Evidence map›Paper›PMID 27436892›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Direct targeting of membrane fusion by SNARE mimicry: Convergent evolution of Legionella effectors.

Xingqi Shi, Partho Halder, Halenur Yavuz, Reinhard Jahn, Howard A Shuman

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.4field-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

29 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. ThemSphere · 2025
    Article
  5. Review
  6. Journal of bacteriology · 2024
    Review
  7. Article
  8. Article
  9. A look beyond the QR code of SNARE proteins.Protein science : a publication of the Protein Society · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Glycosylating Effectors ofBiomolecules · 2022
    Review
  15. Article
  16. Article
  17. Affecting the Effectors: Regulation ofPathogens (Basel, Switzerland) · 2021
    Review
  18. Idiosyncratic Biogenesis of Intracellular Pathogens-Containing Vacuoles.Frontiers in cellular and infection microbiology · 2021
    Review
  19. Review
  20. 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

5 authors at 2 institutions in 2 countries.

Xingqi ShiDepartment of Microbiology, University of Chicago, Chicago, IL 60637;
Partho HalderDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany.
Halenur YavuzDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany.
Reinhard JahnDepartment of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany rjahn@gwdg.de hashuman@uchicago.edu.ORCID 0000-0003-1542-3498
Howard A ShumanDepartment of Microbiology, University of Chicago, Chicago, IL 60637; rjahn@gwdg.de hashuman@uchicago.edu.
Max Planck Institute for Biophysical Chemistry · DEUniversity of Chicago · US

Funding

GENETICS OF MONOCYTE KILLING BY BACTERIAR01AI023549 · NIAID · UNIVERSITY OF CHICAGO · PI SHUMAN, HOWARD A · 1986 to 2013
$6.8M
NIAID NIH HHS R01 AI023549
6 · The paper itself

Abstract

Legionella pneumophila, the Gram-negative pathogen causing Legionnaires' disease, infects host cells by hijacking endocytic pathways and forming a Legionella-containing vacuole (LCV) in which the bacteria replicate. To promote LCV expansion and prevent lysosomal targeting, effector proteins are translocated into the host cell where they alter membrane traffic. Here we show that three of these effectors [LegC2 (Legionella eukaryotic-like gene C2)/YlfB (yeast lethal factor B), LegC3, and LegC7/YlfA] functionally mimic glutamine (Q)-SNARE proteins. In infected cells, the three proteins selectively form complexes with the endosomal arginine (R)-SNARE vesicle-associated membrane protein 4 (VAMP4). When reconstituted in proteoliposomes, these proteins avidly fuse with liposomes containing VAMP4, resulting in a stable complex with properties resembling canonical SNARE complexes. Intriguingly, however, the LegC/SNARE hybrid complex cannot be disassembled by N-ethylmaleimide-sensitive factor. We conclude that LegCs use SNARE mimicry to divert VAMP4-containing vesicles for fusion with the LCV, thus promoting its expansion. In addition, the LegC/VAMP4 complex avoids the host's disassembly machinery, thus effectively trapping VAMP4 in an inactive state.

Indexed as

Membrane FusionBacterial ProteinsCell Line, TumorCell SurvivalEndosomesHost-Pathogen InteractionsHumansLegionella pneumophilaMacrophagesProtein BindingQ-SNARE ProteinsRNA InterferenceR-SNARE ProteinsTransport VesiclesVacuolesBacterial ProteinsQ-SNARE ProteinsR-SNARE ProteinsVAMP4 protein, humanLegionella pneumophilamembrane fusionNSFSNAREs

Identifiers

PMID27436892
PMCPMC4978295
OpenAlexW2503226155

What OpenQuestion holds

Textmetadata
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.