Abstract
Animal viruses enter the host cell by attachment to a virus-specific host cell receptor followed by a chain of events that allows the particle to pass through the plasma membrane. This pathway may involve either the direct fusion of the viral envelope with the cytoplasmic membrane (paramyxoviruses) or internalization via endocytotic vesicles, called endosomes (togaviruses, myxoviruses, possibly also the picornaviruses). Available evidence suggests that the virion contained in the endosomes undergoes acid-induced structural rearrangements that lead to penetration (see ref. 1 for a review).
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References
White J, Kielian M, Helenius A (1983) Membrane fusion proteins of enveloped animal viruses. Rev Biophys 16:151–195.
Mandel B (1982) Interaction of viruses with neutralizing antibodies. In Fraenkel- Conrat, H, Wagner, RR (eds) Comprehensive Virology. Plenum Press, New York, pp 37–121.
Wimmer E, Jameson BA, Emini EA (1984) Poliovirus antigenic sites and vaccines. Nature 308:19.
Emini EA, Jameson BA, Wimmer E (1984) The identification of multiple neutralization antigenic sites on poliovirus type 1 and the priming of immune response with synthetic peptides. In Chanock R, Lerner R (eds) Modern Approaches to Vaccines. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp 65–75.
Fields BN (1984) Viral genes and tissue tropism. In Notkins AL, Oldstone MBA (eds) Concepts in Viral Pathogenesis. Springer-Verlag, New York, pp 102–108.
Diamond DC, Jameson BA, Bonin J, Kohara M, Abe S, Itoh H, Komatsu T, Arita M, Kuge S, Osterhaus ADME, Crainic R, Nomoto A, Wimmer E (1985) Antigenic variation and resistance to neutralization in poliovirus type 1. Science 229:1090–1093.
Lerner RA (1982) Tapping the immunological repertoire to produce antibodies at predetermined specificity. Nature 299:592–596.
Kitamura N, Semler BL, Rothberg PG, Larsen GR, Adler CJ, Dorner AJ, Emini EA, Hanecak R, Lee JJ, van der Werf S, Anderson CW, Wimmer E (1981) Pri-mary structure, gene organization and polypeptide expression of poliovirus RNA. Nature 291:547–553.
Rossman MG, Arnold E, Erichson JW, Frankenberger EA, Griffith JP, Hecht J-J, Johnson J, 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 317:145–153.
Hogle JM, Chow M, Filman DJ (1985) Three-dimensional structure of poliovirus at 2.9 angstrom resolution. Science 229:1358–1363.
Wild TF, Burroughs JN, Brown F (1969) Surface structure of foot-and-mouth disease virus. J Gen Virol 4:313–320.
Laporte J, Grosclaude J, Wantighem J, Bernard S, Rouze P (1973) Neutralisation en culture cellulaire du pouvoir infectieux du virus de la fièvre aphteuse pardés serums provenant de porcs immunisés à paidé d’une proteine virale purifiée. C R Séances Acad Sei [III] 276:3399–3401.
Rueckert RR (1976) On the structure and morphogenesis of picornaviruses. In Fraenkel-Conrat H, Wagner RR (eds) Comprehensive Virology, vol 6. Plenum Press, New York, pp 131–213.
Beatrice ST, Katze MG, Zajac BA, Crowell RL (1980) Induction of neutralizing antibodies by the coxsackie B3 virion polypeptide, VP2. Virology 104:426–438.
Blondel B, Crainic R, Horodniceanu F (1982) Le polypeptide structural VP1 du poliovirus type 1 induit des anticorps neutralisants. C R Séances Acad Sei 294:91–94.
Chow M, Baltimore D (1982) Isolated poliovirus capsid protein VP1 induces a neutralizing response in rats. Proc Natl Acad Sei USA 79:7518–7521.
van der Marel P, Hazendank TG, Henneeke MAC, van Wezel AL (1983) Induction of neutralizing antibodies by poliovirus capsid polypeptides VP1, VP2 and VP3. Vaccine 1:17–22.
Dernick R, Heukeshoven Y, Hilbrig M (1983) Induction of neutralizing antibodies by the three structural poliovirus polypeptides. Virology 130:243–246.
Emini EA, Dorner AJ, Dorner LF, Jameson BA, Wimmer E (1983) Identification of a poliovirus neutralization epitope through use of neutralizing anti-serum raised against a purified viral structural protein. Virology 124:144–151.
Emini EA, Jameson BA, Wimmer E (1985) Antigenic structure of poliovirus. In Neurath AR, van Regenmortel MHV (eds) Immunochemistry of Viruses—the Basis of Serodiagnosis and Vaccines. Elsevier Biomedical Press, Holland, pp. 281–294.
