Evidence map›Paper›PMID 37001523›Full record

ArticleStructure (London, England : 1993)2023

Three structural solutions for bacterial adhesion pilus stability and superelasticity.

Matthew H Doran, Joseph L Baker, Tobias Dahlberg, Magnus Andersson, Esther Bullitt

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. CryoSeek: A strategy for bioentity discovery using cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. 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

5 authors at 3 institutions in 2 countries.

Matthew H DoranDepartment of Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, Boston, MA 02118, USA.
Joseph L BakerDepartment of Chemistry, The College of New Jersey, Ewing, NJ 08628, USA.
Tobias DahlbergDepartment of Physics, Umeå University, Umeå, Sweden.
Magnus AnderssonDepartment of Physics, Umeå University, Umeå, Sweden; Umeå Centre for Microbial Research (UCMR), Umeå University, Umeå, Sweden.
Esther BullittDepartment of Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, Boston, MA 02118, USA. Electronic address: bullitt@bu.edu.
Boston University · USUmeå University · SECollege of New Jersey · US

Funding

Midwest Consortium for High Resolution Cryoelectron MicroscopyU24GM116789 · NIGMS · PURDUE UNIVERSITY · PI BULLITT, ESTHER, DAI, WEI · 2017 to 2021
$3.5M
Seeing Protein Mechanics: The Link Between Molecular Structure, Function, and EvolutionR01GM123456 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI RANGANATHAN, RAMA · 2016 to 2020
$2.0M
Exploiting the Salivary Arsenal to Inhibit Diarrheal DiseaseR21AI156236 · NIAID · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 2021 to 2022
$466k
NIAID NIH HHS R21 AI156236NIGMS NIH HHS R01 GM123456NIGMS NIH HHS U24 GM116789
6 · The paper itself

Abstract

Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis underpinning the biophysical properties of pili originating from enterotoxigenic (ETEC) and uropathogenic bacteria. Using cryo-electron microscopy we solved the structures of three vaccine target pili from ETEC bacteria, CFA/I, CS17, and CS20. Pairing these and previous pilus structures with force spectroscopy and steered molecular dynamics simulations, we find a strong correlation between subunit-subunit interaction energies and the force required for pilus unwinding, irrespective of genetic similarity. Pili integrate three structural solutions for stabilizing their assemblies: layer-to-layer interactions, N-terminal interactions to distant subunits, and extended loop interactions from adjacent subunits. Tuning of these structural solutions alters the biophysical properties of pili and promotes the superelastic behavior that is essential for sustained bacterial attachment.

Indexed as

Bacterial AdhesionFimbriae ProteinsCryoelectron MicroscopyFimbriae, BacterialFimbriae Proteinsbacterial adhesioncryo-EMenterotoxigenic Escherichia colifimbriaeforce spectroscopymolecular modelingoptical tweezerspilisteered molecular dynamicsTraveler's diarrhea

Identifiers

PMID37001523
PMCPMC10164138
OpenAlexW4361269724

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.