of infected erythrocytes to the endothelial receptor CD36. Adhesion to other endothelial receptors was less affected or even unaltered by PFE1605w depletion, suggesting that PHIST proteins might be optimized for subsets of PfEMP1 variants. PFE1605w does not play a role in PfEMP1 transport, but it directly interacts with both the intracellular segment of PfEMP1 and with cytoskeletal components. This is the first report of a PHIST protein interacting with key molecules of the cytoadherence complex and the host cytoskeleton, and this functional role seems to play an essential role in the pathology of P. falciparum.

Indexed as

Cell AdhesionCells, CulturedCytoskeletonErythrocytesHost-Parasite InteractionsHumansMalaria, FalciparumPlasmodium falciparumProtein BindingProtein Interaction MapsProtein TransportProtozoan ProteinsProtozoan Proteins

Identifiers

PMID26916885
PMCPMC5103180

What OpenQuestion holds

Textmetadata
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.