ArticleProceedings of the National Academy of Sciences of the United States of America2016
CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 67 citations in OpenAlex.
- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- UltrastrongScience advances · 2025Article
- Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.The Journal of cell biology · 2025Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Optimal Sacrificial Domains in Mechanical Polyproteins:JACS Au · 2022Article
- Protein nanowires with tunable functionality and programmable self-assembly using sequence-controlled synthesis.Nature communications · 2022Article
- Pan-genomic analysis ofFrontiers in microbiology · 2022Article
- An ester bond underlies the mechanical strength of a pathogen surface protein.Nature communications · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Protein folding modulates the chemical reactivity of a Gram-positive adhesin.Nature chemistry · 2021Article
- Review
- New Paradigms of Pilus Assembly Mechanisms in Gram-Positive Actinobacteria.Trends in microbiology · 2020Review
- Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme fromBioconjugate chemistry · 2020Article
- How Microbes Use Force To Control Adhesion.Journal of bacteriology · 2020Review
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- A Fast, Efficient and Easy to Implement Method to Purify Bacterial Pili FromFrontiers in microbiology · 2020Article
- Cell-to-cell interaction requires optimal positioning of a pilus tip adhesin modulated by gram-positive transpeptidase enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Pathogenic bacteria adhere despite severe mechanical perturbations induced by the host, such as coughing. In Gram-positive bacteria, extracellular protein appendages termed pili are necessary for adherence under mechanical stress. However, little is known about the behavior of Gram-positive pili under force. Here, we demonstrate a mechanism by which Gram-positive pili are able to dissipate mechanical energy through mechanical unfolding and refolding of isopeptide bond-delimited polypeptide loops present in Ig-type CnaA domains. Using single-molecule force spectroscopy, we find that these loops of the pilus subunit SpaA of the SpaA-type pilus from Corynebacterium diphtheriae and FimA of the type 2 pilus from Actinomyces oris unfold and extend at forces that are the highest yet reported for globular proteins. Loop refolding is limited by the hydrophobic collapse of the polypeptide and occurs in milliseconds. Remarkably, both SpaA and FimA initially refold to mechanically weaker intermediates that recover strength with time or ligand binding. Based on the high force extensibility, CnaA-containing pili can dissipate ∼28-fold as much energy compared with their inextensible counterparts before reaching forces sufficient to cleave covalent bonds. We propose that efficient mechanical energy dissipation is key for sustained bacterial attachment against mechanical perturbations.
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