Evidence map›Paper›PMID 40172085›Full record

ArticleThe FEBS journal2025

Fine-tuning regulation of (p)ppGpp-driven outer membrane vesicle formation in Acinetobacter baumannii.

Sunyong Han, Jihyeon Min, Yerim Park, Woojun Park

Abstract read
PubMed Publisher
In one paragraph

Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Sphingolipid-mediated vesiculation in multidrug-resistantApplied and environmental microbiology · 2025
    Article
  4. Article
  5. Signaling inComputational and structural biotechnology journal · 2025
    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

4 authors.

Sunyong HanLaboratory of Molecular Environmental Microbiology, Department of Environmental Science and Ecological Engineering, Korea University, Seoul, Korea.ORCID https://orcid.org/0009-0000-0216-8278
Jihyeon MinLaboratory of Molecular Environmental Microbiology, Department of Environmental Science and Ecological Engineering, Korea University, Seoul, Korea.
Yerim ParkLaboratory of Molecular Environmental Microbiology, Department of Environmental Science and Ecological Engineering, Korea University, Seoul, Korea.
Woojun ParkLaboratory of Molecular Environmental Microbiology, Department of Environmental Science and Ecological Engineering, Korea University, Seoul, Korea.ORCID https://orcid.org/0000-0002-3166-1528

Funding

National Research Foundation of Korea NRF-2023R1A2C1005834
6 · The paper itself

Abstract

The roles of (p)ppGpp in regulating cytosolic proteins are well established; however, their effects on membrane remodeling remain elusive. The translocation of signal recognition particle (SRP)-dependent proteins can be modulated through (p)ppGpp binding to two key GTPase components: FtsY, which interacts with SecYEG, and Ffh, a homolog of SRP54. A (p)ppGpp-specific Broccoli RNA aptamer and the chemometer PyDPA were used to quantify the (p)ppGpp levels in the ΔrelA and ΔrelA/ΔspoT strains of Acinetobacter baumannii, confirming a stepwise reduction in (p)ppGpp levels in the following order: wild-type > ΔrelA > ΔrelA/ΔspoT. The ΔrelA strain, with intermediate (p)ppGpp levels, exhibited increased outer membrane vesicle (OMV) production, whereas the ΔrelA/ΔspoT strain exhibited reduced production, highlighting a non-linear relationship between OMV production and (p)ppGpp levels. Scanning and transmission electron microscopy revealed (p)ppGpp-dependent changes in cell envelope integrity: the relA mutant exhibited outer membrane disruption leading to OMV formation, whereas the relA/spoT mutant maintained an intact outer membrane, suggesting that membrane stability is modulated by fine-tuned (p)ppGpp levels. Western blotting and proteomic analyses identified significant OmpA accumulation in the inner membrane of the ΔrelA/ΔspoT strain, and an accumulation of SRP-dependent inner membrane proteins, including NuoB, NuoL, and TolA, in the ΔrelA strain. These findings indicate that (p)ppGpp levels are crucial for regulating membrane protein incorporation in A. baumannii. Regulation of (p)ppGpp levels using the CRISPRi system revealed that outer membrane disruption and OMV formation peaked at intermediate (p)ppGpp concentrations, highlighting the importance of precise (p)ppGpp adjustment in regulating bacterial phenotypes.

Indexed as

Acinetobacter baumanniiBacterial Outer MembraneBacterial Outer Membrane ProteinsGuanosine PentaphosphateBacterial ProteinsGene Expression Regulation, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsGuanosine PentaphosphateCRISPRimembrane disruptionouter membrane vesicle(p)ppGpp levelprotein crowding

Identifiers

PMID40172085

What OpenQuestion holds

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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.