Abstract
Bacteria entering a host depend on adhesins to achieve colonization. Adhesins are bacterial surface structures mediating binding to host surficial areas. Most adhesins are composed of one or several proteins. Usually a single bacterial strain is able to express various adhesins. The adhesion type expressed may influence host-, tissue or even cell tropism of Gram-negative and of Gram-positive bacteria. The binding of fimbrial as well as of afimbrial adhesins of Gram-negative bacteria to host carbohydrate structures (=receptors) has been elucidated in great detail. In contrast, in Gram-positives, most well studied adhesins bind to proteinaceous partners. Nevertheless, for both bacterial groups the binding of bacterial adhesins to eukaryotic carbohydrate receptors is essential for establishing colonization or infection. The characterization of this interaction down to the submolecular level provides the basis for strategies to interfere with this early step of infection which should lead to the prevention of subsequent disease. However, this goal will not be achieved easily because bacterial adherence is not a monocausal event but rather mediated by a variety of adhesins.
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References
Hacker J, Carniel E (2001) Ecological fitness, genomic islands and bacterial pathogenicity. A Darwinian view of the evolution of microbes. EMBO Rep 2:376–381
Hochhut B, Dobrindt U, Hacker J (2006) The contribution of pathogenecity islands to the evolution of bacterial pathogens. ASM Press, Washington
Nougayrede JP, Homburg S, Taieb F et al. (2006) Escherichia coli. induces DNA double-strand breaks in eukaryotic cells. Science 313:848–851
Ofek I, Hasty DL, Doyle JRJ (2003) Bacterial adhesion to animal cells and tissues. ASM Press, Washington
Dobrindt U, Hochhut B, Hentschel U, Hacker J (2004) Genomic islands in pathogenic and environmental microorganisms. Nat Rev Microbiol 2:414–424
Sharon N, Lis H (1989) Lectins as cell recognition molecules. Science 246:227–234
Sharon N, Lis H (2003) Lectins, 2nd edn. Kluwer Academic, Dordrecht
Khan AS, Schifferli DM (1994) A minor 987P protein different from the structural fimbrial subunit is the adhesin. Infect Immun 62:4233–4243
Khan AS, Johnston NC, Goldfine H et al. (1996) Porcine 987P glycolipid receptors on intestinal brush borders and their cognate bacterial ligands. Infect Immun 64:3688–3693
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
Gornik O, Dumic J, Flögel M et al. (2006) Glycoscience – a new frontier in rational drug design. Acta Pharm 56:19–30
Schulze IT (1975) The biologically active proteins of influenza virus: the hemagglutinin. In: Kilbourne ED (ed) The influenza viruses and influenza. Academic Press, New York, pp 53–82
Lefkowitz SS, Lefkowitz DL (1999) macrophage candidicidal activity of a complete glyconutritional formulation verses aloe polymannose. Proc Fisher Inst Med Res 1:5–7
Cao Z, Jefferson DM, Panjwani N (1998) Role of carbohydrate mediated adherence in cytopathogenic mechanism of Acanthamoeba. J Biol Chem 273:15838–15845
Choudhury D, Thompson A, Stojanoff V et al. (1999) X-ray structure of the FimC–FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science 285:1061–1066
Dupres V, Menozzi FD, Locht C et al. (2005) Nanoscale mapping and functional analysis of individual adhesins on living bacteria. Nat Methods 2:515–520
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
Stromberg N, Marklund B-I, Lund B et al. (1990) Host-specificity of uropathogenic Escherichia coli. depends on differences in binding specificity to Gala 1–4Gal-containing isoreceptors. EMBO 9:2001–2010
Sharon N (2006) Carbohydrates as future anti-adhesion drugs for infectious diseases. Biochim Biophys Acta 1760:527–537
Buts L, Bouckaert J, De Genst E et al. (2003) The fimbrial adhesin F17-G of enterotoxigenic E. coli has an immunoglobulin like lectin domain that binds N-acetylglucosamine. Mol Microbiol 49:705–715
Dodson KW, Pinkner JS, Rose T et al. (2001) Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor. Cell 105:733–743
