Evidence map›Paper›PMID 29599244›Full record

ArticleScience (New York, N.Y.)2018

Molecular mechanism of extreme mechanostability in a pathogen adhesin.

Lukas F Milles, Klaus Schulten, Hermann E Gaub, Rafael C Bernardi

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing 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

101 citing papers in PubMed.

  1. Article
  2. Forces in mechanically interlocked materials.Chemical Society reviews · 2026
    Review
  3. Article
  4. Silanes to Silatranes: Robust Functionalization for Single-Molecule Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. UltrastrongScience advances · 2025
    Article
  14. Article
  15. Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  16. Review
  17. Article
  18. The sticky situation of human skin.Journal of biosciences · 2025
    Article
  19. The strongest protein binder is surprisingly labile.Protein science : a publication of the Protein Society · 2024
    Article
  20. Review

41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Lukas F MillesLehrstuhl für Angewandte Physik and Center for Nanoscience, Ludwig-Maximilians-University, Amalienstrasse 54, 80799 Munich, Germany.ORCID 0000-0001-8417-3205
Klaus SchultenNIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Hermann E GaubLehrstuhl für Angewandte Physik and Center for Nanoscience, Ludwig-Maximilians-University, Amalienstrasse 54, 80799 Munich, Germany. rcbernardi@ks.uiuc.edu gaub@lmu.de.ORCID 0000-0002-4220-6088
Rafael C BernardiNIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. rcbernardi@ks.uiuc.edu gaub@lmu.de.ORCID 0000-0003-0758-2026

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
European Research Council 294438NIGMS NIH HHS P41 GM104601
6 · The paper itself

Abstract

High resilience to mechanical stress is key when pathogens adhere to their target and initiate infection. Using atomic force microscopy-based single-molecule force spectroscopy, we explored the mechanical stability of the prototypical staphylococcal adhesin SdrG, which targets a short peptide from human fibrinogen β. Steered molecular dynamics simulations revealed, and single-molecule force spectroscopy experiments confirmed, the mechanism by which this complex withstands forces of over 2 nanonewtons, a regime previously associated with the strength of a covalent bond. The target peptide, confined in a screwlike manner in the binding pocket of SdrG, distributes forces mainly toward the peptide backbone through an intricate hydrogen bond network. Thus, these adhesins can attach to their target with exceptionally resilient mechanostability, virtually independent of peptide side chains.

Indexed as

Stress, MechanicalAdhesins, BacterialBacterial ProteinsCarrier ProteinsFibrinogenHumansHydrogen BondingMicroscopy, Atomic ForceMolecular Dynamics SimulationPhenylalanineSingle-Cell AnalysisAdhesins, BacterialBacterial ProteinsCarrier ProteinsFbe protein, bacteriaFGB protein, humanFibrinogenPhenylalanine

Identifiers

PMID29599244
PMCPMC6451932

What OpenQuestion holds

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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.