Abstract
Human rhinoviruses (HRVs), members of the Picornaviridae, are the major causative agents of one of the more elusive diseases known to man, namely the common cold (Gwaltney, 1982). To date, there are 102 recognized serotypes that have been isolated and shown to be antigenically distinct (Hamparian et al., 1987). HRVs are non-enveloped viruses that contain four non-glycosylated structural proteins, designated VP1, VP2, VP3, and VP4, which form a protein capsid with icosahedral symmetry. Within the viral capsid lies a single-stranded genome RNA which serves as a monocistronic mRNA for the synthesis of the 4 structural and 7 nonstructural proteins of the virus. Upon entry into a cell, the RNA genome is translated into a large polyprotein which is subsequently cleaved by two viral proteases encoded within the polyprotein (Palmenberg, 1987). The genome RNA of picornaviruses contains all the information needed to initiate a viral infection since transfection of cells with the genome RNA alone will result in the production of infectious progeny virus (Mizutani et al., 1985).
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References
Abraham, G., and Colonno, R.J., 1983, Many rhinovirus serotypes share the same cellular receptor, J. Virol. 51:340–345.
Abraham, G., and Colonno, R.J., 1988, Characterization of human rhinoviruses displaced by an anti-receptor monoclonal antibody, J Virol. 62:2300–2306.
Chow, M., et al., 1987, Myristylation of Picornavirus capsid protein VP4 and its structural significance, Nature (London) 327:482–486.
Colonno, R.J., 1987, Cell surface receptors for picornaviruses, BioEssays 5:270–274.
Colonno, R.J., Callahan, P.L., and Long, W.J., 1986, Isolation of a monoclonal antibody that blocks attachment of the major group of human rhinoviruses, J Virol. 57:7–12.
Colonno, R.J., Tomassini, J.E., and Callahan, P.L., 1987, Isolation and characterization of a monoclonal antibody which blocks attachment of human rhinovirus, In: Positive Strand RNA Viruses (Eds. M.A. Brinton and R. Rueckert) Vol 54:93–102.
Colonno, R.J., et al., 1988, Evidence for the direct involvement of the rhinovirus canyon in receptor binding, Proc. Natl. Acad. Sci USA 85:5449–5453.
Colonno, R.J., et al., 1990, The major-group rhinoviruses utilize the intercellular adhesion molecule 1 ligand as a cellular receptor during infection, In: New Aspects of Positive-Strand RNA Viruses (Eds. M.A. Brinton & F.X. Heinz) 257–261.
Dustin, M.L., Staunton, D.W., and Springer, T.A., 1988, Supergene families meet in the immune system, Immunol Today 9:213–215.
Giranda, V.L., Chapman, M.S., and Rossmann, M.G., 1990, Modeling of the human intercellular adhesion molecule-1, the human rhinovirus major group receptor, In: Proteins: Structure, Function, and Genetics 7:227–233.
Greve, J.M., et al., 1989, The major human rhinovirus receptor is ICAM-1, Cell 56:839–847.
Gwaltney, J.M., Jr., 1982, Rhinoviruses, In: Viral Infection of Man: Epidemiology and Control (ed. E.A. Evans) 491–517.
Hamparian, V.V., et al., 1987, A collaborative report: rhinoviruses-extension of the numbering system from 89 to 100, Virol. 159:191–192.
Hayden, F.G., Gwaltney, Jr., J.M., and Colonno, R J., 1988, Modification of experimental rhinovirus colds by receptor blockade, Antiviral Res. 9:233–247.
Jameson, B.A., et al., 1988, Location and chemical synthesis of a binding site for HIV-1 on the CD4 protein, Science 240:1335–1339.
Kaplan, G., Freistadt, M.S., and Racaniello, V.R., 1990, Neutralization of poliovirus by cell receptors expressed in insect cells, J. Virol. 64:4697–4702.
Kim, S., et al., 1989, Crystal structure of human rhinovirus serotype 1A (HRV1A), J Mol Biol 210:91–111.
Landau, N.R., Warton, M., and Littman, D.R., 1988, The envelope glycoprotein of the human immunodeficiency virus binds to the immunoglobulin-like domain of CDA, Nature 334:159–162.
Lineberger, D.W., et al., 1990, Antibodies that block rhinovirus attachment map to domain 1 of the major group receptor, J. Virol. 64: 2582–2587.
Makgoba, M.W., et al., 1988, Functional evidence that intercellular adhesion molecule-1 (ICAM-1) is a ligand for LFA-1 dependent adhesion in T cell-mediated cytotoxicity, Eur. J. Immunol. 18:637–640.
Mendelsohn, C.L., Wimmer, E., and Racaniello, V., 1989, Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily, Cell 56:855–865.
Mischak, H.C., et al., 1988, Detection of the human rhinovirus minor group receptor on renaturing Western blots, J. Gen. Virol. 69:2653–2656.
Mizutani, S., and Colonno, R.J., 1985, In vitro synthesis of an infectious RNA from cDNA clones of human rhinovirus type 14, J. Virol 56:628–632.
Naclerio, R.M., et al, 1988, Kinins are generated during experimental rhinovirus colds, J Infect. Dis. 157:133–142.
Palmenberg, A.C., 1987, Picornaviral processing: some new ideas, J Cell. Biochem. 33:191–198.
Peterson, A., and Seed, B. 1988, Genetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4, Cell 54:65–72.
Prevear, D.C., et al, 1989, Conformational change in the floor of the human rhinovirus canyon blocks adsorption to HeLa cell receptors, J Virol. 63:2002–2007.
Rossmann, M.G., et al, 1985, Structure of a human common cold virus and functional relationship to other picornaviruses, Nature 317:145–153.
Sherry, B., et al, 1986, Use of monoclonal antibodies to identify four neutralization immunogens on a common cold Picornavirus, human rhinovirus 14, J Virol. 57:246–257.
Simmons, D., Makgoba, M.W., and Seed, B., 1988, ICAM, an adhesion ligand of LFA-1, is homologous to the neural cell adhesion molecule NCAM, Nature 331:624–627.
Staunton, D.E., et al., 1988, Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families, Cell 52:925–933.
Staunton, D.E., et al., 1989, A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses, Cell 56:849–853.
Staunton, D.E., et al, 1990, The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus, Cell, 61:243–254.
Tomassini, J.E., and Colonno, RJ., 1986, Isolation of a receptor protein involved in attachment of human rhinoviruses, J Virol. 58:290–295.
Tomassini, J.E., Maxson, T.R., and Colonno, R.J., 1989b, Biochemical characterization of a glycoprotein required for rhinovirus attachment, J Biol Chem. 264:1656–1662.
Tomassini, J.E., et al, 1989a, cDNA cloning reveals that the major group rhinovirus receptor on HeLa cells is intercellular adhesion molecule 1, Proc. Natl. Acad. Sci USA 86:4907–4911.
Uncapher, C.R., DeWitt, C.M., and Colonno, R.J., 1991, The major and minor group receptor families contain all but one human rhinovirus serotype, Virol, in press.
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© 1992 Springer-Verlag New York, Inc.
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Colonno, R.J. (1992). Molecular Interactions between Human Rhinoviruses and the Adhesion Receptor ICAM-1. In: Hook, M., Switalski, L. (eds) Microbial Adhesion and Invasion. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2924-7_3
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DOI: https://doi.org/10.1007/978-1-4612-2924-7_3
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