title: Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components.
abstract: Typical enteropathogenic Escherichia coli strains express an established virulence factor belonging to the type IV pili family, called the bundle-forming pilus (BFP). BFP are present on the cell surface as bundled filamentous appendages, and are assembled and retracted by proteins encoded by the bfp operon. These proteins assemble to form a molecular machine. The BFP machine may be conceptually divided into three components: the cytoplasmic membrane (CM) subassembly, which is composed of CM proteins and cytoplasmic nucleotide-binding proteins; the outer membrane (OM) subassembly and the pilus itself. The authors have previously characterized the CM subassembly and the pilus. In this study, a more complete characterization of the OM subassembly was carried out using a combination of biochemical, biophysical and genetic approaches. It is reported that targeting of BfpG to the OM was influenced by the secretin BfpB. BfpG and BfpU interacted with the amino terminus of BfpB. BfpU had a complex cellular distribution pattern and, along with BfpB and BfpG, was part of the OM subassembly.
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Anu
authors.initials: A
authors.lastname: Daniel
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Aparna
authors.initials: A
authors.lastname: Singh
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Lynette J
authors.initials: LJ
authors.lastname: Crowther
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Paula J
authors.initials: PJ
authors.lastname: Fernandes
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Wiebke
authors.initials: W
authors.lastname: Schreiber
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Maryland School of Medicine, 20 Penn Street, Baltimore, MD 21201, USA.
authors.forename: Michael S
authors.initials: MS
authors.lastname: Donnenberg
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000502:physiology; D001483:Base Sequence; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000502:physiology; D010861:Fimbriae, Bacterial / Q000502:physiology*; D008074:Lipoproteins / Q000737:chemistry / Q000302:isolation & purification / Q000502:physiology; D008969:Molecular Sequence Data; D020798:Two-Hybrid System Techniques; D037521:Virulence Factors / Q000737:chemistry* / Q000502:physiology
chemical_list: D001425:Bacterial Outer Membrane Proteins; C433794:BfpB protein, E coli; C469813:BfpU protein, E coli; D029968:Escherichia coli Proteins; D008074:Lipoproteins; D037521:Virulence Factors