Evidence map›Paper›PMID 32859904›Full record

ArticleNature communications2020

High force catch bond mechanism of bacterial adhesion in the human gut.

Zhaowei Liu, Haipei Liu, Andrés M Vera, Rafael C Bernardi, Philip Tinnefeld, Michael A Nash

Abstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. UltrastrongScience advances · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. De novo DNA-based catch bonds.Nature chemistry · 2024
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Interaction of theACS nanoscience Au · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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.

Zhaowei LiuInstitute of Physical Chemistry, Department of Chemistry, University of Basel, 4058, Basel, Switzerland.ORCID http://orcid.org/0000-0001-8214-8882
Haipei LiuInstitute of Physical Chemistry, Department of Chemistry, University of Basel, 4058, Basel, Switzerland.ORCID http://orcid.org/0000-0002-8724-5400
Andrés M VeraFaculty of Chemistry and Center for NanoScience, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID http://orcid.org/0000-0002-3932-8236
Rafael C BernardiNIH Center for Macromolecular Modeling and Bioinformatics, Theoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, 61801, Urbana, IL, USA.ORCID http://orcid.org/0000-0003-0758-2026
Philip TinnefeldFaculty of Chemistry and Center for NanoScience, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID http://orcid.org/0000-0003-4290-7770
Michael A NashInstitute of Physical Chemistry, Department of Chemistry, University of Basel, 4058, Basel, Switzerland. michael.nash@unibas.ch.ORCID http://orcid.org/0000-0003-3842-1567

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
NIGMS NIH HHS P41 GM104601
6 · The paper itself

Abstract

Bacterial colonization of the human intestine requires firm adhesion of bacteria to insoluble substrates under hydrodynamic flow. Here we report the molecular mechanism behind an ultrastable protein complex responsible for resisting shear forces and adhering bacteria to cellulose fibers in the human gut. Using single-molecule force spectroscopy (SMFS), single-molecule FRET (smFRET), and molecular dynamics (MD) simulations, we resolve two binding modes and three unbinding reaction pathways of a mechanically ultrastable R. champanellensis (Rc) Dockerin:Cohesin (Doc:Coh) complex. The complex assembles in two discrete binding modes with significantly different mechanical properties, with one breaking at ~500 pN and the other at ~200 pN at loading rates from 1-100 nN s

Indexed as

Mechanical PhenomenaPhysical PhenomenaBacteriaBacterial AdhesionCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsGastrointestinal MicrobiomeGastrointestinal TractGene Knockout TechniquesHumansKineticsMolecular Dynamics SimulationMonte Carlo MethodProtein BindingProtein ConformationCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesins

Identifiers

PMID32859904
PMCPMC7456326

What OpenQuestion holds

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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.