Skip to main content
SpringerLink
Log in

Pathogen-Host Protein-Carbohydrate Interactions as the Basis of Important Infections

  • Chapter
The Molecular Immunology of Complex Carbohydrates —2

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 491))

Abstract

Microbe-host protein-carbohydrate interactions are most likely the essential first step to produce an infection, although this has been strictly proven only in a few cases. Improvedglycotechnology will help identification of new carbohydrate receptors and this knowledge may be used to identify microbial carbohydrate-binding proteins by affinity proteomics approaches. In some cases such conserved proteins may prove to be successful vaccine components, in other cases, like influenza, saccharide analogues may be the only rational alternative. The prognosis may be, based on these improvements, that infection medicine will make considerable progress in the near future

Article FootNote

The work caried out in the author’s laboratory was supported by grants from the Swedish Medical Research Council, the Swedish Research Council for Engineering Sciences, the programs “Glycoconjugates in Biological Systems” and “Infection and Vaccinology” of the Swedish Foundation for Strategic Research, the Giiteborg Medical Faculty, Knut and Alice Wallenberg Foundation, and IngaBritt and Arne Lundberg Foundation.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Beachey, E.H. (1980) “Bacterial Adherence”, Receptors and Recognition, Series B, Vol. 6, Chapman & Hall, London.

    Google Scholar 

  2. Mirelman, D., ed. (1986) “Microbial Lectins and Agglutinins. Properties and Biological Activity”, John Wiley & Sons, New York.

    Google Scholar 

  3. Ofek, I., and Doyle, R.J. (1994)“Bacterial Adhesion to Cells and Tissues”, Chapman & Hall, London.

    Book  Google Scholar 

  4. Karlsson, K.-A. (1998) Meaning and therapeutic potential of microbial recognition of host glycoconjugates. Mol. Microbiol., 29:1–11.

    Article  PubMed  CAS  Google Scholar 

  5. McAuliffe, J.C., and Hindsgaul, O. (1997) Carbohydrate drugs-an ongoing challenge. Chemistry and Industry, No vol.:170–174.

    Google Scholar 

  6. Laver, W.G., Bischofberger, N., and Webster, R.G. (1999) Disarming flu viruses. Sci. Amer., 280:57–65.

    Article  Google Scholar 

  7. Yang, Z., Bergström, J., and Karlsson, K.-A. (1994) Glycoproteins with Gala4Gal are absent from human erythrocyte membranes, indicating that glycolipids are the sole carriers of blood group P activities. J. Biol. Chem., 269: 14620–14624.

    PubMed  CAS  Google Scholar 

  8. Teneberg, S., Lönnroth, I., Torres Lopez, J.F., Galili, U., Ölwegard Halvarsson, M., Angström, J., and Karlsson, K.-A. (1996) Molecular mimicry in the recognition of glycosphingolipids by Gala3Ga1ß4G1cNAc-binding Clostridium docile toxin A, human natural anti a-galactosyl IgG and the monoclonal antibody Gal-13: characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor. Glycobiology, 6:599–609.

    Article  PubMed  CAS  Google Scholar 

  9. H d, K., van Zadelhoff, G., Moononen, P., Kamerling, J.P., and Vliegenthart, J.F.G. (1992) The Asn-linked carbohydrate chains of human Tamm-Horsfall glycoprotein of one male. Novel sulfated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains. Eur. J. Biochem., 209:895–915.

    Article  Google Scholar 

  10. van Rooijen, J.J.M., Voskamp, A.F., Kamerling, J.P., and Vliegenthart, J.F.G. (1999) Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoproetin. Glycobiology, 9:21–30.

    Article  PubMed  Google Scholar 

  11. Mouricout, M., Petit, J.M., Carias, J.R., and Julien, R. (1990) Glycoprotein glycans that inhibit adhesion of Eschericha coli mediated by K99 fimbriae: treatment of experimental colibacillosis. Infect. Immun., 58:98–106.

    PubMed  CAS  Google Scholar 

  12. Teneberg, S., Willemsen, P.T.J., de Graaf, F.K., Stenhagen, G., Pimlott, W., Jovall, P.-A., Angström, J., and Karlsson, K.-A. (1994) Characterization of gangliosides of calf small intestine with special reference to receptor-active sequences for enteropathogenic Escherichia coli K99. J. Biochem., 116:560–574.

