A natural glycolipid exposes the outer membrane interface as a tunable regulator of bacterial surface attachment

Structural basis of biofilm formation mediated by the Pseudomonas aeruginosa fibrillar adhesin CdrA

An electron cryomicroscopy structure of the 60 kDa CdrA adhesive N-terminus is reported, which combined with electron cryotomography of focused-ion beam milled specimens, allows for a complete in situ model of the native adhesin and reveals a small adhesive domain (called ADEPT) at the distal tip of CdrA that is nearly perfectly conserved across the P. aeruginosa pangenome.

Antibiofilm activity of a recombinant mussel-derived antimicrobial protein through surface charge-mediated hydration layer formation.

Biofilm formation on biomedical devices remains a major cause of persistent infections and antibiotic resistance. In this study, we developed a charge-mediated, anti-adhesive platform by immobilizing recombinant mussel adhesive protein-antimicrobial peptide fusions (MAP-AMPs) on solid substrates via a simple EDC/NHS covalent coupling reaction. Using recombinant MAP-foot protein-151 (MAP-fp-151) as a versatile scaffold, immobilized MAP-AMPs were characterized by attenuated total reflectance Fourier-transform infrared (ATR-FTIR) spectroscopy, scanning electron microscopy (SEM), atomic force microscopy (AFM), and Coomassie brilliant blue staining. While soluble MAP-AMPs exhibited potent bactericidal activity against both reference and antibiotic-resistance clinical E. coli strains, their immobilized forms primarily inhibited biofilm formation rather than exhibiting direct bactericidal activity. Computational simulations and experimental surface analyses revealed that the cationic MAP-AMPs formed island-like clusters that elevated surface positive potential and organized a dense, long-range hydration layer extending beyond the clusters into the bare surface regions. This mechanism was experimentally validated using Kelvin probe force microscopy (KPFM) and contact angle analysis, which showed elevated surface potential, increased water retention, and reduced water contact angles. Bacterial adhesion on the MAP-AMP2-immobilized surface was significantly suppressed, with adhesion rates reduced to 27.62-45.16% across all tested strains. These results indicate that MAP-AMP-immobilized surfaces provide a versatile, biocompatible, and resistance-independent strategy for preventing biofilm formation through charge-mediated hydration, offering broad potential for biomedical device coatings and antifouling applications.

Three hydrophobic surface binding a proteins link surface hydrophobicity to sporulation, biofilm formation, and host interaction in Mucor lusitanicus

Results show that HsbA proteins in Mucor lusitanicus function as regulators that couple fungal surface remodeling with developmental transitions, thereby coordinating environmental adaptation and host–pathogen interactions.

Tracking Surface Protein Assembly and Peptidoglycan Biosynthesis in Fusobacterium nucleatum.

Structure of a key adhesin-exopolysaccharide interaction provides insights into matrix assembly in Vibrio cholerae biofilms

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-dependent biofilm assembly.

Outer membrane stiffness gates multidrug tolerance