Evidence map›Paper›PMID 21679290›Full record

ArticleCellular microbiology2011

Coiled-coil domains enhance the membrane association of Salmonella type III effectors.

Leigh A Knodler, J Antonio Ibarra, Ernesto Pérez-Rueda, Calvin K Yip, Olivia Steele-Mortimer

Abstract read
In one paragraph

Article in Cellular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Atomic Structure and Phospholipid Binding Properties of thebioRxiv : the preprint server for biology · 2025
    Article
  3. Functional Divergence of the ParalogInternational journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier.Journal of controlled release : official journal of the Controlled Release Society · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

5 authors.

Leigh A KnodlerLaboratory of Intracellular Parasites, Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana, USA. lknodler@niaid.nih.gov
J Antonio Ibarra
Ernesto Pérez-Rueda
Calvin K Yip
Olivia Steele-Mortimer

Funding

The Salmonella-Containing VacuoleZIAAI000909 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI STEELE-MORTIMER, OLIVIA · 2009 to 2025
$12.9M
Salmonella-Host Cell InteractionsZIAAI001111 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI STEELE-MORTIMER, OLIVIA · 2009 to 2018
$5.6M
Intramural NIH HHS Z99 AI999999Intramural NIH HHS ZIA AI000909Intramural NIH HHS ZIA AI001111NIAID NIH HHS Y99 AI999999
6 · The paper itself

Abstract

Coiled-coil domains in eukaryotic and prokaryotic proteins contribute to diverse structural and regulatory functions. Here we have used in silico analysis to predict which proteins in the proteome of the enteric pathogen, Salmonella enterica serovar Typhimurium, harbour coiled-coil domains. We found that coiled-coil domains are especially prevalent in virulence-associated proteins, including type III effectors. Using SopB as a model coiled-coil domain type III effector, we have investigated the role of this motif in various aspects of effector function including chaperone binding, secretion and translocation, protein stability, localization and biological activity. Compared with wild-type SopB, SopB coiled-coil mutants were unstable, both inside bacteria and after translocation into host cells. In addition, the putative coiled-coil domain was required for the efficient membrane association of SopB in host cells. Since many other Salmonella effectors were predicted to contain coiled-coil domains, we also investigated the role of this motif in their intracellular targeting in mammalian cells. Mutation of the predicted coiled-coil domains in PipB2, SseJ and SopD2 also eliminated their membrane localization in mammalian cells. These findings suggest that coiled-coil domains represent a common membrane-targeting determinant for Salmonella type III effectors.

Indexed as

Cell MembraneComputational BiologyMolecular ChaperonesMutagenesis, Site-DirectedMutant ProteinsMutation, MissenseProtein BindingProtein ConformationProtein StabilityProtein Structure, TertiaryProtein TransportSalmonella typhimuriumVirulence FactorsMolecular ChaperonesMutant ProteinsVirulence Factors

Identifiers

PMID21679290
PMCPMC3418822

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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.