Evidence map›Paper›PMID 40897170›Full record

ArticleStructure (London, England : 1993)2025

Characterization of the OMP biogenesis machinery in Fusobacterium nucleatum.

Claire Overly Cottom, Eva Heinz, Satchal Erramilli, Anthony Kossiakoff, Daniel J Slade, Nicholas Noinaj

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

6 authors.

Claire Overly CottomDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.
Eva HeinzStrathclyde Institute of Pharmacy & Biomedical Sciences, University of Strathclyde, Glasgow, UK; Parasites and Microbes Program, Wellcome Sanger Institute, Hinxton, UK.
Satchal ErramilliDepartment of Biochemistry and Molecular Biophysics, University of Chicago, Chicago, IL, USA; Meso Scale Diagnostics, LLC., Rockville, MD, USA.
Anthony KossiakoffDepartment of Biochemistry and Molecular Biophysics, University of Chicago, Chicago, IL, USA.
Daniel J SladeDepartment of Biochemistry, Virginia Tech, Blacksburg, VA, USA.
Nicholas NoinajDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA; Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA; Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN, USA. Electronic address: nnoinaj@purdue.edu.

Funding

The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
Neisseria gonorrhoeae metal transporters that subvert nutritional immunityR01AI127793 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CYNTHIA N CORNELISSEN, Alison K Criss · 2017 to 2026
$6.8M
Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
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
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
NIAID NIH HHS R01 AI127793NIAID NIH HHS T32 AI148103NIGMS NIH HHS P30 GM138395NIGMS NIH HHS R01 GM117372NIGMS NIH HHS R01 GM127884NIGMS NIH HHS R01 GM127896NIH HHS S10 OD018090Wellcome Trust
6 · The paper itself

Abstract

F. nucleatum is a Gram-negative bacteria that causes oral infections and is linked to colorectal cancer. Pathogenicity relies on a type of β-barrel outer membrane protein (OMP) called an autotransporter. The biogenesis of OMPs is typically mediated by the barrel assembly machinery (BAM) complex. In this study, we investigate the evolution, composition, and structure of the OMP biogenesis machinery in F. nucleatum. Our bioinformatics and proteomics analyses indicate that OMP biogenesis in F. nucleatum is mediated solely by the core component BamA. The structure of FnBamA highlights distinct features, including four POTRA domains and a C-terminal 16-stranded β-barrel domain observed as an inverted dimer. FnBamA represents the original composition of the assembly machinery, and a duplication event that resulted in BamA and TamA occurred after the split of other lineages, including the Proteobacteria, from the Fusobacteria. FnBamA, therefore, likely serves a singular role in the biogenesis of all OMPs.

Indexed as

Bacterial Outer Membrane ProteinsFusobacterium nucleatumCrystallography, X-RayModels, MolecularPhylogenyProtein DomainsProtein MultimerizationBacterial Outer Membrane ProteinsFusobacterium nucleatumMembrane ProteinProtein FoldingProteomicsStructural Biology

Identifiers

PMID40897170
PMCPMC12646852

What OpenQuestion holds

Textmetadata
LicenceTDM
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.