Abstract
The purpose of this chapter is to review briefly the composition and organization of animal cell surface structures that may be potential receptors for adhesins of bacteria. The understanding of the specificity of animal cell—bacteria interactions requires a basic knowledge of the molecular structure of the animal cell surface, especially of those molecules that serve as receptors for ligands in general and for bacterial adhesins in particular. All animal cell membranes share common compositional and organizational features (Figure 3-1): (1) The major membrane lipids are arranged in a planar bilayer configuration that is predominantly in a “fluid” state under physiological conditions. The membrane lipids are commonly composed of glycerolphospholipids, sphingolipids, and sterols. (2) The bilayer membrane contains integral membrane constituents composed of both glycolipids and glycoproteins that are inserted or “intercalated” into the bilayer structure. (3) Other glycoproteins and proteins are bound to the surface of the plasma membrane by weak ionic interactions, hydrogen bonding, or the hydrophobic effect. These surface-associated glycoproteins and proteins bound to integral membrane structures are referred to as peripheral or extrinsic components. (4) In many animal cells there is a substantial layer of carbohydrate-containing materials of variable thicknesses outside the plasma membrane but in close or intimate association with the membrane. This layer is known as the cell coat or extracellular matrix. The distinction between membrane constituents as being integral, peripheral, or belonging to the cell coat is based on the method required to dissociate the constituent in question from the cell membrane. The integral constituents may be released only after disruption or perturbation of the phospholipid bilayer, usually by detergents (Lichtenberg et al., 1983). Nonintegral surface constituents are commonly released by washing the cells with buffers of different pH or ionic strength, or by using chelating agents, such as ethylenediaminetetraacetic acid (EDTA). There is no general method, however, to release selectively either peripheral or extracellular matrix constituents. As a result, the distinction between the two classes of membrane constituents is sometimes difficult to resolve and very often they are referred to as nonintegral membrane constituents. One of the key features of the membrane is its asymmetry. For nonglycosylated lipids the asymmetry is only partial, in that every phospholipid is present on both sides of the bilayer but in different amounts. In human erythrocytes, for example, lipids with positively charged head groups (e.g., phosphatidylethanolamine and phosphatidylserine) are predominant in the internal leaflet facing the cytoplasm (Marinetti and Crain, 1978). The asymmetry with respect to proteins, glycoproteins, and glycolipids is absolute: every molecule of a given membrane constituent has the same orientation across the lipid bilayer, with the carbohydrate moieties of the glycosylated compounds always exposed on the outer surface. For further information on the organization of the animal cell membrane, the reader is referred to reviews (Lodish et al., 1981; Lotan and Nicolson, 1981; Singer, 1981; Aplin and Hughes, 1982) and a book (Sim, 1982).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Aplin, J.D. and R.C. Hughes. 1982. Complex carbohydrates of the intracellular matrix: structures, interactions and biological roles. Biochim. Biophys. Acta 694: 375–418.
Ashwell, G. and J. Harford. 1982. Carbohydrate-specific receptors of the liver. Annu. Rev. Biochem. 51: 531–554.
Beachey, E.H., W.A. Simpson, I. Ofek, D.K. Hasty, J.B. Dale, and E. Whitnack. 1983. Attachment of Streptococcus pyogenes to mammalian cells. Rev. Infect. Dis. 5: 5670–5677.
Callies, R., G. Schwarzmann, K. Radsak, R. Siegert, and H. Wiegandt. 1977. Characterization of the cellular binding of exogenous gangliosides. Eur. J. Biochem. 80: 425–423.
Cherry, R.J. 1979. Rotational and lateral diffusion of membrane proteins. Biochim. Biophys. Acta 559: 289–327.
Clamp, J. 1974. Analysis of glycoproteins. Biochem. Soc. Symp. 40: 3–16.
Critchley, D.R. 1979. Glycolipids as membrane receptors important in growth regulation. In: Hynes, R.O. (ed.), Surfaces of Normal and Malignant Cells. John Wiley & Sons, New York, pp. 63–101.
Critchley, D.R., C.H. Streuli, S. Kellie, S. Ansell, and B. Patel. 1982. Characterization of the cholera toxin receptor on Balb/C3T3 cells as a ganglioside similar to, or identical with, ganglioside GM,: no evidence for galactoproteins with receptor activity. Biochem. J. 204: 209–219.
Cuatrecasas. P. 1974. Membrane receptors. Annu. Rev. Biochem. 43: 169–214.
Duk, M., E. Lisowska, M. Kordowicz, and K. Wasniowska. 1982. Studies on the specificity of the binding site of Vicia graminea anti-N lectin. Eur. J. Biochem. 123: 105–112.
Edidin, M. 1974. Rotational and translational diffusion in membranes. Annu. Rev. Biophys. Bioeng. 8: 165–193.
Eytan, G.D. 1982. Use of liposomes for reconstruction of biological function. Biochim. Biophys. Acta 694: 185–202.