Sung MA, Fleming K, Chen HA et al. (2001) The solution structure of PapGII from uropathogenic Escherichia coli. and its recognition of glycolipid receptors. EMBO Rep 2:621–627
Khan AS, Kniep B, Oelschlaeger TA et al. (2000) Receptor structure for F1C fimbriae of uropathogenic Escherichia coli. Infect Immun 68:3541–3547
Jones CH, Pinkner JS, Roth R et al. (1995) FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae. Proc Natl Acad Sci USA 92:2081–2085
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
Sokurenko EV, Chesnokova V, Dykhuizen DE et al. (1998) Pathogenic adaptation of Escherichia coli. by natural variation of the FimH adhesin. Proc Natl Acad Sci USA 95:8922–8926
Sharon N (1987) Bacterial lectins, cell-cell recognition and infectious disease. FEBS Lett 217:145–157
Firon N, Ofek I, Sharon N (1983) Carbohydrate specificity of the surface lectins of Escherichia coli, Klebsiella pneumoniae, and Salmonella typhimurium. Carbohydr Res 120:235–249
Firon N, Ofek I, Sharon N (1984) Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria. Infect Immun 43:1088–1090
Hung CS, Bouckaert J, Hung D et al. (2002) Structural basis of tropism of Escherichia coli. to the bladder during urinary tract infection. Mol Microbiol 44:903–915
Bouckaert J, Berglund J, Schembri M et al. (2005) Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli. FimH adhesin. Mol Microbiol 55:441–455
Duncan MJ, Mann EL, Cohen MS et al. (2005) The distinct binding specificities exhibited by enterobacterial type 1 fimbriae are determined by their fimbrial shafts. J Biol Chem 280:37707–37716
Pieters RJ (2007) Intervention with bacterial adhesion by multivalent carbohydrates. Med Res Rev 27:796–816
Korhonen TK, Väisänen-Rhen V, Rhen M et al. (1984) Escherichia coli. fimbriae recognizing sialyl galactosides. J Bacteriol 159:762–766
Korhonen TK, Valtonen MV, Parkkinen J et al. (1985) Serotypes, hemolysin production, and receptor recognition of Escherichia coli. strains associated with neonatal sepsis and meningitis. Infect Immun 48:486–491
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
Karlsson KA (1998) Meaning and therapeutic potential of microbial recognition of host glycoconjugates. Mol Microbiol 29:1–11
Roche N, Angstrom J, Hurtig M et al. (2004) Helicobacter pylori and complex gangliosides. Infect Immun 72:1519–1529
Patti JM, Allen BL, McGavin MJ et al. (1994) MSCRAMM-mediated adherence of microorganisms to host tissues. Annu Rev Microbiol 48:585–617
Lun, ZR, Wang, QP, Chen, XG et al. (2007) Streptococcus suis: an emerging zoonotic pathogen. Lancet Infect Dis 7:201–209
Haataja S, Tikkanen K, Liukkonen J et al. (1993) Characterization of a novel bacterial adhesion specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides. J Biol Chem 268:4311–4317
Haataja S, Tikkanen K, Nilsson U et al. (1994) Oligosaccharide-receptor interaction of the Gal alpha 1–4Gal binding adhesin of Streptococcus suis. Combining site architecture and characterization of two variant adhesin specificities. J Biol Chem 269:27466–27472
Haataja S, Tikkanen K, Hytonen J et al. (1996) The Galα 1–4 Gal-binding adhesin of Streptococcus suis, a Gram-positive meningitis-associated bacterium. Adv Exp Med Biol 408:25–34
Tikkanen, K, Haataja, S, Francois-Gerard, C et al. (1995) Purification of a galactosyl-alpha 1–4-galactose-binding adhesin from the Gram-positive meningitis-associated bacterium Streptococcus suis. J Biol Chem 270:28874–28878
Takamatsu D, Bensing BA, Prakobphol A et al (2006) Binding of the streptococcal surface glycoproteins GspB and Hsa to human salivary proteins. Infect Immun 74:1933–1940
Bensing BA, Gibson BW, Sullam PM (2004) The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export. J Bacteriol 186:638–645
Takamatsu, D, Bensing, BA, Cheng, H et al. (2005) Binding of the Streptococcus gordonii surface glycoproteins GspB and Hsa to specific carbohydrate structures on platelet membrane glycoprotein Ibalpha. Mol Microbiol 58:380–392
Ligtenberg AJ, Veerman EC, Nieuw Amerongen AV (2000) A role for Lewis a antigens on salivary agglutinin in binding to Streptococcus mutans. Antonie Van Leeuwenhoek 77:21–30
