Evidence map›Paper›PMID 40988583›Full record

ReviewJournal of cell science2025

Surface protein machineries in Gram-negative bacteria.

Claire Overly Cottom, Evan Billings, Michelle Bush, Dorothy DRozario, Wyatt Scherschel, Nicholas Noinaj

Abstract readReview
In one paragraph

Review in Journal of cell science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Claire Overly CottomMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.
Evan BillingsMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.
Michelle BushMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.
Dorothy DRozarioMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.
Wyatt ScherschelMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.
Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences, Purdue University, West Lafayette, IN47907, USA.ORCID 0000-0001-6361-2336

Funding

Neisseria gonorrhoeae metal transporters that subvert nutritional immunityR01AI127793 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CYNTHIA N CORNELISSEN, Alison K Criss · 2017 to 2026
$6.8M
Purdue University Molecular Biophysics Training ProgramT32GM132024 · NIGMS · PURDUE UNIVERSITY · PI Angeline Marie Lyon, John Tesmer · 2019 to 2026
$2.0M
Structural Characterization of the TOC Protein Translocon MachineryR01GM127896 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2018 to 2022
$1.5M
Unraveling the mechanism by which the BAM complex mediates OMP biogenesisR01GM127884 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2019 to 2022
$1.2M
Drug Discovery in Infectious Disease TrainingT32AI148103 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL, YEO, YOON · 2020 to 2024
$949k
American Heart Association 909066NIAID NIH HHS R01 AI127793NIAID NIH HHS T32 AI148103NIGMS NIH HHS R01 GM127884NIGMS NIH HHS R01 GM127896NIGMS NIH HHS T32 GM132024NIH HHS 1R01AI127793NIH HHS 1R01GM127884NIH HHS 1R01GM127896NIH HHS T32AI148103NIH HHS T32GM132024
6 · The paper itself

Abstract

The major feature that distinguishes Gram-negative bacteria from Gram-positive bacteria is the presence of both an inner and outer membrane. Both membranes contain lipoproteins, peripheral membrane proteins, α-helical membrane proteins and a host of β-barrel membrane proteins. However, the vast majority of outer membrane proteins (OMPs) are β-barrel proteins, with a few select α-helical exceptions. In this Review, we provide a general overview of many of the proteins and protein machineries essential for cell survival that are commonly found on the surface of Gram-negative bacteria. Many of these proteins also serve important roles in mediating virulence in pathogenic strains, making them promising drug and vaccine targets. Examples include the β-barrel assembly machinery (BAM) complex, which is involved in the biogenesis and assembly of OMPs; surface lipoprotein assembly modulator 1 (Slam1), which is involved in the presentation of lipoproteins at the surface; efflux pumps, which remove potentially harmful substrates; as well as the protein assemblies that comprise pili and flagella. The structures of these protein machineries and the underlying mechanisms responsible for their function create a complex and dynamic surface landscape that must adapt quickly to ever-changing environmental conditions.

Indexed as

Bacterial Outer Membrane ProteinsGram-Negative BacteriaLipoproteinsBacterial Outer Membrane ProteinsLipoproteinsMembrane proteinsProtein assembliesProtein biogenesis

Identifiers

PMID40988583
PMCPMC12615155

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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.