Feldner, J., W. Bredt, and I. Kahane. 1979. Adherence of erythrocytes to Mycoplasma pneumoni ae. Infect. Immun. 30: 554–561.
Findlay, J.B.C. 1974. The receptor proteins for concanavalin A and Lens culinaris phytohemagglutinin in the membrane of the human erythrocyte. J. Biol. Chem. 249: 4398–4403.
Finean, J.B., R. Coleman, and R.H. Mitchell. 1984. Membranes and Their Cellular Function, 3rd ed. Blackwell, Oxford.
Finne, J. 1980. Identification of the blood-group ABO-active glycoprotein components of human erythrocyte membrane. Eur. J. Biochem. 104: 181–189.
Fishman, P.H. 1982. Role of membrane gangliosides in the binding and action of bacterial toxins. J. Membr. Biol. 69: 85–97.
Flowers, H.M. and N. Sharon. 1979. Glycosidases-properties and application to the study of complex carbohydrates and cell surfaces. Adv. Enzymol. 48: 29–95.
Fukuda, M. and M.N. Fukuda. 1978. Changes in cell surface glycoproteins and carbohydrate structures during the development and differentiation of human erythroid cells. J. Supramol. Struct. 8: 313–324.
Gahmberg, C.G. 1977. Cell surface proteins: changes during cell growth and malignant transformation. In: Poste, G. and G.L. Nicholson (eds.), Cell Surface Reviews. North-Holland, Amsterdam, pp. 371–421.
Gahmberg, C.G. 1981. Membrane glycoproteins and glycolipids: structure, localization and function of carbohydrates. In: Finean, J.B. and R.H. Mitchell (eds.), Membrane Structure. Elsevier/North-Holland, Amsterdam, pp. 127–160.
Gahmberg, C.G. and L.C. Anderson. 1982. Surface glycoproteins of malignant cells. Biochim. Biophys. Acta 651: 65–83.
Garoff, H. 1979. Structure and assembly of the Semliki Forest virus membrane. Biochem. Soc. Trans. 7: 301–306.
Geiger, B. 1983. Membrane cytoskeleton interactions. Biochim. Biophys. Acta 737: 305–341.
Hakomori, S. 1981. Glycosphingolipids in cellular interaction, differentiation and oncogenesis. Annu. Rev. Biochem. 50: 733–764.
Hynes, R.O. and K.M. Yamada. 1982. Fibronectins: multifunctional molecular glycoproteins. J. Cell Biol. 95: 369–377.
Izhar, M., Y. Nuchamowitz, and D. Mirelman. 1982. Adherence of Shigella flexneri to guinea pig intestinal cells is mediated by a mucosal adhesin. Infect. Immun. 35: 1110–1118.
Kallenius, G., S.B. Svensson, R. Mollby, B. Cedergren, H. Hultberg, and J. Winberg. 1981. Structure of carbohydrate part of receptor on human uroepithelial cells for pyelonephritogenic Escherichia coli. Lancet 2: 604–606.
Koscielak, J., H. Miller-Podraza, R. Krauze, and A. Piasek. 1976. Isolation and characterization of poly(glycosyl) ceramides (megaloglycolipids) with A,H and I blood-group activities. Eur. J. Biochem. 71: 9–18.
Leffler, H. and C. Svanborg-Eden. 1981. Glycolipid receptors for uropathogenic Escherichia coli on human erythrocytes and uroepithelial cells. Infect. Immun. 34: 920–929.
Lichtenberg, D., R.J. Robson, and E.A. Dennis. 1983. Solubilization of phospholipids by detergents: structural and kinetic aspects. Biochim. Biophys. Acta 737: 285–304.
Lodish, H.F., W.A. Braell, A.L. Schwartz, G.J.A.M. Strous, and A. Zilberstein. 1981. Synthesis and assembly of membrane and organelle proteins. Int. Rev. Cytol. Suppl. 12: 247–307.
Lotan, R. and G.L. Nicolson. 1981. Plasma membrane of eukaryotes, In: Schwartz, L.M. and M.M. Azar (eds.), Advanced Cell Biology. Van Nostrand-Reinhold, Princeton, NJ, pp. 129–154.
Marchesi, V.T., H., Furthmayr, and M., Tornita. 1976. The red cell membrane. Annu. Rev. Biochem. 45: 667–698.
Marinetti, G.V. and R.C., Crain, 1978. Topology of amino-phospholipids in the red-cell membrane. J. Supramol. Struct. 8: 191–213.
Mirelman, D. and I. Ofek. 1986. Introduction to microbial lectins and agglutinins. In: Mirelman, D. (ed.), Microbial Lectins and Agglutinins. John Wiley & Sons, New York, pp. 1–19.
Nicolson, G.L. 1976. Trans-membrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence of cell surface components. Biochim. Biophys. Acta 457: 57–108.
