This paper systematically characterize various polymer properties of Vibrio polysaccharide (VPS), the major exopolysaccharide in biofilms formed by Vibrio cholerae, the causative agent of pandemic cholera.
Abstract
Polysaccharides remain the least understood biomacromolecules, particularly in terms of the relationship between their chemical structure and physical properties. On the other hand, polysaccharides often serve as the main structural components in biofilms: surface-attached aggregates of bacterial cells encased within a mechanically resilient extracellular matrix. The large chemical space explored by bacteria within biofilms provides excellent opportunities to establish the structure-function relationship for polysaccharides. In this paper, we systematically characterize various polymer properties of Vibrio polysaccharide (VPS), the major exopolysaccharide in biofilms formed by Vibrio cholerae, the causative agent of pandemic cholera. Using a combination of shear rheology, dynamic and static light scattering, and small-angle X-ray scattering, we measure the viscosity, molecular weight, persistence length, radius of gyration, and hydrodynamic radius of this chemically unique biopolymer. Combining all-atom and coarse-grained simulations, we show how the conformational flexibility of a single glycosidic linkage within each VPS monomer can lead to dramatic compaction of the entire polymer chain and nonclassical entanglement behavior. Our comprehensive quantification represents a rare endeavor for bacterial biofilms, whose matrix composition and physical properties remain largely nebulous; it also represents a significant step towards a detailed understanding of the molecular origins of biofilm mechanics.
The structure reveals for the first time the interaction between a biofilm exopolysaccharide and matrix protein, as well as insights into conformational changes of exopolysaccharide induced by this binding, and provides a generalizable approach for studying the biophysical and biochemical properties of carbohydrate-dep...
Alex Hinbest, Hyerim Bianca Nam, E. Liszczyk et al.· bioRxiv· 0 citations
The findings show that bacterial virulence can be regulated through environmentally controlled transitions between protein assemblies, identifying membrane accumulation as a promising anti-virulence target.
Sambhasan Banerjee, V. Skoryk, Bader Rayan et al.· bioRxiv· 0 citations
It is argued that antifouling arises from a sophisticated synergy of lattice dynamics, crystalline nanotopography, electrostatic mosaicity, fragmented hydrophobicity, structured hydration shells and frequently glycan-mediated steric repulsion, which provides a powerful blueprint for biomimetic surface engineering in (n...
U. Sleytr, B. Schuster· Quarterly Reviews of Biophys...· 0 citations
Results indicate that CAase effectively disrupts multiple components of C. jejuni biofilm architecture despite lacking direct antimicrobial activity, suggesting potential utility in poultry-processing or surface-sanitation applications where targeted enzymatic disruption could enhance cleaning efficacy.
This review presents a comprehensive multiscale framework integrating experimental techniques and computational modeling to elucidate how mechanics drive biofilm architecture and evolution, and establishes a foundation for systematic analysis of biofilm mechanics.
Atomic force microscopy nanoindentation simulations of CypA-decorated capsids reveal that CypA acts as a stoichiometric regulator of capsid mechanical response, highlighting how surface ligand binding programs the mechanical response of protein nanocapsules, offering principles for stimuli-responsive biomolecular mater...
J. Rey, Alexander J. Bryer, J. Perilla· Small· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.