Blondel B, Akacem O, Crainic R, Corillin P, Horodniceanu F (1983) Detection by monoclonal antibodies of an antigenic determinant critical for poliovirus neutralization present on VP1 and on heat-inactivated virions. Virology 126:707–710.
Kupper H, Keller W, Kurz C, Forss S, Schaller H, Franze R, Strohmaier K, Marquardt O, Zaslasky VG, Hofschneider PH (1981) Cloning of cDNA of major antigen of foot and mouth disease virus and expression in E. coli. Nature 289:555–559.
Kleid DG, Yansura D, Small B, Doubenko D, Moore DM, Grubman MJ, McKercher PD, Morgan DO, Robertson BH, Bachrach HL (1981) Cloned viral protein vaccine for foot-and-mouth disease: Responses in cattle and swine. Science 214:1125–1129.
Boothroyd JC, Highfield PE, Cross GAM, Rowlands DJ, Lowe PA, Brown F, Harris TJR (1981) Molecular cloning of foot and mouth disease virus genome and nucleotide sequences in the structural protein genes. Nature 290:800–802.
Strohmaier K, Franze R, Adam KH (1982) Location and characterization of the antigenic portion of the FMDV immunizing protein. J Gen Virol 59:295–306.
Kurz C, Forss S, Kupper H, Strohmaier K, Schaller H (1981) Nucleotide sequence and corresponding amino acid sequence of the gene for the major antigen of foot and mouth disease virus. Nucleic Acids Res 9:1919–1930.
Boothroyd JC, Harris TJR, Rowland DJ, Lowe PA (1982) The nucleotide sequence of cDNA coding for the structural proteins of foot-and-mouth disease virus. Gene 17:153–161.
Weddel GN, Yansura DG, Doubenko DJ, Hartlin ME, Grubman MJ, Moore DM, Kleid DG (1985) Sequence variation in the gene for the immunogenic capsid protein VP1 of foot-and-mouth disease virus type A. Proc Natl Acad Sci USA 82:2618–2622.
Bittle JL, Houghten RA, Alexander H, Shinnick TM, Suteliffe YG, Lerner RA, Rowlands DJ, Brown F (1982) Protection against foot-and-mouth disease by immunization with a chemically synthesized peptide predicted from the viral nucleotide sequence. Nature 298:30–33.
Pfaff E, Mussgay M, Bohm HO, Schulz GE, Schaller H (1982) Antibodies against a preselected peptide recognize and neutralize foot-and-mouth disease virus. EMBO J 1:869–874.
Rowlands DJ, Clarke BE, Carroll AR, Brown F, Nicholson BH, Bittle JL, Houghten RA, Lerner RA (1983) The chemical basis for variation in the major antigenic site eliciting neutralizing antibodies in foot-and-mouth disease. Nature 306:694–697.
Emini EA, Jameson BA, Lewis AJ, Larsen GR, Wimmer E (1982) Poliovirus neutralization epitopes: Analysis and localization with neutralizing monoclonal antibodies. J Virol 43:997–1005.
Toyoda H, Kohara M, Kataoka Y, Suganuma T, Omata T, Imura N, Nomoto A (1984) The complete nucleotide sequence of all three poliovirus serotype genomes (Sabin): Implication for the genetic relationship, gene function and antigenic determinants. J Mol Biol 174:561–585.
Emini EA, Jameson BA, Wimmer E (1983) Priming for and induction of anti-poliovirus neutralizing antibodies by synthetic peptides. Nature 304:699–703.
Crainic R, Coullin P, Blondel B, Caban N, Bone A, Horodniceanu F (1983) Natural variation of poliovirus neutralization epitopes. Infect Immun 41:1217–1225.
Emini EA, Kao S-Y, Lewis AJ, Crainie R, Wimmer E (1983) The functional basis of polio virus neutralization determined with monospecific neutralizing antibodies. J Virol 46:466–474.
Minor PD, Schild GC, Bootman J, Evans DMA, Ferguson M, Reeve P, Spitz M, Stan way G, Cann AJ, Hauptmann R, Clarke LD, Mountford RC, Almond JW (1983) Location and primary structure of the antigenic site for poliovirus neutralization. Nature 301:674–679.
Wychowski C, van der Werf S, Siffert O, Crainie R, Bruneau P, Girard M (1983) A poliovirus type 1 neutralization epitope is located within amino acid residues 93 to 104 of viral capsid polypeptide VP1. EMBO J 2:2019–2024.
van der Werf S, Wychowski C, Bruneau P, Blondel B, Crainie R, Horadniceanu F, Girard M (1983) Localization of a poliovirus type 1 neutralization epitope in a viral capsid polypeptide VP1. Proc Natl Acad Sei USA 80:5080–5084.
