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Structural basis of Pseudomonas biofilm-forming functional amyloid FapC formation
Open accessPublished version of a preprint
Abstract
Biofilm-protected Pseudomonas aeruginosa causes chronic infections that are difficult to treat. FapC, the major biofilm-forming functional amyloid in Pseudomonas , is essential for biofilm integrity, yet its structural details remain unresolved. Using an integrative structural biology approach, we combine a solution nuclear magnetic resonance–based structural ensemble of unfolded monomeric FapC, a ~3.3-angstrom-resolution cryo–electron microscopy (cryo-EM) density map of FapC fibril, and all-atom molecular dynamics (MD) simulations to capture the transition from the unfolded to folded monomer to the fibrillar fold, providing a complete structural view of FapC biogenesis. Cryo-EM reveals a unique irregular triple-layer β solenoid cross-β fibril composed of a single protofilament. MD simulations initiated from monomeric and fibrillar FapC mapped structural transitions, offering mechanistic insights into amyloid assembly and disassembly. Understanding FapC reveals how Pseudomonas exploits functional amyloids for biofilm formation, and establishes a structural and mechanistic foundation for developing therapeutics targeting biofilm-related infection and antimicrobial resistance.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861
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Metadata
- Authors
- Hansen, K. H., Golcuk, M., Byeon, C. H., Tunc, A., Plechinger, E. B., Dueholm, M. K. D., Conway, J. F., Andreasen, M., Gur, M., & Akbey, Ü.
- Affiliations
- University of Pittsburgh (US)
- Computational Systems Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA.
- Aarhus University (DK)
- Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.
- Corresponding author
- Akbey, Ümit
- ORCID
- Venue
- Science Advances
- Published
- 2025-09-26
- Volume
- 11
- Issue
- 39
- Pages
- eadx7829-eadx7829
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC12459412
- OpenAlex
- W4414533212
- Cited by
- 18
- References
- 2
- Citations by year
- 2026: 15 · 2025: 3
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc)
- VBN Forskningsportal (Aalborg Universitet) (submittedVersion, cc-by-nc)
- Funders
- Aarhus Universitet
- University of Pittsburgh
- Aarhus Universitets Forskningsfond
- National Institutes of Health (1s10od019995-01, 1s10od025009-01)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- functional amyloids, Pseudomonas aeruginosa, biofilm formation, amyloid fibril structure, chronic infection, antimicrobial resistance
- MeSH terms
- Amyloid, Bacterial Proteins, Protein Conformation, Pseudomonas, Pseudomonas aeruginosa, Biofilms, Cryoelectron Microscopy, Molecular Dynamics Simulation
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