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Biochemical characteristic of biofilm of uropathogenic Escherichia coli Dr(+) strains.
Microbiol Res
July 2013
Department of Microbiology, Gdańsk University of Technology, ul. G. Narutowicza 11/12, 80-233 Gdańsk, Poland.
Urinary tract infections caused by Escherichia coli are very common health problem in the developed countries. The virulence of the uropathogenic E. coli Dr(+) IH11128 is determined by Dr fimbriae, which are homopolymeric structures composed of DraE subunits with the DraD protein capping the fiber.
View Article and Find Full Text PDFFimbrial polyadhesins: anti-immune armament of Yersinia.
Adv Exp Med Biol
September 2012
Joint Biotechnology Laboratory, Department of Chemistry, University of Turku, BioCity 6A, Tykistökatu 6, 20520, Turku, Finland.
Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.
FEMS Microbiol Rev
May 2010
Joint Biotechnology Laboratory, University of Turku, Turku, Finland.
This review summarizes current knowledge on the structure, function, assembly and biomedical applications of the superfamily of adhesive fimbrial organelles exposed on the surface of Gram-negative pathogens with the classical chaperone/usher machinery. High-resolution three-dimensional (3D) structure studies of the minifibers assembling with the FGL (having a long F1-G1 loop) and FGS (having a short F1-G1 loop) chaperones show that they exploit the same principle of donor-strand complementation for polymerization of subunits. The 3D structure of adhesive subunits bound to host-cell receptors and the final architecture of adhesive fimbrial organelles reveal two functional families of the organelles, respectively, possessing polyadhesive and monoadhesive binding.
View Article and Find Full Text PDFFGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens.
FEMS Microbiol Rev
July 2007
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
This review summarizes the current knowledge on the structure, function, assembly, and biomedical applications of the family of adhesive fimbrial organelles assembled on the surface of Gram-negative pathogens via the FGL chaperone/usher pathway. Recent studies revealed the unique structural and functional properties of these organelles, distinguishing them from a related family, FGS chaperone-assembled adhesive pili. The FGL chaperone-assembled organelles consist of linear polymers of one or two types of protein subunits, each possessing one or two independent adhesive sites specific to different host cell receptors.
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