Identification and Biology of Cellular Receptors for the Coxsackie B Viruses Group

  • R. J. Kuhn
Part of the Current Topics in Microbiology and Immunology book series (CT MICROBIOLOGY, volume 223)


The picornaviruses represent a diverse and well studied family of RNA-containing animal viruses. In addition to having a simple structural organization and a limited size plus-strand RNA genome, members of the family constitute a significant group of human and animal pathogens. The coxsackie B viruses (CVB), which belong to the enterovirus genus of Picornaviridae, have long been recognized as the causative agents for a number of human ailments frequently involving the heart. Infection of neonates with CVB commonly occurs and can sometimes result in severe consequences. The tissue tropism of these and other viruses has long been thought to be controlled at least in part by the interaction of surface residues on the virus with specific cellular proteins found on the membrane of the target cells. The binding of the virus to these cellular proteins, which act as receptors, results ultimately in the entry of viral nucleic acid into the target cell through processes that are poorly understood (Rossmann 1994).


HeLa Cell Cellular Receptor Virus Group Decay Accelerate Factor Short Consensus Repeat 
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  1. Bergelson JM, Shepley MP, Chan BMC, Hemler ME, Finberg RW (1992) Identification of the integrin VLA-2 as a receptor for echovirus 1. Science 255:1718–1720PubMedCrossRefGoogle Scholar
  2. Bergelson JM, Chen M, Solomon KR, St John NF, Lin H, Finberg RW (1994) Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses. Proc Natl Acad Sci US 91:6245–6248CrossRefGoogle Scholar
  3. Bergelson M, Mohanty JG, Crowell RL, St John NF, Lublin DM, Finberg RW (1995) Coxsackievirus B3 adapted to growth in RD cells binds to decay-accelerating factor (CD55). J Virol 69:1903–1906PubMedGoogle Scholar
  4. Berinstein A, Roivainen M, Hovi T, Mason PW, Baxt B (1995) Antibodies to the vitronectin receptor (integrin a ) inhibit binding and infection of foot-and-mouth disease virus to cultured cells. J Virol 69:2664–2666PubMedGoogle Scholar
  5. Borer RA, Lehner CF, Eppenberger HM (1989) Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56:379–390PubMedCrossRefGoogle Scholar
  6. Butters TD, Hughes RC (1974) Solubilization and fractionation of glycoproteins and glycolipids of KB cell membranes. Biochem J 140:469–78PubMedGoogle Scholar
  7. Campbell BA, Cords, CE (1983) Monoclonal antibodies that inhibit attachment of group B coxsackieviruses. J Virol 48:561–564PubMedGoogle Scholar
  8. Caras IW, Davitz MA, Rhee L, Weddell G, DW, Martin J, Nussenzweig V (1987) Cloning of decay-accelerating factor suggests novel use of splicing to generate two proteins. Nature 325: 545–549PubMedCrossRefGoogle Scholar
  9. Clarkson NA, Kaufman R, Lublin DM, Ward T, Pipkin PA, Minor PD, Evans DJ, Almond, JW (1995) Characterization of the echovirus 7 receptor: Domains of CD55 critical for virus binding. J Virol 69:5497–5501PubMedGoogle Scholar
  10. Colonno RJ, Callahan PL, Long WL (1986) Isolation of a monoclonal antibody that blocks attachment of the major group of human rhinoviruses. J Virol 57:7–12PubMedGoogle Scholar
  11. Cooper NR, Moore MD, Nemerow GR (1988) Immunobiology of CR2, the lymphocyte receptor for Epstein-Barr virus and the C3d complement fragment. Annu Rev Immunol 6:85–113PubMedCrossRefGoogle Scholar
  12. Cova L, Aymard M (1980) Isolation and characterization of non-hemagglutinating echovirus 11. J Gen Virol 51:219–222PubMedCrossRefGoogle Scholar
