Evidence map›Paper›PMID 20855594›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Complement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand.

Wai-Hong Tham, Danny W Wilson, Sash Lopaticki, Christoph Q Schmidt, Patience B Tetteh-Quarcoo, Paul N Barlow, Dave Richard, Jason E Corbin, James G Beeson, Alan F Cowman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
16.7field-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

127 citing papers in PubMed, 230 citations in OpenAlex.

  1. Trial
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  9. iScience · 2025
    Article
  10. Article
  11. Article
  12. Frontiers in immunology · 2025
    Article
  13. Article
  14. Article
  15. Cells · 2024
    Review
  16. Complement receptor 1 is the human erythrocyte receptor forProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Structural biology of complement receptors.Frontiers in immunology · 2023
    Review
  18. Review
  19. Article
  20. Review

67 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

10 authors at 4 institutions in 3 countries.

Wai-Hong ThamThe Walter and Eliza Hall Institute of Medical Research, Parkville 3052, Australia.
Danny W Wilson
Sash Lopaticki
Christoph Q Schmidt
Patience B Tetteh-Quarcoo
Paul N Barlow
Dave Richard
Jason E Corbin
James G Beeson
Alan F Cowman
Walter and Eliza Hall Institute of Medical Research · AUUniversity of Edinburgh · GBUniversity of Ghana · GHUniversity of Melbourne · AU

Funding

Howard Hughes Medical InstituteWellcome Trust
6 · The paper itself

Abstract

Plasmodium falciparum is responsible for the most severe form of malaria disease in humans, causing more than 1 million deaths each year. As an obligate intracellular parasite, P. falciparum's ability to invade erythrocytes is essential for its survival within the human host. P. falciparum invades erythrocytes using multiple host receptor-parasite ligand interactions known as invasion pathways. Here we show that CR1 is the host erythrocyte receptor for PfRh4, a major P. falciparum ligand essential for sialic acid-independent invasion. PfRh4 and CR1 interact directly, with a K(d) of 2.9 μM. PfRh4 binding is strongly correlated with the CR1 level on the erythrocyte surface. Parasite invasion via sialic acid-independent pathways is reduced in low-CR1 erythrocytes due to limited availability of this receptor on the surface. Furthermore, soluble CR1 can competitively block binding of PfRh4 to the erythrocyte surface and specifically inhibit sialic acid-independent parasite invasion. These results demonstrate that CR1 is an erythrocyte receptor used by the parasite ligand PfRh4 for P. falciparum invasion.

Indexed as

AnimalsErythrocytesHumansMembrane ProteinsN-Acetylneuraminic AcidPlasmodium falciparumProtein BindingProtozoan ProteinsReceptors, ComplementRecombinant ProteinsMembrane ProteinsN-Acetylneuraminic AcidProtozoan ProteinsReceptors, ComplementRecombinant ProteinsRH4 protein, Plasmodium falciparum

Identifiers

PMID20855594
PMCPMC2951459
OpenAlexW2035712449

What OpenQuestion holds

Textmetadata
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.