Conformational dynamics of exopolysaccharides underlie biofilm matrix mechanics in Vibrio cholerae
Nam, K.-M.; Fowler, N.; Kandel, R.; Zhu, Y.; Liu, Y.; Lai, Y.-J.; Hassan, M. F.; Gerace, E.; Asp, M.; Olson, R.; Li, Y.; Nieh, M.-P.; Zhong, M.; Woods, R. J.; Moreau, A.; Yan, J.
Show 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.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Sticky Interactions Govern Sequence-Dependent Dynamics in Biomolecular Condensates 97%
- Identifying Sequence Perturbations to an Intrinsically Disordered Protein that Determine Its Phase Separation Behavior 96%
- Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes 96%
Similar papers in this journal
- Expanding the molecular language of protein liquid-liquid phase separation 97%
- Asymmetric oligomerization state and sequence patterning can tune multiphase condensate miscibility 97%
- Deciphering how naturally occurring sequence features impact the phase behaviors of disordered prion-like domains 97%
Similar papers in this journal
- Resolving the nanoscale structure of β-sheet assemblies using single-molecule orientation-localization microscopy 96%
- Rapid exchange of stably bound protein and DNA cargo on a DNA origami receptor 95%
- Comparing multifunctional viral and eukaryotic proteins for generating scission necks in membranes 95%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.