Evidence map›Paper›PMID 38305166›Full record

ArticlemSphere2024

Redundant essentiality of AsmA-like proteins in

Davide Sposato, Jessica Mercolino, Luisa Torrini, Paola Sperandeo, Massimiliano Lucidi, Riccardo Alegiani, Ilaria Varone, Giorgia Molesini, Livia Leoni, Giordano Rampioni and 2 more

Open access · goldAbstract read
In one paragraph

Article in mSphere, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
9.9field-weighted citation impact, top 2% 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

21 citing papers in PubMed, 19 citations in OpenAlex.

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  20. Frontiers in immunology · 2024
    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

12 authors at 2 institutions in 1 country.

Davide Sposato *Department of Science, University Roma Tre, Rome, Italy.
Jessica Mercolino *Department of Science, University Roma Tre, Rome, Italy.
Luisa TorriniDepartment of Science, University Roma Tre, Rome, Italy.
Paola SperandeoDepartment of Pharmacological and Biomolecular Sciences, University of Milano, Milan, Italy.ORCID 0000-0001-9573-5672
Massimiliano LucidiDepartment of Science, University Roma Tre, Rome, Italy.ORCID 0000-0003-3238-9164
Riccardo AlegianiDepartment of Science, University Roma Tre, Rome, Italy.
Ilaria VaroneDepartment of Science, University Roma Tre, Rome, Italy.
Giorgia MolesiniDepartment of Science, University Roma Tre, Rome, Italy.
Livia LeoniDepartment of Science, University Roma Tre, Rome, Italy.
Giordano RampioniDepartment of Science, University Roma Tre, Rome, Italy.ORCID 0000-0002-1735-8565
Paolo ViscaDepartment of Science, University Roma Tre, Rome, Italy.ORCID 0000-0002-6128-7039
Francesco ImperiDepartment of Science, University Roma Tre, Rome, Italy.ORCID 0000-0001-5080-5665
Roma Tre University · ITUniversity of Milan · IT

Funding

Italian Ministry of University and Research Excellence DepartmentsItalian Ministry of University and Research PRIN 2017 - 20177J5Y3PItalian Ministry of University and Research PRIN 2020 - 202089LLEHItalian Ministry of University and Research PRIN 2020 - 20208LLXEJItalian Ministry of University and Research PRIN 2022 - 20224BYR59
6 · The paper itself

Abstract

The outer membrane (OM) is an essential structure of Gram-negative bacteria that provides mechanical strength and protection from large and/or hydrophobic toxic molecules, including many antibiotics. The OM is composed of glycerophospholipids (GPLs) and lipopolysaccharide (LPS) in the inner and outer leaflets, respectively, and hosts integral β-barrel proteins and lipoproteins. While the systems responsible for translocation and insertion of LPS and OM proteins have been elucidated, the mechanism(s) mediating transport of GPLs from the inner membrane to the OM has remained elusive for decades. Very recently, studies performed in IMPORTANCE: Given the importance of the outer membrane (OM) for viability and antibiotic resistance in Gram-negative bacteria, in the last decades, several studies have focused on the characterization of the systems involved in OM biogenesis, which have also been explored as targets for antibacterial drug development. However, the mechanism mediating translocation of glycerophospholipids (GPLs) to the OM remained unknown until recent studies provided evidence that AsmA-like proteins could be responsible for this process. Here, we demonstrate for the first time that AsmA-like proteins are essential and redundant for growth and OM integrity in a Gram-negative bacterium other than the model organism

Indexed as

Escherichia coliPseudomonas aeruginosaAnti-Bacterial AgentsBacterial Outer Membrane ProteinsGlycerophospholipidsHumansLipopolysaccharidesAnti-Bacterial AgentsBacterial Outer Membrane ProteinsGlycerophospholipidsLipopolysaccharidesepaFglycerophospholipid transportouter membranePA2708PA4735TamATamBYdbHYhdP

Identifiers

PMID38305166
PMCPMC10900882
OpenAlexW4391472814

What Socratic 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 Socratic graph.