  13. Coyne KE, Hall,SE, Thompson ES, Arce MA, Kinoshita T, Fujita T, Anstee DJ, Rosse W, Lublin DM (1992) Mapping of epitopes, glycosylation sites, and complement regulatory domains in human decay accelerating factor. J Immunol 149:2906–2913PubMedGoogle Scholar
  14. Crowell RL (1963) Specific viral interference in HeLa cell cultures chronically infected with coxsackie B5 virus. J Bacteriol 86:517–526PubMedGoogle Scholar
  15. Crowell RL (1966) Specific cell-surface alteration by enteroviruses as reflected by viral-attachment interference. J Bacteriol 91:198–204PubMedGoogle Scholar
  16. Crowell RL, Field AK, Schleif WA, Long WL, Colonno RJ, Mapoles JE, Emini EA (1986) Monoclonal antibody that inhibits infection of the HeLa and rhabdomyosarcoma cells by selected enteroviruses through receptor blockade. J Virol 57:438–445PubMedGoogle Scholar
  17. Crowell RL, Landau BJ (1983) Receptors in the initiation of picornavirus infections. In: Fraenkel-Conrat HWagner RR (eds) Comprehensive virology, Plenum, New York, 18:1–42Google Scholar
  18. Crowell RL, Philipson L (1971) Specific alterations of coxsackievirus B3 eluted from HeLa cells. J Virol 8:509–515PubMedGoogle Scholar
  19. Crowell RL, Siak J-S (1978) Receptor for the group B coxsackieviruses: characterization and extraction from HeLa cell plasma membrane. In: Pollard M (ed) Perspectives in Virology. Raven, New York, pp 39–53Google Scholar
  20. deVerdugo UR, Selinka,HC, Huber M, Kramer B, Kellermann J, Hofschneider PH, Kandolf R (1995) Characterization of a 100-kilodalton binding protein for the six serotypes of coxsackie B viruses. J Virol 69:6751–6757Google Scholar
  21. Dorig RE, Marcil A, Chopra A, Richardson CD (1993) The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295–305PubMedCrossRefGoogle Scholar
  22. Gerlier D, Varior-Krishnan G, Devaux, P (1995) CD46-mediated measles virus entry: a first key to hostrange specificity. Trends in Microbiol 3:338–345CrossRefGoogle Scholar
  23. Greve JM, Davis G, Meyer AM, Forte CP, Yost SC, Marlor CW, Karmarck ME, McClelland, A (1989) The major human rhinovirus receptor is ICAM-1. Cell 56:839–847PubMedCrossRefGoogle Scholar
  24. Greve JM, Forte CP, Marlor CW, Meyer AM, Hoover-Litty H, Wunderlich D, McClelland A (1991) Mechanisms of receptor-mediated rhinovirus neutralization defined by two soluble forms of ICAM-1. J Virol 65:6015–6023PubMedGoogle Scholar
  25. Hofer F, Gruenberger M, Kowalski H, Machat H, Huettinger M, Kuechler E, Blaas D (1994) Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus. Proc Natl Acad Sci USA 91: 1839–1842PubMedCrossRefGoogle Scholar
  26. Hogle JM, Chow M, Filman DJ (1985) Three-dimensional structure of poliovirus at 2.9 A resolution. Science 229:1358–1365PubMedCrossRefGoogle Scholar
  27. Holland JJ (1962) Irreversible eclipse of poliovirus by HeLa cells. Virology 16:163–176PubMedCrossRefGoogle Scholar
  28. Holland JJ, McLaren LC, Syverton JT (1959a) Mammalian cell-virus relationship III. Poliovirus production by nonprimate cells exposed to poliovirus ribonucleic acid. Proc Soc Exp Med 100: 843–845Google Scholar
  29. Holland JJ, McLaren LC, Syverton JT (1959b) The mammalian cell-virus relationship IV. Infection of naturally insusceptible cells with enterovirus ribonucleic acid. J Exp Med 110:65–80PubMedCrossRefGoogle Scholar
  30. Hsu KHL, Paglini S, Alstein B, Crowell RL (1990) Identification of a second cellular receptor for a coxsackievirus B3 variant, CB3-RD. In: MA Brinton FX Heinz (ed) New aspects of positive-strand RNA viruses, American Society for Microbiology, Washington, DC pp 271–277Google Scholar
