ArticleProceedings of the National Academy of Sciences of the United States of America2022
Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Article
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Structural and Functional Versatility of the Amyloidogenic Non-Amidated Variant of the Antimicrobial Peptide Citropin 1.3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Purification tags markedly affect self-aggregation of CPEB3.FEBS letters · 2025Article
- Cryo-EM for atomic characterization of supramolecular gels.Faraday discussions · 2025Article
- Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.Angewandte Chemie (International ed. in English) · 2025Article
- Fragment-Based Approach for Hierarchical Nanotube Assembly of Small Molecules in Aqueous Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Interaction of Arginine-Rich Surfactant-like Peptide Nanotubes with Liposomes.Biomacromolecules · 2024Article
- Cell-Free Nonequilibrium Assembly for Hierarchical Protein/Peptide Nanopillars.Journal of the American Chemical Society · 2024Article
- The role of Staphylococcus aureus quorum sensing in cutaneous and systemic infections.Inflammation and regeneration · 2024Review
- The role of filamentous matrix molecules in shaping the architecture and emergent properties of bacterial biofilms.The Biochemical journal · 2024Review
- SarZ inhibits the hemolytic activity through regulation of phenol soluble modulins inFrontiers in cellular and infection microbiology · 2024Article
- Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics.Nature communications · 2023Article
- Article
- Differential fibril morphologies and thermostability determine functional roles ofFrontiers in molecular biosciences · 2023Article
- The great divide: rhamnolipids mediate separation betweenFrontiers in cellular and infection microbiology · 2023Article
- The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils.Nature communications · 2022Article
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Authors and funding
7 authors.
Funding
Abstract
Phenol-soluble modulins (PSMs) are peptide-based virulence factors that play significant roles in the pathogenesis of staphylococcal strains in community-associated and hospital-associated infections. In addition to cytotoxicity, PSMs display the propensity to self-assemble into fibrillar species, which may be mediated through the formation of amphipathic conformations. Here, we analyze the self-assembly behavior of two PSMs, PSMα3 and PSMβ2, which are derived from peptides expressed by methicillin-resistant Staphylococcus aureus (MRSA), a significant human pathogen. In both cases, we observed the formation of a mixture of self-assembled species including twisted filaments, helical ribbons, and nanotubes, which can reversibly interconvert in vitro. Cryo–electron microscopy structural analysis of three PSM nanotubes, two derived from PSMα3 and one from PSMβ2, revealed that the assemblies displayed remarkably similar structures based on lateral association of cross-α amyloid protofilaments. The amphipathic helical conformations of PSMα3 and PSMβ2 enforced a bilayer arrangement within the protofilaments that defined the structures of the respective PSMα3 and PSMβ2 nanotubes. We demonstrate that, similar to amyloids based on cross-β protofilaments, cross-α amyloids derived from these PSMs display polymorphism, not only in terms of the global morphology (e.g., twisted filament, helical ribbon, and nanotube) but also with respect to the number of protofilaments within a given peptide assembly. These results suggest that the folding landscape of PSM derivatives may be more complex than originally anticipated and that the assemblies are able to sample a wide range of supramolecular structural space.
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