ArticleNature communications2023
Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Targeting phenol-soluble modulin α3-driven M1 macrophage polarization and necroptosis mitigates MRSA infection in mice.Nature communications · 2026Article
- Ampicillin promotes the biofilm formation ofMicrobiology spectrum · 2026Article
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Novel antibacterial peptide HfAMP against methicillin-resistant Staphylococcus aureus.BMC microbiology · 2025Article
- Natural Design of a Stabilized Cross-β Fold: Structure of the FuA FapC from Pseudomonas Sp. UK4 Reveals a Critical Role for Stacking of Imperfect Repeats.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Allosteric amyloid catalysis by coiled coil fibrils.Nature communications · 2025Article
- Capturing the micro-communities: Insights into biogenesis and architecture of bacterial biofilms.BBA advances · 2025Article
- Amyloid transformations of phenol soluble modulin α1 in Staphylococcus aureus and their modulation deploying a prenylated chalcone.Scientific reports · 2024Article
- β-lactam antibiotics induce metabolic perturbations linked to ROS generation leads to bacterial impairment.Frontiers in microbiology · 2024Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibiotic resistance of bacteria is considered one of the most alarming developments in modern medicine. While varied pathways for bacteria acquiring antibiotic resistance have been identified, there still are open questions concerning the mechanisms underlying resistance. Here, we show that alpha phenol-soluble modulins (PSMαs), functional bacterial amyloids secreted by Staphylococcus aureus, catalyze hydrolysis of β-lactams, a prominent class of antibiotic compounds. Specifically, we show that PSMα2 and, particularly, PSMα3 catalyze hydrolysis of the amide-like bond of the four membered β-lactam ring of nitrocefin, an antibiotic β-lactam surrogate. Examination of the catalytic activities of several PSMα3 variants allowed mapping of the active sites on the amyloid fibrils' surface, specifically underscoring the key roles of the cross-α fibril organization, and the combined electrostatic and nucleophilic functions of the lysine arrays. Molecular dynamics simulations further illuminate the structural features of β-lactam association upon the fibril surface. Complementary experimental data underscore the generality of the functional amyloid-mediated catalytic phenomenon, demonstrating hydrolysis of clinically employed β-lactams by PSMα3 fibrils, and illustrating antibiotic degradation in actual S. aureus biofilms and live bacteria environments. Overall, this study unveils functional amyloids as catalytic agents inducing degradation of β-lactam antibiotics, underlying possible antibiotic resistance mechanisms associated with bacterial biofilms.
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