Resilience and Charge-Dependent Fibrillation of functional amyloid: Interactions of Pseudomonas Biofilm-Associated FapB and FapC Amyloids.

Autor:	Golan N; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel., Parizat A; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel., Tabachnikov O; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel; Current address: Department of Nephrology, Rambam Health Care Campus, Haifa, Israel., Barnea E; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel., Olsen WP; Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark., Otzen DE; Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark., Landau M; Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel; CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY, 22607 Hamburg, Germany; The Center for Experimental Medicine, Universitätsklinikum Hamburg-Eppendorf (UKE), Hamburg, Germany; European Molecular Biology Laboratory (EMBL), Hamburg, Germany. Electronic address: meytal.landau@desy.de.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2024 Dec 18, pp. 108096. Date of Electronic Publication: 2024 Dec 18.
DOI:	10.1016/j.jbc.2024.108096
Abstrakt:	FapC and FapB are biofilm-associated amyloids involved in the virulence of Pseudomonas and other bacteria. We herein demonstrate their exceptional thermal and chemical resilience, suggesting that their biofilm structures might withstand standard sterilization, thereby contributing to the persistence of P. aeruginosa infections. Our findings also underscore the impact of environmental factors on Fap proteins, suggesting that orthologs in different Pseudomonas strains adapt to specific environments and roles. Challenging previous assumptions about a simple nucleation role for FapB in promoting FapC aggregation, the study shows a significant influence of FapC on FapB aggregation. The interaction between these FapB and FapC is intricate: FapB stabilizes FapC fibrils, while FapC slows down FapB fibrillation but can still serve as a cross-seeding template. This complex interplay is key to understanding their roles in bacterial biofilms. Furthermore, the study highlights distinct differences between Fap and E. coli's CsgA (curli) amyloid, where CsgB assumes a simple unidirectional role in nucleating CsgA fibrillation, emphasizing the importance of a comprehensive understanding of various amyloid systems. This knowledge is vital for developing effective intervention strategies against bacterial infections and leveraging the unique properties of these amyloids in technological applications such as novel bio-nanomaterials or protective coatings. (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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