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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Fimbriae, Bacterial

 
 
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Disease relevance of Fimbriae, Bacterial

  • In this study, we demonstrate that Porphyromonas gingivalis fimbrillin, a major component of bacterial fimbriae, is one of the fibronectin-binding proteins and that fibronectin is a potent inhibitor of the adherence of the bacteria to host cells and of the pathogenesis of the bacterium that acts by binding to the fimbriae [1].
 

High impact information on Fimbriae, Bacterial

  • Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus [2].
  • Common pili were purified from these bacteria by shearing them from the bacteria followed by selective precipitation in acid and ammonium sulfate [3].
  • Absorption of immune sera by a heterologous pilus reduced the inhibition of attachment antibodies to pre-immune level, suggesting that the immune response was directed at a common pilus determinant [4].
  • Integrin activation by bacterial fimbriae through a pathway involving CD14, Toll-like receptor 2, and phosphatidylinositol-3-kinase [5].
  • Target cell activation was independent of bacterial fimbriae expression since the fimA knockout strain A7436 DeltafimA induced the same level of ICAM-1 as the corresponding wild type (A7436-WT) [6].
 

Biological context of Fimbriae, Bacterial

 

Associations of Fimbriae, Bacterial with chemical compounds

  • This adherence was mediated by a mannose-sensitive lectin in the bacterial pili, and not on the intestinal cells [8].
  • Synthesis of bacterial fimbriae (group 1, subtype 1) was shown to be dependent on cyclic AMP and was subject to catabolite repression by many carbohydrates [9].
  • After metabolization, erdosteine (a mucoactive drug) produces an active metabolite (Met I) with an SH group that is capable of opening disulphide bonds, including those of pilin, a protein of bacterial fimbriae [10].
 

Gene context of Fimbriae, Bacterial

  • Common fimbriae and flagellar antigen were avoided by careful control of growth conditions and the use of a nonmotile (H-) mutant of the prototype strain H-10407 (O78:H11) [11].
  • These subunits are connected by interactions along the fimbrial backbone which, unlike other classes of bacterial fimbriae, has no axial channel [12].
  • Further, we describe the identification and isolation of a small peptide structural element found in P. aeruginosa strain K (PAK) bacterial pili, which has been proven to function as a host epithelial cell-surface receptor binding domain [13].

References

  1. Porphyromonas gingivalis fimbrillin is one of the fibronectin-binding proteins. Murakami, Y., Iwahashi, H., Yasuda, H., Umemoto, T., Namikawa, I., Kitano, S., Hanazawa, S. Infect. Immun. (1996) [Pubmed]
  2. Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus. Lindberg, F., Lund, B., Johansson, L., Normark, S. Nature (1987) [Pubmed]
  3. Hemagglutination by purified type I Escherichia coli pili. Salit, I.E., Gotschlich, E.C. J. Exp. Med. (1977) [Pubmed]
  4. Gonococcal pilus vaccine. Studies of antigenicity and inhibition of attachment. Tramont, E.C., Sadoff, J.C., Boslego, J.W., Ciak, J., McChesney, D., Brinton, C.C., Wood, S., Takafuji, E. J. Clin. Invest. (1981) [Pubmed]
  5. Integrin activation by bacterial fimbriae through a pathway involving CD14, Toll-like receptor 2, and phosphatidylinositol-3-kinase. Harokopakis, E., Hajishengallis, G. Eur. J. Immunol. (2005) [Pubmed]
  6. Porphyromonas gingivalis strain-dependent activation of human endothelial cells. Walter, C., Zahlten, J., Schmeck, B., Schaudinn, C., Hippenstiel, S., Frisch, E., Hocke, A.C., Pischon, N., Kuramitsu, H.K., Bernimoulin, J.P., Suttorp, N., Krüll, M. Infect. Immun. (2004) [Pubmed]
  7. Porphyromonas gingivalis fimbriae inhibit caspase-3-mediated apoptosis of monocytic THP-1 cells under growth factor deprivation via extracellular signal-regulated kinase-dependent expression of p21 Cip/WAF1. Ozaki, K., Hanazawa, S. Infect. Immun. (2001) [Pubmed]
  8. The effect of postnatal age on the adherence of Shigella flexneri, Escherichia coli 0124, and E. coli 0128 to guinea pig intestinal cells. Ashkenazi, S., Mirelman, D. Pediatr. Res. (1984) [Pubmed]
  9. Cyclic AMP-dependent synthesis of fimbriae in Salmonella typhimurium: effects of cya and pts mutations. Saier, M.H., Schmidt, M.R., Leibowitz, M. J. Bacteriol. (1978) [Pubmed]
  10. Bacterial adhesiveness: effects of the SH metabolite of erdosteine (mucoactive drug) plus clarithromycin versus clarithromycin alone. Braga, P.C., Zuccotti, T., Dal Sasso, M. Chemotherapy. (2001) [Pubmed]
  11. Purification and characterization of the CFA/I antigen of enterotoxigenic Escherichia coli. Evans, D.G., Evans, D.J., Clegg, S., Pauley, J.A. Infect. Immun. (1979) [Pubmed]
  12. Three-dimensional structure of Bordetella pertussis fimbriae. Heck, D.V., Trus, B.L., Steven, A.C. J. Struct. Biol. (1996) [Pubmed]
  13. Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa. Cachia, P.J., Hodges, R.S. Biopolymers (2003) [Pubmed]
 
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