    PubMed  CAS  Google Scholar 

  13. Roberts, J.A., Markfund, B.-I., Iiver, D., Haslam, D., Kaack, M.D., Baskin, G., Louis, M., Möllby, R., Winberg, J., and Normark, S. (1994) The Gala4Gal-specific tip adhesin of Escherichia cob P fimbriae is needed for pyelonephritis to occur in the normal urinary tract. Proc. Natl. Acad. Sci. USA, 91:11889–11893.

    Article  CAS  Google Scholar 

  14. Petterson, J., Nordfelth, R., Dubinina, E., Bergman, T., Gustafsson, M., Magnusson, K.-E., and olf-Watz, H. (1996) Modulation of virulence factor expression by pathogen target cell contact. Science, 273:1231–1233.

    Article  Google Scholar 

  15. Comelis, G.R., and Wolf-Watz, H. (1997) The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol. Microbiol., 23:861–867.

    Article  Google Scholar 

  16. Zang, J.P., and Normark, S. (1996) Induction of gene expression in Escherichia coli after pilus-mediated adherence. Science, 273:1234–1236.

    Article  Google Scholar 

  17. Connel, H., Agace, W., Hedlund, M., Klemm, P., Shembri, M., and Svanborg, C. (1996) Fimbriae-mediated adherence induces mucosal inflammation and bacterial clearance. Consequences for antiadhesion therapy. Adv. Exp. Biol. Med., 408:73–80.

    Article  Google Scholar 

  18. Ofek, I., Goldhar, J., Keisari, Y., and Sharon, N. (1995) Nonopsonic phagocytosis of microorganisms. Annu. Rev. Microbiol., 49:239–276.

    Article  PubMed  CAS  Google Scholar 

  19. Haataja, S., Zhang, Z., Tikkanen, K., Magnusson, G., and Finne, J. (1999) Determination of the cell adhesion specificity of Streptococcus suis with the complete set of monodeoxy analogues of globotriose. Glycoconj. J., 16:67–71.

    Article  PubMed  CAS  Google Scholar 

  20. Lindberg, A.A., Brown, J.E., Stromberg, N., Westling-Ryd, M., and Karlsson, K.-A. (1987) Identification of the carbohydrate receptor for Shiga toxin produced by Shigella dysenteriae type 1. J. Biol. Chem., 262:1779–1785.

    PubMed  CAS  Google Scholar 

  21. Lacy, D.B., and Stevens, R.C. (1998) Unravelling the structures and mode of action of bacterial toxins. Curr. Op. Struct. Biol., 8:778–784.

    Article  CAS  Google Scholar 

  22. Brown, K.E., Anderson, S.M., and Young, N.S. (1993) Erythrocyte P antigen: cellular receptor for B19 parvovirus. Science, 262:114–117.

    Article  PubMed  CAS  Google Scholar 

  23. Bock, K., Breimer, M.E., Brignole, A., Hansson, G.C., Karlsson, K.-A., Larson, G., Leffler, H., Samuelsson, B.E., Str berg, N., Svanborg Edén, C., and Thurin, J. (1985) Specificity of binding of a strain of uropathogenic Escherichia coli to Gala4Gal-containing glycosphingolipids. J. Biol. Chem., 260:8545–8551.

    PubMed  CAS  Google Scholar 

  24. Stapleton, A.E., Stroud, M.R., Hakomori, S.-i., and Stamm, W.E. (1998) The globoseries glycosphingolipid sialosyl galactosyl globoside is found in urinary tract tissues and is a preferred binding receptor in vitro for uropathogenic E. coli expressing pap-encoded adhesins. Infect. Immun., 66:3856–3861.

    PubMed  CAS  Google Scholar 

  25. Stroud, M.R., Stapleton, A.E., and Levery, S.B. (1998) The P histo-blood group-related glycosphingolipid sialosyl galactosyl globoside as a preferred binding receptor for uropathogenic Escherichia coli: Isolation and structural characterization from human kidney. Biochemistry, 37:17420–17428.

    Article  PubMed  CAS  Google Scholar 

  26. Borén, T., Falk, P., Roth, K.A., Larson, G., and Normark, S. (1993) Attachment of Helicobacter pylori to human gastric epithelium mediated by blood group antigens. Science, 262:1892–1895.