  31. Hsu KL, Crowell RL (1989) Characterization of a YAC-1 mouse cell receptor for Group B caxsackieviruses. J Virol 63:3105–3108PubMedGoogle Scholar
  32. Hsu KL, Longberg-Holm K, Alstein B, Crowell RL (1988) A monoclonal antibody specific for the cellular receptor for the group B coxsackieviruses. J Virol 62:1647–1652PubMedGoogle Scholar
  33. Huber SA (1994) VCAM-1 is a receptor for encephalomyocarditis virus on murine vascular endothelial cells. J Virol 68:3453–3458PubMedGoogle Scholar
  34. Jordan P, Heid H, Kinzel V, Kiibler D (1994) Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins. Biochemistry 33:14696–14706PubMedCrossRefGoogle Scholar
  35. Kaplan G, Freistadt MS, Racaniello VR (1990) Neutralization of poliovirus by cell receptors expressed in insect cells. J Virol 64:4697–4702PubMedGoogle Scholar
  36. Krah DL, Crowell RL (1985) Properties of the deoxycholate-solubilized HeLa cell plasma membrane receptor for binding group B coxsackieviruses. J Virol 53:867–870PubMedGoogle Scholar
  37. Lindberg AM, Crowell RL, Zell R, Kandolf R, Pettersson U (1992) Mapping of the RD phenotype of the Nancy strain of coxsackievirus B3. Virus Res 24:187–196PubMedCrossRefGoogle Scholar
  38. Lonberg-Holm K, Crowell RL, Philipson L (1976) Unrelated animal viruses share receptors. Nature 259:679–681PubMedCrossRefGoogle Scholar
  39. Lublin DM, Atkinson JP (1989) Decay-accelerating factor: biochemistry, molecular biology, and function. Annu Rev Immunol 7:35–58PubMedCrossRefGoogle Scholar
  40. Lublin,DM, Coyne KE (1991) Phospholipid-anchored and transmembrane versions of either decay-accelerating factor or membrane cofactor protein show equal efficiency in protection from complementmediated cell damage. J Exp Med 174:35-14PubMedCrossRefGoogle Scholar
  41. Lublin DM, Krsek-Staples J, Pangburn MK, Atkinson JP (1986) Biosynthesis and glycosylation of the human complement regulatory protein decay-accelerating factor. J Immunol 137:1629–1635PubMedGoogle Scholar
  42. Mapoles JE, Krah DL, Crowell RL (1985) Purification of a HeLa cell receptor protein for group B coxsackieviruses. J Virol 55:560–566PubMedGoogle Scholar
  43. Medof ME, Lublin DM, Holers VM, Ayers DJ, Getty RR, Leykan JF, Atkinson JP, Tykocinski ML (1987) Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement. Proc Natl Acad Sci USA 84:2007–2011PubMedCrossRefGoogle Scholar
  44. Mendelsohn C, Johnson B, Lionetti KA, Nobis P, Wimmer E, Racaniello VR (1986) Transformation of a human poliovirus receptor gene into mouse cells. Proc Natl Acad Sci USA 83:7845–7849PubMedCrossRefGoogle Scholar
  45. Mohanty JG, Crowell RL (1993) Attempts to purify a second cellular receptor for a coxsackievirus B3 variant, CB3-RD from HeLa cells. Virus Res 29:305–320PubMedCrossRefGoogle Scholar
  46. Muckelbauer JK, Kremer M, Minor I, Rossmann MG, Diana G, Dutko FJ, Groarke J, Pevear DC (1995) The structure of coxsackievirus B3 at 3.5 A resolution. Structure 3:653–667PubMedCrossRefGoogle Scholar
  47. Naniche D, Varior-Krishnan G, Cervoni F, Wild TF, Rossi B, Rabourdin-Combe C, Gerlier D (1993) Human membrane cofactor protein (CD46) acts a cellular receptor for measles virus. J Virol 67:6025–6032PubMedGoogle Scholar
  48. Nicholson-Weller (1994) Structure and function of decay accelerating factor CD55. J Lab Clin Med 123:485–191Google Scholar
  49. Norman DG, Barlow PN, Baron M, Day AJ, Sim RB, Campbell ID (1991) Three-dimensional structure of a complement control protein module in solution. J Mol Biol 219:717–725PubMedCrossRefGoogle Scholar
