Adhesion mechanisms of curli subunit CsgA to abiotic surfaces

DeBenedictis, Elizabeth P.; Liu, Jenny; Keten, Sinan

doi:10.1126/sciadv.1600998

Cited by 74 publications

(54 citation statements)

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“…3). As curli is important for binding to abiotic surfaces 27,55,56 , it is possible that 3H3 interferes with the domains of curli required for surface binding. Antibiotics that belong to the beta-lactam, fluoroquinolone, and aminoglycoside drug classes all demonstrated increased cell killing when the biofilm extracellular matrix was altered by 3H3.…”

Section: Discussionmentioning

confidence: 99%

Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli

et al. 2020

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Bacterial biofilms, especially those associated with implanted medical devices, are difficult to eradicate. Curli amyloid fibers are important components of the biofilms formed by the Enterobacteriaceae family. Here, we show that a human monoclonal antibody with panamyloid-binding activity (mAb 3H3) can disrupt biofilms formed by Salmonella enterica serovar Typhimurium in vitro and in vivo. The antibody disrupts the biofilm structure, enhancing biofilm eradication by antibiotics and immune cells. In mice, 3H3 injections allow antibioticmediated clearance of catheter-associated S. Typhimurium biofilms. Thus, monoclonal antibodies that bind a pan-amyloid epitope have potential to prevent or eradicate bacterial biofilms.

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Section: Discussionmentioning

confidence: 99%

Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli

et al. 2020

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“…To progress beyond AFM-based mechanical testing and determine binding behavior at an atomistic resolution, in silico free energy calculations are necessary. Recently, we have presented atomistic models for individual CsgA and CsgB subunits, 30 which can be used as a foundation for investigations of fibrils using both all-atom 31 and coarse-grained molecular dynamics (MD) simulations. 32 From this work by DeBenedictis et al, the RobB-5 CsgB structure and the CsgA-map model based upon it will be utilized in this paper.…”

Section: Althoughmentioning

confidence: 99%

Dimerization energetics of curli fiber subunits CsgA and CsgB

2019

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Curli fibers are functional amyloids that exhibit strong adhesion and robust self-assembly as biofilm structural components; however, the binding energetics and mechanical properties of wild-type curli are not well understood. To address this, we present dimer structures made up of the major and minor curli subunits (CsgA and CsgB), perform free energy calculations to obtain absolute binding energies, and estimate the Young's modulus and persistence length of curli fibers. Equilibrium molecular dynamics simulations are used to evaluate nonbonded interactions. Binding energies are most favorable for CsgB-CsgA, while CsgA-CsgA dimers have a higher binding energy than CsgB-CsgB despite possessing less favorable nonbonded interaction energies. Decomposing each potential of mean force of separation indicated that solvent effects positively impact CsgA-CsgA binding but not CsgB-CsgB and CsgB-CsgA. Charged residues and conserved polar residues were also notable contributors to attractive nonbonded interactions, underlining their importance in dimer assembly. Our findings elucidate sequence effects on binding energy contributions and establish theoretical limits for the elasticity, persistence length, and strength of curli fibers.npj Computational Materials (2019) 5:27 ; https://doi.

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“…In another study, HA coating has been prepared by a biofilm inspired approach using the CsgA component of E. coli biofilm and a short peptide bioinspired from dental biofilm 23 . Keten group has examined CsgA adsorption onto graphene and silica surfaces through atomistic simulation 24 . Since there is an increasing number of efforts to use biofilm proteins as intelligent materials 18,[25][26][27] , there is a need for an extensive characterization of their interactions with solid surfaces.…”

Section: Introductionmentioning

confidence: 99%

Binding Behavior of Microbial Functional Amyloids on Solid Surfaces

Yuca

Kehribar

Şeker

2020

Preprint

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KEYWORDS (Word Style "BG_Keywords"). If you are submitting your paper to a journal that requires keywords, provide significant keywords to aid the reader in literature retrieval. ABSTRACTSelf-assembling protein subunits hold great potential as biomaterials with improved functions.Among the self-assembled protein structures functional amyloids are promising unique properties such as resistance to harsh physical and chemical conditions their mechanical strength, and ease of functionalization. Curli proteins, which are functional amyloids of bacterial biofilms can be programmed as intelligent biomaterials. In order to obtain controllable curli based biomaterials for biomedical applications, and to understand role of each of the curli forming monomeric proteins (namely CsgA and CsgB from Escherichia coli) we characterized their binding kinetics to gold, hydroxyapatite, and silica surfaces. We demonstrated that CsgA, CsgB, and their equimolar mixture have different binding strengths for different surfaces. On hydroxyapatite and silica surfaces, CsgB is the crucial element that determines the final adhesiveness of the CsgA-CsgB mixture. On the gold surface, on the other hand, CsgA controls the behavior of the mixture. Those findings uncover the binding behavior of curli proteins CsgA and CsgB on different biomedically valuable surfaces to obtain a more precise control on their adhesion to a targeted surface.

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Adhesion mechanisms of curli subunit CsgA to abiotic surfaces

Abstract: The curli fiber subunit, CsgA, adheres strongly to abiotic surfaces through side-chain interactions and also exhibits correlated motion.

Cited by 74 publications

References 80 publications

Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli

Salmonella Typhimurium biofilm disruption by a human antibody that binds a pan-amyloid epitope on curli

Dimerization energetics of curli fiber subunits CsgA and CsgB

Binding Behavior of Microbial Functional Amyloids on Solid Surfaces

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