ArticleNature communications2021
An ester bond underlies the mechanical strength of a pathogen surface protein.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 44 citations in OpenAlex.
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- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- Dual Micromechanical Interlocking Through Filler Surface Modification for Enhanced Dental Composites.Polymers · 2025Article
- Multi-state catch bond formed in the Izumo1:Juno complex that initiates human fertilization.Nature communications · 2025Article
- Protease mimicry: Dissecting the ester bond crosslinking mechanics in bacterial adhesin proteins.Protein science : a publication of the Protein Society · 2025Article
- Application of photodynamic activation of prodrugs combined with phototherapy in tumor treatment.Molecular cancer · 2025Review
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Tailorable biosensors for real-time monitoring of stress distribution in soft biomaterials and living tissues.Nature communications · 2025Article
- Folds from fold: Exploring topological isoforms of a single-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular Mechanism of Interaction between DNA Aptamer and Receptor-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus 2 Variants Revealed by Steered Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2024Article
- Ester Bonds for Modulation of the Mechanical Properties of Protein Hydrogels.International journal of molecular sciences · 2023Article
- Engineering Functional Membrane-Membrane Interfaces by InterSpy.Small (Weinheim an der Bergstrasse, Germany) · 2023Article
- Dynamic Covalent Hydrogels: Strong yet Dynamic.Gels (Basel, Switzerland) · 2022Review
- Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin.International journal of molecular sciences · 2022Article
- Single-Molecule Force Spectroscopy Reveals Stability of mitoNEET and its [2Fe2Se] Cluster in Weakly Acidic and Basic Solutions.ChemistryOpen · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-positive bacteria can resist large mechanical perturbations during their invasion and colonization by secreting various surface proteins with intramolecular isopeptide or ester bonds. Compared to isopeptide bonds, ester bonds are prone to hydrolysis. It remains elusive whether ester bonds can completely block mechanical extension similarly to isopeptide bonds, or whether ester bonds dissipate mechanical energy by bond rupture. Here, we show that an ester-bond containing stalk domain of Cpe0147 is inextensible even at forces > 2 nN. The ester bond locks the structure to a partially unfolded conformation, in which the ester bond remains largely water inaccessible. This allows the ester bond to withstand considerable mechanical forces and in turn prevent complete protein unfolding. However, the protecting effect might be reduced at non-physiological basic pHs or low calcium concentrations due to destabilizing the protein structures. Inspired by this design principle, we engineer a disulfide mutant resistant to mechanical unfolding under reducing conditions.
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