Evidence map›Paper›PMID 34031901›Full record

ArticleThe EMBO journal2021

Dephospho-CoA kinase, a nuclear-encoded apicoplast protein, remains active and essential after Plasmodium falciparum apicoplast disruption.

Russell P Swift, Krithika Rajaram, Hans B Liu, Sean T Prigge

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-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

38 citing papers in PubMed, 52 citations in OpenAlex.

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  14. tRNA modifying enzymes MnmE and MnmG are essential forbioRxiv : the preprint server for biology · 2025
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  15. In Silico Screening ofBiologics : targets & therapy · 2025
    Article
  16. 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

4 authors at 1 institution in 1 country.

Russell P SwiftDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, USA.
Krithika RajaramDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, USA.ORCID 0000-0003-4830-5471
Hans B LiuDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, USA.
Sean T PriggeDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, USA.ORCID 0000-0001-9684-1733
Johns Hopkins University · US

Funding

Determinants of apicoplast maintenance in malaria parasitesR01AI125534 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Sean Taylor PRIGGE · 2016 to 2026
$3.9M
Roles of Lipoate Pathways in Plasmodium SurvivalR01AI065853 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2006 to 2010
$2.0M
Conditional probes of secretory protein function in malaria parasitesR21AI101589 · NIAID · JOHNS HOPKINS UNIVERSITY · PI PRIGGE, SEAN TAYLOR · 2012 to 2013
$428k
NIAID NIH HHS R01 AI065853NIAID NIH HHS R01 AI125534NIAID NIH HHS R21 AI101589
6 · The paper itself

Abstract

Malaria parasites contain an essential organelle called the apicoplast that houses metabolic pathways for fatty acid, heme, isoprenoid, and iron-sulfur cluster synthesis. Surprisingly, malaria parasites can survive without the apicoplast as long as the isoprenoid precursor isopentenyl pyrophosphate (IPP) is supplemented in the growth medium, making it appear that isoprenoid synthesis is the only essential function of the organelle in blood-stage parasites. In the work described here, we localized an enzyme responsible for coenzyme A synthesis, DPCK, to the apicoplast, but we were unable to delete DPCK, even in the presence of IPP. However, once the endogenous DPCK was complemented with the E. coli DPCK (EcDPCK), we were successful in deleting it. We were then able to show that DPCK activity is required for parasite survival through knockdown of the complemented EcDPCK. Additionally, we showed that DPCK enzyme activity remains functional and essential within the vesicles present after apicoplast disruption. These results demonstrate that while the apicoplast of blood-stage P. falciparum parasites can be disrupted, the resulting vesicles remain biochemically active and are capable of fulfilling essential functions.

Indexed as

ApicoplastsPantothenic AcidPhosphotransferases (Alcohol Group Acceptor)Plasmodium falciparumProtozoan Proteinsdephospho-CoA kinasePantothenic AcidPhosphotransferases (Alcohol Group Acceptor)Protozoan Proteinsapicoplastcoenzyme ADPCKmalariaPlasmodium falciparum

Identifiers

PMID34031901
PMCPMC8365264
OpenAlexW3165320556

What OpenQuestion holds

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Registered trials

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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.