Evidence map›Paper›PMID 37673860›Full record

ArticleNature communications2023

Visualizing the membrane disruption action of antimicrobial peptides by cryo-electron tomography.

Eric H-L Chen, Chun-Hsiung Wang, Yi-Ting Liao, Feng-Yueh Chan, Yui Kanaoka, Takayuki Uchihashi, Koichi Kato, Longsheng Lai, Yi-Wei Chang, Meng-Chiao Ho and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

52 citing papers in PubMed, 77 citations in OpenAlex.

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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

11 authors at 5 institutions in 3 countries.

Eric H-L Chen *Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.
Chun-Hsiung Wang *Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.ORCID http://orcid.org/0000-0003-2242-7200
Yi-Ting Liao *Institute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan.ORCID http://orcid.org/0000-0001-5050-7481
Feng-Yueh ChanDepartment of Physics, Nagoya University, Nagoya, 464-8602, Japan.ORCID http://orcid.org/0000-0002-4879-6015
Yui KanaokaDepartment of Physics, Nagoya University, Nagoya, 464-8602, Japan.
Takayuki UchihashiDepartment of Physics, Nagoya University, Nagoya, 464-8602, Japan.ORCID http://orcid.org/0000-0002-0263-5312
Koichi KatoExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Aichi, 444-8787, Japan.
Longsheng LaiDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-6059, USA.
Yi-Wei ChangDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-6059, USA.ORCID http://orcid.org/0000-0003-2391-473X
Meng-Chiao HoInstitute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan. joeho@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0002-5424-4524
Rita P-Y ChenInstitute of Biological Chemistry, Academia Sinica, Taipei, 11529, Taiwan. pyc@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0003-3987-033X
Institute of Biological Chemistry, Academia Sinica · TWNagoya University · JPNational Institutes of Natural Sciences · JPNational Taiwan University · TWUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The abuse of antibiotics has led to the emergence of multidrug-resistant microbial pathogens, presenting a pressing challenge in global healthcare. Membrane-disrupting antimicrobial peptides (AMPs) combat so-called superbugs via mechanisms different than conventional antibiotics and have good application prospects in medicine, agriculture, and the food industry. However, the mechanism-of-action of AMPs has not been fully characterized at the cellular level due to a lack of high-resolution imaging technologies that can capture cellular-membrane disruption events in the hydrated state. Previously, we reported PepD2M, a de novo-designed AMP with potent and wide-spectrum bactericidal and fungicidal activity. In this study, we use cryo-electron tomography (cryo-ET) and high-speed atomic force microscopy (HS-AFM) to directly visualize the pepD2M-induced disruption of the outer and inner membranes of the Gram-negative bacterium Escherichia coli, and compared with a well-known pore-forming peptide, melittin. Our high-resolution cryo-ET images reveal how pepD2M disrupts the E. coli membrane using a carpet/detergent-like mechanism. Our studies reveal the direct membrane-disrupting consequence of AMPs on the bacterial membrane by cryo-ET, and this information provides critical insights into the mechanisms of this class of antimicrobial agents.

Indexed as

Antimicrobial PeptidesElectron Microscope TomographyAnti-Bacterial AgentsCell Physiological PhenomenaEscherichia coliAnti-Bacterial AgentsAntimicrobial Peptides

Identifiers

PMID37673860
PMCPMC10482868
OpenAlexW4386483189

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.