title: Molecular determinants of mechanical properties of V. cholerae biofilms at the air-liquid interface.
abstract: Biofilm formation increases both the survival and infectivity of Vibrio cholerae, the causative agent of cholera. V. cholerae is capable of forming biofilms on solid surfaces and at the air-liquid interface, termed pellicles. Known components of the extracellular matrix include the matrix proteins Bap1, RbmA, and RbmC, an exopolysaccharide termed Vibrio polysaccharide, and DNA. In this work, we examined a rugose strain of V. cholerae and its mutants unable to produce matrix proteins by interfacial rheology to compare the evolution of pellicle elasticity in real time to understand the molecular basis of matrix protein contributions to pellicle integrity and elasticity. Together with electron micrographs, visual inspection, and contact angle measurements of the pellicles, we defined distinct contributions of the matrix proteins to pellicle morphology, microscale architecture, and mechanical properties. Furthermore, we discovered that Bap1 is uniquely required for the maintenance of the mechanical strength of the pellicle over time and contributes to the hydrophobicity of the pellicle. Thus, Bap1 presents an important matrix component to target in the prevention and dispersal of V. cholerae biofilms.
authors.affiliation: Department of Chemical Engineering, Stanford University, Stanford, California.
authors.forename: Emily C
authors.initials: EC
authors.lastname: Hollenbeck
authors.affiliation: Department of Microbiology and Environmental Toxicology, UC Santa Cruz, Santa Cruz, California.
authors.forename: Jiunn C N
authors.initials: JC
authors.lastname: Fong
authors.affiliation: Department of Chemistry, Stanford University, Stanford, California.
authors.forename: Ji Youn
authors.initials: JY
authors.lastname: Lim
authors.affiliation: Department of Microbiology and Environmental Toxicology, UC Santa Cruz, Santa Cruz, California.
authors.forename: Fitnat H
authors.initials: FH
authors.lastname: Yildiz
authors.affiliation: Department of Chemical Engineering, Stanford University, Stanford, California.
authors.forename: Gerald G
authors.initials: GG
authors.lastname: Fuller
authors.affiliation: Department of Chemistry, Stanford University, Stanford, California. Electronic address: cegelski@stanford.edu.
authors.forename: Lynette
authors.initials: L
authors.lastname: Cegelski
mesh_terms: D000388:Air; D001426:Bacterial Proteins / Q000378:metabolism; D018441:Biofilms; D001696:Biomechanical Phenomena; D004548:Elasticity; D057927:Hydrophobic and Hydrophilic Interactions; D055595:Mechanical Phenomena; D008854:Microscopy, Electron; D012212:Rheology; D014734:Vibrio cholerae / Q000166:cytology / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins