Evidence map›Paper›PMID 26694741›Full record

ArticlePLoS pathogens2015

Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.

Wai-Hong Tham, Nicholas T Y Lim, Greta E Weiss, Sash Lopaticki, Brendan R E Ansell, Megan Bird, Isabelle Lucet, Dominique Dorin-Semblat, Christian Doerig, Paul R Gilson and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 56 citations in OpenAlex.

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  11. Biophysical Tools and Concepts Enable Understanding of Asexual Blood Stage Malaria.Frontiers in cellular and infection microbiology · 2022
    Review
  12. Article
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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

12 authors at 4 institutions in 2 countries.

Wai-Hong ThamThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Nicholas T Y LimThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Greta E WeissBurnet Institute, Melbourne, Victoria, Australia.
Sash LopatickiThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Brendan R E AnsellThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Megan BirdDepartment of Microbiology, Monash University, Melbourne, Victoria, Australia.
Isabelle LucetThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Dominique Dorin-SemblatINSERM UMR_S 1134, Université Paris Diderot, GIP INTS, Paris, France.
Christian DoerigDepartment of Microbiology, Monash University, Melbourne, Victoria, Australia.
Paul R GilsonBurnet Institute, Melbourne, Victoria, Australia.
Brendan S CrabbBurnet Institute, Melbourne, Victoria, Australia.
Alan F CowmanThe Walter & Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
University of Melbourne · AUMonash University · AUBurnet Institute · AUDélégation Paris 7 · FR

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The most severe form of malaria in humans is caused by the protozoan parasite Plasmodium falciparum. The invasive form of malaria parasites is termed a merozoite and it employs an array of parasite proteins that bind to the host cell to mediate invasion. In Plasmodium falciparum, the erythrocyte binding-like (EBL) and reticulocyte binding-like (Rh) protein families are responsible for binding to specific erythrocyte receptors for invasion and mediating signalling events that initiate active entry of the malaria parasite. Here we have addressed the role of the cytoplasmic tails of these proteins in activating merozoite invasion after receptor engagement. We show that the cytoplasmic domains of these type 1 membrane proteins are phosphorylated in vitro. Depletion of PfCK2, a kinase implicated to phosphorylate these cytoplasmic tails, blocks P. falciparum invasion of red blood cells. We identify the crucial residues within the PfRh4 cytoplasmic domain that are required for successful parasite invasion. Live cell imaging of merozoites from these transgenic mutants show they attach but do not penetrate erythrocytes implying the PfRh4 cytoplasmic tail conveys signals important for the successful completion of the invasion process.

Indexed as

Amino Acid SequenceErythrocytesHumansMalaria, FalciparumMerozoitesMolecular Sequence DataPhosphorylationPhosphotransferasesPlasmodium falciparumProtozoan ProteinsPhosphotransferasesProtozoan Proteins

Identifiers

PMID26694741
PMCPMC4687929
OpenAlexW2209591539

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.