  50. Philipson L, Lonberg-Holm K, Pettersson U (1968) Virus-receptor interaction in an adenovirus system. J Virol 2:1064–1075PubMedGoogle Scholar
  51. Racaniello VR (1992) Interaction of poliovirus with its cell receptor. Sem Virol 3:473–482Google Scholar
  52. Racaniello VR, Baltimore D (1981) Cloned poliovirus complementary DNA is infectious in mammalian cells. Science 214:916–919PubMedCrossRefGoogle Scholar
  53. Reagan KJ, Goldberg B, Crowell RL (1984) Altered receptor specificity of coxsackievirus B3 after growth in rhabdomyosarcoma cells. J Virol 49:635–640PubMedGoogle Scholar
  54. Roesing TG, Toselli PA, Crowell RL (1975) Elution and uncoating of coxsackievirus B3 by isolated HeLa cell plasma membranes. J Virol 15:654–667PubMedGoogle Scholar
  55. Roivainen M, Piirainen L, Hovi T, Virtanen I, Riikonen T, Heino J, Hyypia T (1994) Entry of coxsackievirus A9 into host cells: specific interactions with ανβξ integrin, the vitronectin receptor. Virology 203:357–365PubMedCrossRefGoogle Scholar
  56. Rossmann MG (1994) Viral cell recognition and entry. Prot Sci 3:1712–1725CrossRefGoogle Scholar
  57. Rossmann MG, Arnold E, Erickson JW, Frankenberger EA, Griffith JP, Hecht HJ, Johnson JE, Kamer G, Luo M, Mosser AG, Rueckert RR, Sherry B, Vriend G (1985) Structure of a human common cold virus and functional relationship to other picornaviruses. Nature 317:145–153PubMedCrossRefGoogle Scholar
  58. Semenkovich CF, Ostlund RE, Olson MO, Yang JW (1990) A protein partially expressed on the surface of HepG2 cells that binds lipoproteins specifically in nucleolin. Biochemistry 29:9708–9713PubMedCrossRefGoogle Scholar
  59. Shafren DR, Bates RC Agrez MV, Herd RL, Burns GF, Barry RD (1995) Coxsackieviruses Bl, B3, and B5 use decay accelerating factor as a receptor for cell attachment. J Virol 69:3873–3877PubMedGoogle Scholar
  60. Smith TJ (1992) MacInPlot Il-an updated program to display electron density and atomic models on the Macintosh personal computer. J Appl Cryst 26:496—498Google Scholar
  61. Srivastava M, Fleming P, Pillard HB, Burns AL (1989) Cloning and sequencing of the human nucleolin cDNA. FEBS Letters 250:99–105PubMedCrossRefGoogle Scholar
  62. Staunton ED, Merluzzi VJ, Rothlein R, Barton R, Marlin SD, Springer, TA (1989) A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell 56:849–853PubMedCrossRefGoogle Scholar
  63. Tomassini JE, Graham D, DeWitt CM, Lineberger DW, Rodkey JA, Colonno RJ (1989) cDNA cloning reveals that the major group rhinovirus receptor on HeLa cells is intercellular adhesion molecule 1. Proc Natl Acad Sci USA 86:4907–4911PubMedCrossRefGoogle Scholar
  64. Ward T, Pipkin PA, Clarkson NA, Stone DM, Minor PD, Almond JW (1994) Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method. EMBO J 13:5070–5074PubMedGoogle Scholar
  65. Wickham TJ, Mathias P, Cheresh DA, Nemerow GR (1993) Integrins avp3 and ocvP5 promote adenovirus internalization but not virus attachment. Cell 73:309–319PubMedCrossRefGoogle Scholar
  66. Zajac I, Crowell RL (1965a) Effect of enzymes on the interaction of enteroviruses with living HeLa cells. J Bacteriol 89:574–582PubMedGoogle Scholar
  67. Zajac I, Crowell RL (1965b) Location and regeneration of enterovirus receptors of HeLa cells. J Bacteriol 89:1097–1100PubMedGoogle Scholar
  68. Zajac I, Crowell RL (1969) Differential inhibition of attachment and eclipse activities of HeLa cells for enteroviruses. J Virol 3:422-28PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • R. J. Kuhn
    • 1
  1. 1.Department of Biological SciencesPurdue UniversityWest LafayetteUSA

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