title: Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation.
abstract: Campylobacter jejuni remains the leading cause of bacterial gastroenteritis in developed countries, and yet little is known concerning the mechanisms by which this fastidious organism survives within its environment. We have demonstrated that C. jejuni 11168 can form biofilms on a variety of surfaces. Proteomic analyses of planktonic and biofilm-grown cells demonstrated differences in protein expression profiles between the two growth modes. Proteins involved in the motility complex, including the flagellins (FlaA, FlaB), the filament cap (FliD), the basal body (FlgG, FlgG2), and the chemotactic protein (CheA), all exhibited higher levels of expression in biofilms than found in stationary-phase planktonic cells. Additional proteins with enhanced expression included those involved in the general (GroEL, GroES) and oxidative (Tpx, Ahp) stress responses, two known adhesins (Peb1, FlaC), and proteins involved in biosynthesis, energy generation, and catabolic functions. An aflagellate flhA mutant not only lost the ability to attach to a solid matrix and form a biofilm but could no longer form a pellicle at the air-liquid interface of a liquid culture. Insertional inactivation of genes that affect the flagellar filament (fliA, flaA, flaB, flaG) or the expression of the cell adhesin (flaC) also resulted in a delay in pellicle formation. These findings demonstrate that the flagellar motility complex plays a crucial role in the initial attachment of C. jejuni 11168 to solid surfaces during biofilm formation as well as in the cell-to-cell interactions required for pellicle formation. Continued expression of the motility complex in mature biofilms is unusual and suggests a role for the flagellar apparatus in the biofilm phenotype.
authors.affiliation: Health Canada Bureau of Microbial Hazards, Ottawa, Ontario K1A 0L2.
authors.forename: Martin
authors.initials: M
authors.lastname: Kalmokoff
authors.forename: Patricia
authors.initials: P
authors.lastname: Lanthier
authors.forename: Tammy-Lynn
authors.initials: TL
authors.lastname: Tremblay
authors.forename: Mary
authors.initials: M
authors.lastname: Foss
authors.forename: Peter C
authors.initials: PC
authors.lastname: Lau
authors.forename: Greg
authors.initials: G
authors.lastname: Sanders
authors.forename: John
authors.initials: J
authors.lastname: Austin
authors.forename: John
authors.initials: J
authors.lastname: Kelly
authors.forename: Christine M
authors.initials: CM
authors.lastname: Szymanski
mesh_terms: D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism / Q000502:physiology; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism / Q000502:physiology*; D018441:Biofilms / Q000254:growth & development*; D016123:Campylobacter jejuni / Q000378:metabolism / Q000502:physiology*; D015180:Electrophoresis, Gel, Two-Dimensional; D005407:Flagella / Q000378:metabolism / Q000502:physiology*; D005408:Flagellin / Q000378:metabolism; D009068:Movement; D020543:Proteome / Q000378:metabolism / Q000502:physiology*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D020543:Proteome; C117211:flgFG protein, bacteria; D005408:Flagellin; C076733:FlaD protein, Bacteria