title: Two repetitive, biofilm-forming proteins from Staphylococci: from disorder to extension.
abstract: Staphylococcus aureus and Staphylococcus epidermidis are an important cause of medical device-related infections that are difficult to treat with antibiotics. Biofilms, in which bacteria are embedded in a bacterially-produced exopolymeric matrix, form on the surface of the implanted medical device. Our understanding of the molecular mechanisms underlying the initial surface attachment and subsequent intercellular interactions as the biofilm matures is improving. Biofilm accumulation can be mediated by a partially deacetylated form of poly-N-acetylglucosamine (PNAG) but, more recently, the role of bacterial surface proteins is being recognized. Here we describe the structure and function of two S. aureus cell surface proteins, FnBPA and SasG, implicated in host interactions and biofilm accumulation. These multifunctional proteins employ intrinsic disorder for distinct molecular outcomes. In the case of FnBPA, disorder generates adhesive arrays that bind fibronectin (Fn); in the case of SasG, disorder is, counterintuitively, used to maintain a strong extended fold.
authors.affiliation: Department of Biology, University of York, Wentworth Way, York YO10 5DD, U.K.
authors.forename: Fiona
authors.initials: F
authors.lastname: Whelan
authors.affiliation: Department of Biology, University of York, Wentworth Way, York YO10 5DD, U.K. jennifer.potts@york.ac.uk.
authors.forename: Jennifer R
authors.initials: JR
authors.lastname: Potts
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018441:Biofilms; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D020449:Repetitive Sequences, Amino Acid; D013211:Staphylococcus aureus / Q000502:physiology*; D013212:Staphylococcus epidermidis / Q000502:physiology*; D040681:Structural Homology, Protein
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D008565:Membrane Proteins; C524374:SasG protein, Staphylococcus aureus; C078635:fibronectin-binding proteins, bacterial
keywords: FnBPA; SasG; Staphylococcus aureus; biofilm