    Article  PubMed  Google Scholar 

  27. Dunn, B.E., Cohen, H., and Blaser, M.J.(1997) Helicobacter pylori. Clin. Microbiol. Rev., 10:720–741.

    PubMed  CAS  Google Scholar 

  28. Rodighiero, C., Aman, A.T., Kenny, M.J., Moss, J., Lencer, W.I., and Hirst, T.R. (1999) Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity. J. Biol. Chem., 274:3962–3969.

    Article  PubMed  CAS  Google Scholar 

  29. Covacci, A., Telford, J.L., Del Giudice, G., Parsonnet, J., and Rappuoli, R. (1999) Helicobacter pylori virulence and genetic geography. Science, 284:1328–1333.

    Article  PubMed  CAS  Google Scholar 

  30. Evans, D.G., Evans Jr, D.J., and Graham, D.Y. (1988) N-acetylneuraminyllactose-binding fibrillar hemagglutinin of Campylobacter pylori: a putative colonization factor antigen. Infect. Immun., 56:2896–2906.

    PubMed  CAS  Google Scholar 

  31. Hirmo, S., Kelm, S., Schauer, R., Nilsson, B., and Wadström, T. (1996) Adhesion of Helicobacter pylori strains to a2,3-linked sialic acids. Glycoconj. 1, 13:1–7.

    Google Scholar 

  32. Miller-Podraza, H., Larsson, T., Nilsson, J., Teneberg, S., Matrosovich, M., and Johansson, L. (1998) Epitope dissection of of receptor-active gangliosides with affmity for Helicobacter pylori and influenza virus. Acta Biochim. Polon., 45:439–449.

    PubMed  CAS  Google Scholar 

  33. Miller-Podraza, H., Abul Milh, M., Bergstrom, J., and Karlsson, K.-A. (1996) Recognition of glycoconjugates by Helicobacter pylori: an apparently high-affinity binding of human polyglycosylceramides, a second sialic acid-based specificity. Glycoconj. J., 13:453–460.

    Article  PubMed  CAS  Google Scholar 

  34. Miller-Podraza, H., Bergstrom, J., Abul Milh, M., and Karlsson, K.-A. (1997) Recognition of glycoconjugates by Helicobacter pylori: comparison of two sialic acid-dependent specificities based on hemagglutination and binding to human erythrocyte glycoconjugates. Glycoconj. J., 14:467–471.

    Article  PubMed  CAS  Google Scholar 

  35. Miller-Podraza, H., Stenhagen, G., Larsson, T., Andersson, C., and Karlsson, K.-A. (1997) Screening for the presence of polyglycosylceramides in various tissues: partial characterization of blood group-active complex glycosphingolipids of rabbit and dog small intestines. Glycoconj. J., 14:231–239.

    Article  PubMed  CAS  Google Scholar 

  36. Teneberg, S., Miller-Podraza, H., Lampert, H.C., Evans Jr, D.J., Evans, D.G., Danielsson, D., and Karlsson, K.-A. (1997) Carbohydrate binding specificity of the neutrophil-activating protein of Helicobacter pylori. J. Biol. Chem., 272:19067–19071.

    Article  CAS  Google Scholar 

  37. Saitoh, T., Natomi, H., Zhao, W., Okuzumi, K., Sugano, K., Iwamori, M., and Nagai, Y. (1991) Identification of glycolipid receptors for Helicobacter pylori by TLC immunostaining. FEBS Lett., 282:385–387.

    Article  PubMed  CAS  Google Scholar 

  38. Ascencio, F., Fransson, L.-A., and Wadström, T. (1993) Affinity of the gastric pathogen Helicobacter pylori for the N-sulphated glycosaminoglycan heparan sulphate. J. Med. Microbiol., 38:240–244.

    Article  PubMed  CAS  Google Scholar 

  39. Gold, B., Huesca, M., Sherman, P., and Lingwood, C.A. (1993) Helicobacter mustelae and Helicobacter pylori bind to common receptors in vitro. Infect. Immun., 61:2632–2638.

    PubMed  CAS  Google Scholar 

  40. Angström, J., Teneberg, S., Abul Milh, M., Larsson, T., Leonardsson, I., Olsson, B.-M., Ölwegärd Halvarsson, M., Danielsson, D., Näslund, I., Ljung, A., Wadström, T., and Karlsson, K.-A. (1998) The lactosylceramide binding specificity of Helicobacter pylori. Glycobiology, 8:297–309.