Barthelson R, Mobasseri A, Zopf D et al. (1998) Adherence of Streptococcus pneumoniae to respiratory epithelial cells is inhibited by sialylated oligosaccharides. Infect Immun 66:1439–1444
Idanpaan-Heikkila I, Simon PM, Zopf D et al. (1997) Oligosaccharides interfere with the establishment and progression of experimental pneumococcal pneumonia. J Infect Dis 176:704–712
Krivan HC, Roberts DD, Ginsburg V (1988) Many pulmonary pathogenic bacteria bind specifically to the carbohydrate sequence GalNAcβ1–4Gal found in some glycolipids. Proc Natl Acad Sci USA 85:6157–6161
Costerton, JW, Stewart, PS, Greenberg, EP (1999) Bacterial biofilms: a common cause of persistent infections. Science 284:1318–1322
Goetz F (2002) Staphylococcus and biofilms. Mol Microbiol 43:1367–1378
Ohlsen K, Lorenz U (2007) Novel targets for antibiotics in Staphylococcus aureus. Future Microbiol 2:655–666
Mack D, Becker P, Chatterjee I et al. (2004) Mechanisms of biofilm formation in Staphylococcus epidermidis and Staphylococcus aureus: functional molecules, regulatory circuits, and adaptive responses. Int J Med Microbiol 294:203–212
Heilmann C, Schweitzer O, Gerke C et al. (1996) Molecular basis of intercellular adhesion in the biofilm-forming Staphylococcus epidermidis. Mol Microbiol 20:1083–1091
Kozitskaya S, Cho SH, Dietrich K et al. (2004) The bacterial insertion sequence element IS256 occurs preferentially in nosocomial Staphylococcus epidermidis isolates: association with biofilm formation and resistance to aminoglycosides. Infect Immun 72:1210–1215
Mack D, Fischer W, Krokotsch A et al. (1996) The intercellular adhesin involved in biofilm accumulation of Staphylococcus epidermidis is a linear beta-1,6-linked glucosaminoglycan: purification and structural analysis. J Bacteriol 178:175–183
Anderson KL, Billington J, Pettigrew D et al. (2004) An atomic resolution model for assembly, architecture, and function of the Dr adhesins. Mol Cell 15:647–657
Oelschlaeger TA (2001) Adhesins as invasins. Int J Med Microbiol 291:7–14
Korhonen TK, Virkola R, Lähteenmäki K et al. (1992) Penetration of fimbriated enteric bacteria through basement membranes: a hypothesis. FEMS Microbiol Lett 79:307–312
Hernandes RT, Silva RM, Carneiro SM et al. (2008) The localized adherence pattern of an typical enteropathogenic Escherichia coli. is mediated by intimin micron and unexpectedly promotes HeLa cell invasion. Cell Microbiol 10:415–425
Jepson MA, Pellegrin S, Peto L et al. (2003) Synergistic roles for the Map and Tir effector molecules in mediating uptake of enteropathogenic Escherichia coli. (EPEC) into non-phagocytic cells. Cell Microbiol 5:773–783
DeVinney R, Gauthier A, Abe A et al. (1999) Enteropathogenic Escherichia coli: a pathogen that inserts its own receptor into host cells. Cell Mol Life Sci 55:961–976
Sinclair JF, Dean-Nystrom EA, O'Brien AD (2006) The established intimin receptor Tir and the putative eucaryotic intimin receptors nucleolin and ²1 integrin localize at or near the site of enterohemorrhagic Escherichia coli. O157:H7 adherence to enterocytes in vivo. Infect Immun 74:1255–1265
Selvarangan R, Goluszko P, Singhal J et al. (2004) Interaction of Dr adhesin with collagen type IV is a critical step in Escherichia coli. renal persistence. Infect Immun 72:4827–4835
Lillehoj EP, Kim BT, Kim KC (2002) Identification of Pseudomonas aeruginosa flagellin as an adhesin for Muc1 mucin. Am J Physiol Lung Cell Mol Physiol 282:L751–L756
Soto GE, Hultgren SJ (1999) Bacterial adhesins: common themes and variations in architecture and assembly. J Bacteriol 181:1059–1071
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Ohlsen, K., Oelschlaeger, T.A., Hacker, J., Khan, A.S. (2008). Carbohydrate Receptors of Bacterial Adhesins: Implications and Reflections. In: Lindhorst, T., Oscarson, S. (eds) Glycoscience and Microbial Adhesion. Topics in Current Chemistry, vol 288. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2008_10
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