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Biogenesis and adhesion of type 1 and P pili

Biochimica et Biophysica Acta (BBA) - General Subjects, 2014
Uropathogenic Escherichia coli (UPEC) cause urinary tract infections (UTIs) in approximately 50% of women. These bacteria use type 1 and P pili for host recognition and attachment. These pili are assembled by the chaperone-usher pathway of pilus biogenesis.The review examines the biogenesis and adhesion of the UPEC type 1 and P pili.
James, Lillington   +2 more
openaire   +2 more sources

Reprint of “Biogenesis and adhesion of type 1 and P pili”

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
Uropathogenic Escherichia coli (UPEC) cause urinary tract infections (UTIs) in approximately 50% of women. These bacteria use type 1 and P pili for host recognition and attachment. These pili are assembled by the chaperone-usher pathway of pilus biogenesis.The review examines the biogenesis and adhesion of the UPEC type 1 and P pili.
James, Lillington   +2 more
openaire   +2 more sources

Light-microscopic Visualization of F and Type 1 Pili

Microbiology, 1984
Methods for the direct visualization of F and type 1 pili of Escherichia coli in the light microscope are described. The method for visualizing F pili is based on the specific adsorption of fluorescent dye-labelled RNA phages to F pili. The best results were obtained with MS2 phages labelled with rhodamine B.
Biebricher, C., Düker, E.
openaire   +3 more sources

A key role for type 1 pili in enterobacterial communicability

Molecular Microbiology, 1992
SummaryUp to 80% of faecal Escherichia coil strains are able to produce type 1 pili. These filamentous bacterial surface organelles, which mediate mannose‐sensitive attachment to mammalian epithelial cells, are also conserved throughout the Enterobacteriaceae. As a potential explanation for their prevalence among intestinal isolates of enteric bacteria,
C A, Bloch, B A, Stocker, P E, Orndorff
openaire   +2 more sources

Exploring the 3D Molecular Architecture of Escherichia coli Type 1 Pili

Journal of Molecular Biology, 2002
An integrated approach combining information gained by Fourier transformation, linear Markham superposition (real space) and mass-per-length measurement by scanning transmission electron microscopy was used to analyze the helical structure of the rod-like type 1 pili expressed by uropathogenic Escherichia coli strain W3110.
Hahn E   +9 more
openaire   +3 more sources

Renal Scarring by Mannose-Sensitive Adhesin of EscherichiacoliType 1 Pili

Nephron, 1998
Most Escherichia coli isolates from patients with pyelonephritis possess both pap (mannose-resistant) pili and type 1 (mannose-sensitive) pili. In the experimental pyelonephritis model of rats, the mannose-sensitive-piliated strain caused severe renal scarring, whereas the mannose-resistant or nonpiliated strain did not.
Y, Mizunoe   +6 more
openaire   +2 more sources

Type 1 and P pili of uropathogenic Escherichia coli.

2014
AbstractIn uropathogenic Escherichia coli (UPEC), type 1 pili (T1P) and P pili enable the bacterium to bind to host epithelial cells within the urinary tract, which can lead to a urinary tract infection. This chapter reviews the genetics, structure and functions of UPEC T1P and P pili. It also describes the mechanisms by which T1P and P pili contribute
C. Russell, M. Mulvey
openaire   +1 more source

Structural and functional insights into the assembly of type 1 pili from Escherichia coli

Microbes and Infection, 2006
Type 1 pili are filamentous protein complexes that are anchored to the outer membrane of uropathogenic Escherichia coli and mediate bacterial adhesion to the surface of urinary epithelium cells. We review here the current status of structural and functional studies on the assembly of type 1 pili.
Capitani, Guido   +3 more
openaire   +4 more sources

Characterization of FimC, a Periplasmic Assembly Factor for Biogenesis of Type 1 Pili in Escherichia coli

Biochemistry, 2000
Assembly of type 1 pili from Escherichia coli is mediated by FimC, a periplasmic chaperone (assembly factor) consisting of two immunoglobulin-like domains. FimC is assumed to recognize the individual pilus subunits in the periplasm mainly via their conserved C-terminal segments and to deliver the subunits to an assembly platform in the outer membrane ...
U, Hermanns   +3 more
openaire   +2 more sources

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