    Article  Google Scholar 

  41. Ilver, D., Arngvist, A., Ogren, J., Frick, I.-M., Kersulyte, D., Incecik, E.T., Berg, D.E., Covacci, A., Engstrand, L., and Borén, T. (1998) Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging. Science, 279:373–377.

    Article  PubMed  CAS  Google Scholar 

  42. Mandavi, J., Sondén, B., Forsberg, L., Olfat, F.O., Sjöström, R., Roche, N., Angström, J., Teneberg, S., Karlsson, K.-A., Kersulyte, D., Berg, D.E., El-Zimaity, H.M.T., Graham, D.Y., Dubois, A., Lindh, F., Lundskog, B.B., Hammarström, L., and Borén, T. (1999) Helicobacter pylori infection elicits expression of sialylated Lewis antigens that confer bacterial adherence to the inflamed gastric epithelial lining. Submitted.

    Google Scholar 

  43. Miller-Podraza, H., Bergstr, J., Teneberg, S., Abul Milh, M., Longard, M., Olsson, B.-M., Uggla, L., and Karlsson, K.-A. (1999) Helicobacter pylori and neutrophils: sialic acid-dependent binding to various isolated glycoconjugates. Infect. Immun., in press.

    Google Scholar 

  44. Sakamoto, S., Watanabe, T., Tokumaro, T., Takagi, H., Nakazato, H., and Lloyd, K.O. (1989) Expression of Lewis a, Lewis b, Lewis x, Lewis y, sialyl-Lewis a, and sialyl-Lewis x blood group antigens in human gastric carcinoma and in normal gastric tissue. Cancer es., 49:745–752.

    CAS  Google Scholar 

  45. Hakomori, S.-i. (1996) Tumor malignancy defined by aberrant glycosylation and sphingo(glyco)lipid metabolism. Cancer Res., 6:5309–5318.

    Google Scholar 

  46. Snyder, A.J., Guruge, J.L., Li, Q., Hu, Y., Oleksiewicz, C.M., Lorenz, R.G., Karam, S.M., Falk, P.G., and Gordon, J.I. (1999) Helicobacter pylori attaches to NeuAca2,3Galß1,4 glycoconjugates produced in the stomach of transgenic mice lacking parietal cells. Mol. Cell., 3:263–274.

    Article  Google Scholar 

  47. Rautelin, H., Blomberg, B., Fredlund, H., Jämerot, G., and Danielsson, D. (1993) Incidence of Helicobacter pylori strains activating neutrophils in patients with peptic ulcer disease. Gut, 34;599–603.

    Article  PubMed  CAS  Google Scholar 

  48. Kirshner, D.E., and Blaser, M.J. (1995) The dynamics of Helicobacter pylori infection in the human stomach. J. Theoret. Biol., 76:281–290.

    Article  Google Scholar 

  49. Blaser, M.J. (1996) The bacteria behind ulcers. Sci. Amer., 274:92–97.

    Article  Google Scholar 

  50. Blaser, M.J. (1997) Not all Helicobacter strains are created equal: should all be eliminated? Lancet, 349:1020-.

    Article  PubMed  CAS  Google Scholar 

  51. Telford, J.L., Covacci, A., Rappuoli, R., and Ghiara, P. (1997) Immunobiology of Helicobacter pylori infection. Curr. Opin. Immunol., 9:498–503.

    Article  PubMed  CAS  Google Scholar 

  52. Karlsson, H., Johansson, L., Miller-Podraza, H., and Karlsson, K.-A. (1999) Fingerprinting of large oligosaccharides linked to eramide by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: highly heterogeneous olyglycosylceramides of uman erythrocytes with receptor activity for Helicobacter pylori. Glycobiology, 9:765–778.

    Article  CAS  Google Scholar 

  53. Tomb, J.-F., White, O., Kerlavage, A.R., Clayton, R.A., Sutton, G.G., Fleishmann, R.D., Ketchum, K.A., Klenk, H.P., Gill, S., Dougherty, B.A., Nelson, K., Quackenbush, J., Zhou, L., Kirkness, E.F., Peterson, S., Loftus, B., Richardson, D., Dodson, R., Khalak, H. G., Glodek, A., McKenney, K., Fitzgerald, L.M., Lee, N., Adams, M.D., Hickey, E.K., Berg, D.E., Gocayne, J.D., Utterback, T.R., Peterson, J.D., Kelley, J.M., Cotton, M.D., Weidman, J.W., Fuji, C., Bowman, C., Whattey, L., Wallin, E., Hayes, W.S., Borodowski, M., Karp, P.D., Smith, H.O., Fraser, C.M., and Venter, J.C. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature, 388:539–547.

