Evidence map›Paper›PMID 25900212›Full record

ArticleInternational journal for parasitology2015

Biogenesis of the crystalloid organelle in Plasmodium involves microtubule-dependent vesicle transport and assembly.

Sadia Saeed, Annie Z Tremp, Johannes T Dessens

Open access · hybridAbstract read
In one paragraph

Article in International journal for parasitology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. A pleckstrin homology domain protein is involved in crystalloid formation inFrontiers in cellular and infection microbiology · 2026
    Article
  4. Review
  5. Open biology · 2024
    Article
  6. The molecular mechanisms driving Plasmodium cell division.Biochemical Society transactions · 2024
    Review
  7. Review
  8. Article
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  17. Article
  18. Review
  19. Maternally supplied S-acyl-transferase is required for crystalloid organelle formation and transmission of the malaria parasite.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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

3 authors at 1 institution in 1 country.

Sadia SaeedPathogen Molecular Biology Department, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom.
Annie Z TrempPathogen Molecular Biology Department, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom.
Johannes T DessensPathogen Molecular Biology Department, Faculty of Infectious and Tropical Diseases, London School of Hygiene & Tropical Medicine, Keppel Street, London WC1E 7HT, United Kingdom. Electronic address: Johannes.Dessens@lshtm.ac.uk.
London School of Hygiene & Tropical Medicine · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M001598Wellcome Trust 076648Wellcome Trust 088449
6 · The paper itself

Abstract

Malaria parasites possess unique subcellular structures and organelles. One of these is the crystalloid, a multivesicular organelle that forms during the parasite's development in vector mosquitoes. The formation and function of these organelles remain poorly understood. A family of six conserved and modular proteins named LCCL-lectin adhesive-like proteins (LAPs), which have essential roles in sporozoite transmission, localise to the crystalloids. In this study we analyse crystalloid formation using transgenic Plasmodium berghei parasites expressing GFP-tagged LAP3. We show that deletion of the LCCL domain from LAP3 causes retarded crystalloid development, while knockout of LAP3 prevents formation of the organelle. Our data reveal that the process of crystalloid formation involves active relocation of endoplasmic reticulum-derived vesicles to common assembly points via microtubule-dependent transport. Inhibition of microtubule-dependent cargo transport disrupts this process and replicates the LCCL domain deletion mutant phenotype in wildtype parasites. These findings provide the first clear insight into crystalloid biogenesis, demonstrating a fundamental role for the LAP family in this process, and identifying the crystalloid and its formation as potential targets for malaria transmission control.

Indexed as

AnimalsFemaleHumansMalariaMiceMicrotubulesOrganellesPlasmodium bergheiProtein TransportProtozoan ProteinsTransport VesiclesProtozoan ProteinsCargo transportCrystalloidLCCL proteinPlasmodium bergheiTransgenic parasite

Identifiers

PMID25900212
PMCPMC4459735
OpenAlexW2057062529

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.