Nicolson, G.L. 1979. Topographic display of cell surface components and their role in trans-membrane signaling. Curr. Top. Dev. Biol. 3: 305–338.
Ofek, I., H. Lis, and N. Sharon. 1985. Animal cell surface membranes. In: Savage, D.C. and M. Fletcher (eds.), Bacterial Adhesion: Mechanisms and Physiological Significance, Plenum Press, New York, pp. 71–88.
Prives, J.M. 1980. Nicotinic acetylcholine receptors. In: Schulster, D. and A. Levitski (eds.), Cellular Receptors for Hormones and Neurotransmitters. John Wiley & Sons, New York, pp. 331–351.
Raff, M.C. and S. dePetris. 1973. Movement of lymphocyte surface antigens and receptors: the fluid nature of the lymphocyte plasma membrane and its immunological significance. Fed. Proc. 32: 48–54.
Roth, J. 1980. The use of lectins as probes for carbohydrates-cytochemical techniques and their application in studies on cell surface dynamics. Acta Histochem. Suppl. 22: 113–121.
Ruoslahti, E. 1988. Fibronectin and its receptors. Annu. Rev. Biochem. 57:375–413. Ruoslahti, E. 1991. Integrins. J. Clin. Invest. 87: 1–5.
Ruoslahti, E., M. Pierschbacher, E.G. Hayman, and E. Engvall. 1982. Fibronectin: a molecule with remarkable structural and functional diversity. Trends Biochem. Sci. 7: 188–190.
Schulster, D. and A. Levitski (eds.). 1980. Cellular Receptors for Hormones and Neurotransmitters. John Wiley & Sons, New York.
Sedlacek, H.H., J. Stark, F.R. Seiler, W. Ziegler, and H. Wiegandt. 1976. Cholera toxin induces redistribution of sialoglycolipid receptor at the lymphocyte membrane. FEBS Lett. 61: 272–276.
Sharon, N. 1975. Complex Carbohydrates: Their Chemistry, Biosynthesis, and Functions. Addison-Wesley, Reading, MA.
Sharon, N. 1981. Glycoproteins in membranes. In: Balian, R., M. Chabre, and P.F. Devaux (eds.), Membranes and Intercellular Communications. North-Holland, Amsterdam, pp. 117–182.
Sharon, N. and H. Lis 1981. Glycoproteins: research booming on long-ignored, ubiquitous compounds. Chem. Engr. News 59: 21–24.
Sharon, N. and H. Lis. 1982. Glycoproteins. In: Neurath, H., and R.L. Hill (eds.), The Proteins, Vol. V, 3rd ed. Academic Press, New York, pp. 1–144.
Sharon, N. and H. Lis. 1989. Lectins as cell recognition molecules. Science 246: 227–234.
Sim, E. 1982. Membrane Biochemistry. Chapman and Hall, London.
Singer, S.J. 1974. The molecular organization of membranes. Annu. Rev. Biochem. 43: 805–833.
Singer, S.J. 1981. The cell membrane. In: Balian, R., M. Chabre, and P.F. Devaux (eds.), Membranes and Intercellular Communication. North-Holland, Amsterdam, pp. 1–16.
Singer, S.J. and G.L. Nicolson. 1972. The fluid mosaic model of cell membranes. Science 175: 710–731.
Steck, T.L. 1978. Band 3 protein of the human red cell membrane: a review. J. Supramol. Struct. 8: 311–324.
Tanner, M.J.A. 1978. Erythrocyte glycoproteins. Curr. Top. Membr. Transp. 11: 279–325.
Tollefsen, S.E. and R. Kornfeld. 1983. The B4 lectin from Vicia villosa interacts with N-acetylgalactosamine residues linked to serine or threonine residues in cell surface glycoproteins. J. Biol. Chem. 258: 5172–5176.
Wicken, A.J. and K.W. Knox. 1981. Composition and properties of amphiphiles. In: Shockman, G.D. and A.J. Wicken (eds.), Chemistry and Biological Activities of Bacterial Surface Amphiphiles. Academic Press, New York, pp. 1–7.
Wiegandt, H., S. Kanda, K. Inoue, K. Utsumi, and S. Nojima. 1981. Studies on the cell association of exogenous glycolipids. Adv. Exp. Med. Biol. 152: 343–352.
Yamakawa, T. and Y. Nagai. 1978. Glycolipids at the cell surface and their biological functions. Trends Biochem. Sci. 3: 128–131.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1994 Chapman & Hall, Inc.
About this chapter
Cite this chapter
Ofek, I., Doyle, R.J. (1994). Animal Cell Membranes as Substrata for Bacterial Adhesion. In: Bacterial Adhesion to Cells and Tissues. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6435-1_3
Download citation
DOI: https://doi.org/10.1007/978-1-4684-6435-1_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-6437-5
Online ISBN: 978-1-4684-6435-1
eBook Packages: Springer Book Archive