Evidence map›Paper›PMID 42591034›Full record

ArticleMolecular microbiology2026

Characterization of Sec14 Domain-Containing Proteins in the Malaria Parasite Plasmodium falciparum.

Florian Lauruol, Dominik Šťastný, J Pedro Fernandez-Murray, Christopher R McMaster, Peter Griač, Dave Richard

Abstract read
In one paragraph

Article in Molecular microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Florian LauruolDepartment of Microbiology-Infectious Diseases and Immunology, Faculty of Medicine, Université Laval, Québec, Quebec, Canada.ORCID https://orcid.org/0000-0001-5919-1372
Dominik ŠťastnýCentre of Biosciences, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Bratislava, Slovakia.ORCID https://orcid.org/0009-0002-2015-4309
J Pedro Fernandez-MurrayDepartment of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada.ORCID https://orcid.org/0000-0002-9921-5487
Christopher R McMasterDepartment of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada.ORCID https://orcid.org/0000-0003-0822-5776
Peter GriačCentre of Biosciences, Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Bratislava, Slovakia.ORCID https://orcid.org/0000-0003-3538-0405
Dave RichardDepartment of Microbiology-Infectious Diseases and Immunology, Faculty of Medicine, Université Laval, Québec, Quebec, Canada.ORCID https://orcid.org/0000-0003-2269-6240

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
CIHR 406675Natural Sciences and Engineering Research Council of Canada RGPIN 06491NIGMS NIH HHS R01 GM129325Scientific Grant Agency of the Ministry of Education, Research, Development, and Youth of the Slovak Republic and the Slovak Academy of Sciences 2/0075/26Scientific Grant Agency of the Ministry of Education, Research, Development, and Youth of the Slovak Republic and the Slovak Academy of Sciences VEGA 2/0047/23Stefan Schwarz Support Fund of the Slovak Academy of Sciences 2024/OV2/011
6 · The paper itself

Abstract

Plasmodium falciparum parasites cause the most virulent form of malaria, a disease that remains a major global health burden. The appearance of resistance to first line artemisinin-based therapies emphasizes the need to identify new parasite vulnerabilities to develop new therapeutics. Phosphoinositides are central regulators of membrane identity, vesicular trafficking, and signaling, and their synthesis depends on tightly controlled phosphatidylinositol transfer by Sec14-like phosphatidylinositol transfer proteins in many eukaryotes, yet their roles in P. falciparum remain poorly defined. Here, we analyzed six P. falciparum Sec14 domain-containing proteins: PfSec14-1 (PF3D7_0626400), PfSec14-2 (PF3D7_0629900), PfSec14-3 (PF3D7_0717100), PfSec14-4 (PF3D7_0920700), PfSec14-5 (PF3D7_1007200), and PfSec14-6 (PF3D7_1127600). Domain organization segregates these proteins into a BNIP-2 and Cdc42GAP homology (BCH) subfamily (PfSec14-3, PfSec14-5) and a canonical Sec14 subfamily (PfSec14-1, PfSec14-2, PfSec14-4, and PfSec14-6). Yeast complementation assays showed that PfSec14-1, PfSec14-4, and PfSec14-6 partially rescue growth of a temperature-sensitive sec14 mutant, suggesting phosphatidylinositol and phosphatidylcholine transfer activity. Gene disruption revealed that PfSec14-1 is important for asexual blood-stage proliferation, whereas PfSec14-2 is dispensable under standard culture conditions. In contrast, mislocalization of PfSec14-2 and PfSec14-4 using a knock-sideways approach did not impair asexual growth. Subcellular localization indicates distinct distributions for PfSec14-1, PfSec14-2, and PfSec14-4. Together, these findings reveal potential functional and spatial diversification of Sec14-like phosphatidylinositol transfer proteins in P. falciparum.

Indexed as

Phospholipid Transfer ProteinsPlasmodium falciparumProtozoan ProteinsMalaria, FalciparumPhosphatidylinositolsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPhosphatidylinositolsPhospholipid Transfer ProteinsProtozoan ProteinsSaccharomyces cerevisiae ProteinsSEC14 protein, S cerevisiaemalariaphosphoinositidesPITPPlasmodiumsec14

Identifiers

PMID42591034
PMCPMC13644383

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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.