Evans DMA, Minor PD, Schild, GS Almond JW (1983) Critical rate of an eight- amino acid sequence of VP1 in neutralization of poliovirus type 3. Nature 304:452–462.
Crainie R, Blondel B, Horaud F (1984) Antigenic variation of poliovirus studied by means of monoclonal antibodies. Rev Infect Dis 6:S535–S539.
van der Werf S (1984) Clonage moleculaire du poliovirus type 1 et expression de ses proteines de capside chez Escherichia coli: Identification d’un epitode de neutralization. Thèse De Doctorat, D’Etat Universität, Paris 7.
Enger-Valk BE, Jore J, Pouwels PH, van der Marel P, van Wezel TL (1984) Expression in Escherichi coli of capsid protein VP1 of poliovirus type 1. In Chanock RM, Lerner RA (eds) Modem Approaches to Vaccines. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp 173–178.
Blondel B, Crainie R, Fichot O, Onfraise G, Candrea A, Diamond D, Girard M, Horaud F (1986) Mutations conferring resistance of neutralization with monoclonal antibodies in type 1 poliovirus can be located outside or inside the antibody- binding site. J Virol 57:81–90.
Ferguson M, Evans DMA, Magrath DI, Minor PD, Almond JW, Schild GC (1985) Introduction by synthetic peptides of broadly reactive, type-specific neutralizing antibody to poliovirus type 3. Virology 143:505–515.
Emini EA, Jameson BA, Wimmer E (1984) Peptide induction of poliovirus neutralizing antibodies: Identification of a new antigenic site on coat protein VP2. J Virol 52:719–721.
Chow M, Yabrov R, Bittle J, Hogle J, Baltimore D (1985) Synthetic peptides from four separate regions of the poliovirus type 1 capsid protein VP1 induce neutralizing antibodies. Proc Natl Acad Sei USA 82:910–914.
Francis MJ, Fry CM, Rowlands DJ, Brown F, Bittle JL, Hough ten RA, Lerner RA (1985) Priming with peptides of foot-and-mouth disease virus. In Lerner RA, Chanock RM, Brown F (eds) Vaccines 49. Cold Spring Harbor Press, New York, pp 203–210.
Robinson IK, Harrison SC (1982) Structure of the expanded state of tomato bushy stunt virus. Nature 297:563–568.
Hughes JV, Stanton LW, Tomassini JE, Long WJ, Scolnick EM (1984) Neutralizing monoclonal antibodies to hepatitis A virus: Partial localization of a neutralizing antigenic site. J Virol 52:465–473.
Emini EA, Hughes JV, Perlow DS, Boger J (1985) Induction of hepatitis A virus- neutralizing antibody by a virus-specific synthetic peptide. J Virol 55:836–839.
Sherry B, Rueckert RR (1985) Evidence for at least two dominant neutralization antigens on human rhinovirus 14. J Virol 53:137–143.
Sherry B, Mosser AG, Colonno RJ, Rueckert RR (1986) Use of monoclonal antibodies to identify four neutralization immunogens on a common cold Picornavirus, human rhinovirus 14. J Virol 57:246–257.
Jameson BA, Bonin J, Wimmer E, Kew OM (1986) Natural variants of the Sabin type 1 vaccine strain of poliovirus and correlation with a poliovirus neutralization site. Virology 143:337–341.
Crowell RL, Landau BJ (1983) Receptors in the initiation of Picornavirus infections. In Fraenkel-Conrat H, Wagner RR (eds) Comprehensive Virology. Plenum Press, New York, pp 1–42.
Argos P, Kamer G, Nickiin MJH, Wimmer E (1984) Similarity in gene organization and homology between proteins at animal picornaviruses and a plant comovirus suggest common ancestry of these virus families. Nuceic Acids Res 12:7251–7276.
Cherry JD, Donald MD, Nelson DB (1966) Enterovirus infections: Their epidemiology and pathogenesis. Clin Pediatr 5:659–664.
Brown F, Wild F (1974) Variation in the coxsackievirus type B5 and its possible role in the etiology of swine vesicular disease. Intervirol 3:125–128.
Icenogle J, Shiwen H, Duke G, Gilbert S, Rueckert R, Anderegg J (1983) Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry. Virology 127:412–425.
Emini EA, Ostapchuk P, Wimmer E (1983) Bivalent attachment of antibody onto poliovirus leads to conformational alteration and neutralization. J Virol 48:547–550.
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Wimmer, E., Emini, E.A., Diamond, D.C. (1986). Mapping Neutralization Domains of Viruses. In: Notkins, A.L., Oldstone, M.B.A. (eds) Concepts in Viral Pathogenesis II. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4958-0_19
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DOI: https://doi.org/10.1007/978-1-4612-4958-0_19
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