Evidence map›Paper›PMID 27084458›Full record

ArticleCellular microbiology2016

Palmitoyl transferases have critical roles in the development of mosquito and liver stages of Plasmodium.

Christine S Hopp, Amanda E Balaban, Ellen S C Bushell, Oliver Billker, Julian C Rayner, Photini Sinnis

Abstract read
In one paragraph

Article in Cellular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Global Release of Translational Repression AcrossbioRxiv : the preprint server for biology · 2024
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  10. Identification of Three NovelFrontiers in cellular and infection microbiology · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Protein S-palmitoylation in cellular differentiation.Biochemical Society transactions · 2017
    Review
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

6 authors at 2 institutions in 2 countries.

Christine S HoppDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, 21205, USA. chopp1@jhu.edu.
Amanda E BalabanDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, 21205, USA.
Ellen S C BushellWellcome Trust Sanger Institute, Hinxton, CB10 1SA, UK.
Oliver BillkerWellcome Trust Sanger Institute, Hinxton, CB10 1SA, UK.
Julian C RaynerWellcome Trust Sanger Institute, Hinxton, CB10 1SA, UK. julian.rayner@sanger.ac.uk.
Photini SinnisDepartment of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD, 21205, USA. psinnis1@jhu.edu.
Johns Hopkins University · USWellcome Sanger Institute · GB

Funding

Structure and Function of the Circumsporozoite ProteinR01AI056840 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SINNIS, PHOTINI · 2005 to 2014
$3.8M
NIAID NIH HHS R01 AI056840Wellcome Trust
6 · The paper itself

Abstract

As the Plasmodium parasite transitions between mammalian and mosquito host, it has to adjust quickly to new environments. Palmitoylation, a reversible and dynamic lipid post-translational modification, plays a central role in regulating this process and has been implicated with functions for parasite morphology, motility and host cell invasion. While proteins associated with the gliding motility machinery have been described to be palmitoylated, no palmitoyl transferase responsible for regulating gliding motility has previously been identified. Here, we characterize two palmityol transferases with gene tagging and gene deletion approaches. We identify DHHC3, a palmitoyl transferase, as a mediator of ookinete development, with a crucial role for gliding motility in ookinetes and sporozoites, and we co-localize the protein with a marker for the inner membrane complex in the ookinete stage. Ookinetes and sporozoites lacking DHHC3 are impaired in gliding motility and exhibit a strong phenotype in vivo; with ookinetes being significantly less infectious to their mosquito host and sporozoites being non-infectious to mice. Importantly, genetic complementation of the DHHC3-ko parasite completely restored virulence. We generated parasites lacking both DHHC3, as well as the palmitoyl transferase DHHC9, and found an enhanced phenotype for these double knockout parasites, allowing insights into the functional overlap and compensational nature of the large family of PbDHHCs. These findings contribute to our understanding of the organization and mechanism of the gliding motility machinery, which as is becoming increasingly clear, is mediated by palmitoylation.

Indexed as

AcyltransferasesAnimalsAnophelesHep G2 CellsHost-Parasite InteractionsHumansLipoylationLiverMiceOocystsPlasmodium bergheiProtein Processing, Post-TranslationalProtozoan ProteinsSalivary GlandsSporozoitesAcyltransferasesProtozoan Proteins

Identifiers

PMID27084458
PMCPMC5565149
OpenAlexW2340010299

What OpenQuestion holds

Textmetadata
LicenceTDM
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.