    CAS  Google Scholar 

  54. Alm, R.A., Ling, L.S.-L., Moir, D.T., King, B.L., Brown, E.D., Doig, P.C., Smith, D.R., Noonan, B., Guild, B.C., deJonge, B.L., Cannel, G., Tummino, P.J., Caruso, A., Uria-Nickelsen, M., Mills, D.M., Ives, C., Gibson, R., Merberg, D., Mills, S.D., Jiang, Q., Taylor, D.E., Vovis, G.F., and T.J. Trust, T.J. (1999) Genomic-sequence comparison of two unrelated isolates of the human pathogen Helicobacter pylori. Nature, 397:176–180.

    Article  PubMed  Google Scholar 

  55. Falk, P.G., Bry, L., Holgersson, J., and Gordon, J.I. (1995) Expression of a human a-1,3/4-fucosyltransferase in the pit cell lineage of FVB/N mouse stomach results in the production of Leb-containing glycoconjugates: a potential transgenic mouse model for studying Helicobacter pylori infection. Proc. Natl. Acad. Sci. USA, 92:1515–1519.

    Article  PubMed  CAS  Google Scholar 

  56. Guruge, J.L., Falk, P.G., Lorenz, R.G., Dans, M., Wirth, H.-P., Blaser, M.J., Berg, D.E., and J.I. Gordon, J.I. (1998) Epithelial attachment alters the outcome of Helicobacter pylori infection. Proc. Natl. Acad. Sci. USA, 95:3925–3930.

    Article  PubMed  CAS  Google Scholar 

  57. . Karlsson, K.-A. (1995) Microbial recognition of target-cell glycoconjugates. Curr. Opin. Struct. Biol., 5:622-635.

    Article  PubMed  CAS  Google Scholar 

  58. Weis, W., Brown, J.H., Cusack, S., Paulson, J.C., Skehel, J.J., and D.C. Wiley, D.C. (1988) Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature, 333:426–431.

    Article  PubMed  CAS  Google Scholar 

  59. von Itzstein, M., Wu, W.-Y., Kok, G.B., Pegg, M.S., Dyason, J.C., Jin, B., Van Phan, T., Smythe, M.L., White, H.F., Oliver, S.W., Colman, P.M., Varghese, J.N., Ryan, D.M., Woods, J.M., Bethell, R.C., Hotman, V.J., Cameron, J.M., and Penn, C.R. (1993) Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature, 363:418–423.

    Article  Google Scholar 

  60. Kim, C.U., Lew, W., Williams, M.A., Liu, H., Zhang, L., Swaminathan, S., Bischofberger, N., Chen, M.S., Mendel, D.B., Tai, C.Y., Laver, W.G., and Stevens, R.C. (1997) Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc., 119:681–690.

    Article  PubMed  CAS  Google Scholar 

  61. Choudbury, D., Thompson, A., Stojanoff, V., Langermann, S., Pinkner, J., Hultgren, S.J., and Knight, S.D. (1999) X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science, 285:1061–1066.

    Google Scholar 

  62. Gagneux, P., and Varki, A. (1999) Evolutionary considerations in relating oligosaccharide diversity to biological function. lycobiology, 9:747–755.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Medical Biochemistry, Göteborg University, P.O. Box 440, Göteborg, SE-405 30, Sweden

    Karl-Anders Karlsson

Authors
  1. Karl-Anders Karlsson
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Glyco Research Laboratory Institutes of Basic Medical Sciences and Natural Products, College of Medicine Chang-Gung University, Kwei-san, Tay-yuan, Taiwan

    Albert M. Wu

  2. Tao-yuan, 333, Taiwan

    Albert M. Wu

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Springer Science+Business Media New York

About this chapter

Cite this chapter

Karlsson, KA. (2001). Pathogen-Host Protein-Carbohydrate Interactions as the Basis of Important Infections. In: Wu, A.M. (eds) The Molecular Immunology of Complex Carbohydrates —2. Advances in Experimental Medicine and Biology, vol 491. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1267-7_28

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-1267-7_28

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5469-7

  • Online ISBN: 978-1-4615-1267-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation