Fimbriae Escherichia coli

T. K. Lindhorst, S. Kotter, U. Krallmann-Wenzel, and S. Ehlers, Trivalent a-D-mannoside clusters as inhibitors of type-1 fimbriae-mediated adhesion of Escherichia coli Structural variation and biotinylation, J. Chem. Soc. Perkin Trans., 1 (2001) 823-831. 

Nataro JP, DengY, ManevalDR, German AL, Martin WC, Levine MM Aggregative adherence fimbriae I of enteroaggregative Escherichia coli mediate adherence to HEp-2 cells and hemagglutination of human erythrocytes. Infect Immun 1992 60 2297-2304. 

Nataro JP, Yikang D, Giron JA, Savarino SJ, Kothary MH, Hall R Aggregative adherence fimbria I expression in enteroaggregative Escherichia coli requires two unlinked plasmid regions. Infect Immun 1993 61 1126-1131. 

Doughty, S., Sloan, J., Bennett-Wood, V., Robertson, M., Robins-Brown, R. M., and Hartland, E. L. (2002). Identification of a novel fibrial gene cluster related to long polar fimbriae in locus of enterocyte effacement-negative strains of enterohemorrhagic Escherichia coli. Infect. Immun. 70, 6761-6769. 

Hanisch, F.-G., Hacker, J., and Schroten, H. (1993). Specificity of S fimbriae on recombinant Escherichia coli Preference binding to gangliosides expressing NeuGc-a-(2-3)Gal and NeuAc-a-NeuAc. Infect. Immun. 61, 2108-2115. 

Klemm, P., and Krogfelt, K. A. (1994). Type 1 fimbriae of Escherichia coli. In "Fimbriae Adhesion, Genetics, Biogenesis, and Vaccines." (P. Klemm, ed.), pp. 9-26. CRC Press, Boca Raton. 

Krogfelt, K. A., Bergmans, H., and Klemm, P. (1995). Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae. Infect. Immun. 58, 1995-1998. 

Lindahl, M., and Carlstedt, I. (1990). Binding of K99 fimbriae of enterotoxigenic Escherichia coli to pig small intestinal mucin glycopeptides. J. Gen. Microbiol. 136,1609-1614. 

Moricout, M., Petit, J. M., Carias, J. R., and JuUen, R. (1990). Glycoprotein glycans that inhibit adhesion of Escherichia coli mediated K99 fimbriae Treatment of experimental colibacil-... 

Ono, E., Abe, K., Nakazawa, M., and Naiki, M. (1989). Ganglioside epitope recognized by K99 fimbriae from enterotoxigenic Escherichia coli. Infect. Immun. 57, 907-911. 

Thankavel, K., Madison, B., Ikeda, T., Malaviya, R., Shah, A. H., Arumugen, P. M., and Abraham, S. N. (1997). Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection. /. Clin. Invest. 100, 1123-1126. 

Xia, Y., Gaily, D., Forsman-Semb, K., and Uhlin, B. E. (2000). Regulatory cross-talk between adhesin operons in Escherichia coli Inhibition of type 1 fimbriae expression by the PapB protein. EMBO. 19,1450-1457. 

M. Forero, O. Yakovenko, E.V. Sokurenko, W.E. Thomas, V. Vogel, Uncoiling mechanics of escherichia coli type I fimbriae are optimized for catch bonds. PLoS Biol. 4, 1509-1516 (2006)... 

Escherichia coli is responsible for 85% of urinary tract infections (Schultz, 1984). Virtually all E. coli express type 1 fimbrae, and most uropathogenic E. coli express P fimbriae which are responsible for mediating the adherence of the bacteria to uroepithelial cells (Zafriri et al., 1989). Fructose is responsible for inhibiting the adherence of type 1 fimbriated E. coli while a polymeric compound inhibits P fimbriated E. coli (Zafriri et al., 1989). Recently, a study (Howell and Vorsa, 1998) identified this polymeric compound as condensed tannins (proanthocyanidins) based on the ability of proanthocyanidins purified from cranberries to inhibit the ability of P-fimbriated E. coli to attach to isolated uroepithelial cells at concentrations of 10-50 pg/mL. Blueberries, another member of the Vaccinium genus, may be a more palatable source of proanthicyanidins. 

Virtually all bacterial species and genera express lectins or lectin-like activities, frequently of more than one type and with different specificities. However, it is usually not known whether individual cells coexpress multiple types of lectin or each lectin is confined to a distinct cell population. Many Gram negative bacteria (for example, Escherichia coli and Salmonellae spp.) and a few Gram positive ones (e.g. certain actinomyces), produce surface lectins that are often in the form of submicroscopic hairlike appendages known as fimbriae (pili) that protrude from the surface of the cells. The best characterized bacterial surface lectins with respect to their molecular properties, carbohydrate specificity and genetics are the type 1 fimbriae specific for mannose and the type P fimbriae specific for galabiose, [Gal(al-4)Gal], produced by many strains of E. coli. Other examples are S fimbriae of E. coli, specific for NeuAc(a2-3)Gal, and type 2... 

This observation has an analogy in the world of microbes, which need to adhere effectively to the surface of their host cells to escape the shear forces of body fluids. Bacteria utilize both protein-protein and carbohydrate-protein interactions for adhesion. Pathogenic Escherichia coli (E. coli) bacteria, for example, responsible for more than 80% of urinary tract infections [2], possess thin hair-like structures on their surfaces, called pili and the shorter fimbriae. Fimbriae specifically recognize carbohydrates. Type 1 fimbriae of E. coli, for example, can, via their FimH lectin domain [3], bind a-D-mannopyranosides. Lectins, e.g. [4-7] named after the Latin word legere to pick out or choose [8] are carbohydrate recognizing proteins found everywhere in nature, e.g. [9-13] and are intensively studied structures. 

Yuyama Y, Yoshimatsu K, Ono E et al. (1993) Postnatal change of pig intestinal ganglioside bound by Escherichia coli with K99 fimbriae. J Biochem 113 488-492... 

Hacker J, Bender L, Ott M et al. (1990) Deletion of chromosomal regions coding for fimbriae and hemolysins occur in vitro and in vivo in various extraintestinal Escherichia coli isolates. Microb. Pathogenesis 8 213-225... 

Khan AS, Kniep B, Oelschlaeger TA et al. (2000) Receptor structure for F1C fimbriae of uropathogenic Escherichia coli. Infect Immun 68 3541-3547... 

Ponniah S, Endres RO, Hasty DL et al. (1991) Fragmentation of Escherichia coli type 1 fimbriae exposes cryptic D-mannose-binding sites. J Bacteriol 173 4195—4202... 

Korhonen TK, Vaisanen-Rhen V, Rhen M et al. (1984) Escherichia coli fimbriae recognizing sialyl galactosides. J Bacteriol 159 762-766... 

Prasadarao NV, Wass CA, Hacker J et al. (1993) Adhesion of S-fimbriated Escherichia coli to brain glycolipids mediated by sfaA gene-encoded protein of S-fimbriae J Biol chem 268 10356-10363... 

K Hedegaard, P Klemm. Type 1 fimbriae of Escherichia coli as carriers of heterologous antigenic sequences. Gene 85 115-124, 1989. 

The capacity of pathogenic bacteria to adhere to mucosal membranes has been exploited in the modification of new mucoadhesive polymers. The ability of bacteria to adhere to a specific target is rooted from particular cell-surface components or appendages, known as fimbriae, which promote adhesion to other cells or inanimate surfaces. Fimbriae are extracellular, long thread-like protein polymers of bacteria that play a major role in many diseases. It has been reported that Escherichia coli adheres specifically to the lymphoid follicle epithelium of the ileal Peyer s patch in rabbits. Similarly, different staphylococci possess the ability to adhere specifically to the surface of mucus gel layers and not mucus-free surfaces. Thus, polymers have been modified by the attachment of these fimbriae to enhance mucoadhesion. An attachment protein derived from E. coli, K99-fimbriae, has been covalently attached to polyacrylic acid networks in an attempt to provide a novel polymer with enhanced adhesive properties (Figure 52.7). ... 

Curli fimbriae, electron microscopy, environmental conditions, Escherichia coli, GGDEF domain, ompR, regulation, rpoS, Salmonella typhimurium, thin aggregative fimbriae. 

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