ArticleNPJ biofilms and microbiomes2022
Bacterial biofilm functionalization through Bap amyloid engineering.
Article in NPJ biofilms and microbiomes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Biofilm-mediated antibiotic tolerance in bacterial pathogens: Integrated molecular networks and novel therapeutic avenues.Virulence · 2026Review
- The Gut-Brain Axis in Neurodegeneration: Mechanistic Links Between Dysbiosis and Neuropathology.Iranian journal of pathology · 2026Review
- Protein Nanofibrils as Emerging Biomaterials for Sustainable Food Packaging: Advances, Challenges, and Future Opportunities.Comprehensive reviews in food science and food safety · 2026Review
- Biofilm-Associated Amyloid Proteins Linked with the Progression of Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- Light-activated nanoclusters with tunable ROS for wound infection treatment.Bioactive materials · 2024Article
- Gut microbiota produces biofilm-associated amyloids with potential for neurodegeneration.Nature communications · 2024Article
- Strategies and materials for the prevention and treatment of biofilms.Materials today. Bio · 2023Review
- Amyloid Fibrils Produced byInternational journal of molecular sciences · 2023Article
- Hierarchical organization and assembly of the archaeal cell sheath from an amyloid-like protein.Nature communications · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biofilm engineering has emerged as a controllable way to fabricate living structures with programmable functionalities. The amyloidogenic proteins comprising the biofilms can be engineered to create self-assembling extracellular functionalized surfaces. In this regard, facultative amyloids, which play a dual role in biofilm formation by acting as adhesins in their native conformation and as matrix scaffolds when they polymerize into amyloid-like fibrillar structures, are interesting candidates. Here, we report the use of the facultative amyloid-like Bap protein of Staphylococcus aureus as a tool to decorate the extracellular biofilm matrix or the bacterial cell surface with a battery of functional domains or proteins. We demonstrate that the localization of the functional tags can be change by simply modulating the pH of the medium. Using Bap features, we build a tool for trapping and covalent immobilizing molecules at bacterial cell surface or at the biofilm matrix based on the SpyTag/SpyCatcher system. Finally, we show that the cell wall of several Gram-positive bacteria could be functionalized through the external addition of the recombinant engineered Bap-amyloid domain. Overall, this work shows a simple and modulable system for biofilm functionalization based on the facultative protein Bap.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.