Evidence map›Paper›PMID 39900531›Full record

ArticleJournal of the American Chemical Society2025

Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.

Jana S Anton, Ioan Iacovache, Juan F Bada Juarez, Luciano A Abriata, Louis W Perrin, Chan Cao, Maria J Marcaida, Benoît Zuber, Matteo Dal Peraro

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Aerolysin-like proteins fromFrontiers in fungal biology · 2026
    Article
  5. Article
  6. 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

9 authors.

Jana S AntonInstitute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.ORCID 0009-0003-0165-8752
Ioan IacovacheInstitute of Anatomy, University of Bern, Baltzerstrasse 2, 3012 Bern, Switzerland.
Juan F Bada JuarezInstitute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.ORCID 0000-0002-1337-6424
Luciano A AbriataInstitute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.ORCID 0000-0003-3087-8677
Louis W PerrinDepartment of Inorganic and Analytical Chemistry, Chemistry and Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
Chan CaoDepartment of Inorganic and Analytical Chemistry, Chemistry and Biochemistry, University of Geneva, 1211 Geneva, Switzerland.ORCID 0000-0003-2592-0690
Maria J MarcaidaInstitute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.
Benoît ZuberInstitute of Anatomy, University of Bern, Baltzerstrasse 2, 3012 Bern, Switzerland.ORCID 0000-0001-7725-5579
Matteo Dal PeraroInstitute of Bioengineering, School of Life Sciences, École Polytechnique Fédérale de Lausanne, 1015 Lausanne, Switzerland.ORCID 0000-0002-2973-3975

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aerolysin is a β-pore-forming toxin produced by most Aeromonas bacteria, which has attracted large attention in the field of nanopore sensing due to its narrow and charged pore lumen. Structurally similar proteins, belonging to the aerolysin-like family, are present throughout all kingdoms of life, but very few of them have been structurally characterized in a lipid environment. Here, we present the first high-resolution atomic cryo-EM structures of aerolysin prepore and pore in a membrane-like environment. These structures allow the identification of key interactions, which are relevant for understanding the pore formation mechanism and for correctly positioning the pore β-barrel and its anchoring β-turn motif in the membrane. Moreover, we elucidate at high resolution the architecture of key pore mutations and precisely identify four constriction rings in the pore lumen that are highly relevant for nanopore sensing experiments.

Indexed as

Bacterial ToxinsNanoporesPore Forming Cytotoxic ProteinsCryoelectron MicroscopyLipid BilayersModels, MolecularaerolysinBacterial ToxinsLipid BilayersPore Forming Cytotoxic Proteins

Identifiers

PMID39900531
PMCPMC11826888

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.