Evidence map›Paper›PMID 20228060›Full record

ArticleThe Journal of biological chemistry2010

Interaction between Plasmodium falciparum apical membrane antigen 1 and the rhoptry neck protein complex defines a key step in the erythrocyte invasion process of malaria parasites.

Dave Richard, Christopher A MacRaild, David T Riglar, Jo-Anne Chan, Michael Foley, Jake Baum, Stuart A Ralph, Raymond S Norton, Alan F Cowman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
24.0field-weighted citation impact, top 1% 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

142 citing papers in PubMed, 245 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. The essential function of the apical polar ring during the blood stage ofbioRxiv : the preprint server for biology · 2026
    Article
  8. Physiology of invasiveFrontiers in cellular and infection microbiology · 2026
    Review
  9. Article
  10. mBio · 2025
    Article
  11. Article
  12. Identification of a novel rhoptry protein expressed predominantly inFrontiers in cellular and infection microbiology · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Atlas ofeLife · 2023
    Article
  18. Article
  19. Atlas ofbioRxiv : the preprint server for biology · 2023
    Article
  20. Article

82 more citing papers are in PubMed but not listed here.

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.

Dave RichardWalter and Eliza Hall Institute of Medical Research, Parkville, Melbourne, Victoria 3052, Australia.
Christopher A MacRaild
David T Riglar
Jo-Anne Chan
Michael Foley
Jake Baum
Stuart A Ralph
Raymond S Norton
Alan F Cowman
Walter and Eliza Hall Institute of Medical Research · AULa Trobe University · AUUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Invasion of host cells by apicomplexan parasites, including Plasmodium falciparum and Toxoplasma gondii, is a multistep process. Central to invasion is the formation of a tight junction, an aperture in the host cell through which the parasite pulls itself before settling into a newly formed parasitophorous vacuole. Two protein groups, derived from different secretory organelles, the micronemal protein AMA1 and the rhoptry proteins RON2, RON4, and RON5, have been shown to form part of this structure, with antibodies targeting P. falciparum AMA1 known to inhibit invasion, probably via disruption of its association with the PfRON proteins. Inhibitory AMA1-binding peptides have also been described that block P. falciparum merozoite invasion of the erythrocyte. One of these, R1, blocks invasion some time after initial attachment to the erythrocyte and reorientation of the merozoite to its apical pole. Here we show that the R1 peptide binds the PfAMA1 hydrophobic trough and demonstrate that binding to this region prevents its interaction with the PfRON complex. We show that this defined association between PfAMA1 and the PfRON complex occurs after reorientation and engagement of the actomyosin motor and argue that it precedes rhoptry release. We propose that the formation of the AMA1-RON complex is essential for secretion of the rhoptry contents, which then allows the establishment of parasite infection within the parasitophorous vacuole.

Indexed as

Antigens, ProtozoanCarrier ProteinsErythrocytesHumansImmunoprecipitationMagnetic Resonance SpectroscopyMalaria, FalciparumMembrane ProteinsMerozoitesPlasmodium falciparumProtein ConformationProtozoan ProteinsSchizontsAntigens, Protozoanapical membrane antigen I, PlasmodiumCarrier ProteinsMembrane Proteinspeptide R1Protozoan Proteins

Identifiers

PMID20228060
PMCPMC2863225
OpenAlexW1997960416

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.