Picornavirus Inhibition of Host Cell Protein Synthesis

  • Ellie Ehrenfeld
Part of the Comprehensive Virology book series (COVI, volume 19)

Abstract

Infection of cultured cells with many lytic viruses results in a marked decrease in the rate of cellular protein synthesis. Usually, this decrease is accompanied by increasing rates of viral protein synthesis, marked cytopathic effects, and ultimately cell death. In most cases, it is not known whether the “shut-off” of host cell protein synthesis results from an active process induced by the virus evolved for that (or some other) purpose, or whether it is merely a passive result of another viral function, such as production of large quantities of viral mRNA which compete effectively with their cellular counterparts. In the case of poliovirus, however, three types of studies suggested that the former, active type of mechanism was at work. Kinetic analysis of the rate of protein synthesis in cells synchronously infected with high multiplicities of virus showed that cellular protein synthesis could be virtually completely inhibited prior to the synthesis of significant quantities of viral RNA and protein (Summers et al., 1965). In addition, infection in the presence of 1–3 mM guanidine, which prevents detectable replication of viral RNA, nevertheless results in viral inhibition of host cell protein synthesis (Holland, 1964; Bablanian et al., 1965, Penman and Summers, 1965). Last, infection with a temperature-sensitive mutant of poliovirus that synthesizes no single-stranded RNA at restrictive temperature nevertheless induces normal inhibition of cellular protein synthesis (Hewlett et al., 1982). All of these results argue against a competition between cellular and viral mRNAs for cellular components as an explanation for the selective inhibition of cellular protein synthesis. A large body of experimental work on this subject has been performed with poliovirusinfected cells, and consequently, the major focus of this review is on the inhibiton of protein synthesis by poliovirus.

Keywords

Permeability Hepatitis Codon Sedimentation Fractionation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Abreu, S. L., and Lucas-Lenard, J., 1976, Cellular protein synthesis shut-off by mengovirus: Translation of nonviral and viral mRNAs in extracts from uninfected and infected Ehrlich ascites tumor cells, J. Virol. 18:182.PubMedGoogle Scholar
  2. Alonso, M. A., and Carrasco, L., 1981, Reversion by hypotonic medium of the shutoff of protein synthesis induced by encephalomyocarditis virus, J. Virol. 37:535.PubMedGoogle Scholar
  3. Bablanian, R., 1972, Depression of macromolecular synthesis in cells infected with guanidine-dependent poliovirus under restrictive conditions, Virology 47:255.PubMedCrossRefGoogle Scholar
  4. Bablanian, R., and Russell, W C., 1974, Adenovirus polypeptide synthesis in the presence of non-replicating poliovirus, J. Gen. Virol. 24:261.PubMedCrossRefGoogle Scholar
  5. Bablanian, R., Eggers, H. J., and Tamm, I., 1965, Studies on the mechanism of poliovirus-induced cell damage. I. The relation between poliovirus-induced metabolic and morphologic alterations in cultured cells, Virology 26:100.PubMedCrossRefGoogle Scholar
  6. Baglioni, C., Simili, M., and Shafritz, D. A., 1978, Initiation activity of EMC virus RNA, binding to initiation factor eIF-4B and shut-off of host cell protein synthesis, Nature 275:240.PubMedCrossRefGoogle Scholar
  7. Banerjee, A. K., 1980, 5′-Terminal cap structure in eukaryotic messenger ribonucleic acids, Microbiol. Rev. 44:175.PubMedGoogle Scholar
  8. Benne, R., and Hershey, J. W. B., 1978, The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes, J. Biol. Chem. 253:3078.PubMedGoogle Scholar
  9. Borgert, K., Koschel, K., Tauber, H., and Wecker, E., 1971, Effect of hydroxylamine on early functions of poliovirus, J. Virol. 8:1.PubMedGoogle Scholar
  10. Bossart, W., and Bienz, R., 1981, Regulation of protein synthesis in Hep-2 cells and their cytoplasmic extracts after poliovirus infection, Virology 111:555.PubMedCrossRefGoogle Scholar
  11. Brown, B., and Ehrenfeld, E., 1980, Initiation factor preparations from poliovirusinfected cells restrict translation in reticulocyte lysates, Virology 103:327.PubMedCrossRefGoogle Scholar
  12. Brown, D., Hansen, J., and Ehrenfeld, E., 1980, Specificity of initiation factor preparations from poliovirus-infected cells, J. Virol. 34:573.PubMedGoogle Scholar
  13. Brown, D., Jones, C. L., Brown, B. A., and Ehrenfeld, E., 1982, Translation of capped and uncapped VSV mRNAs in the presence of initiation factors from poliovirus-infected cells, Virology 123:60.PubMedCrossRefGoogle Scholar
  14. Carrasco, L., 1977, The inhibition of cell functions after viral infection. A proposed general mechanism, FEBS Lett. 76:11.CrossRefGoogle Scholar
  15. Carrasco, L., and Smith, A. E., 1976, Sodium ions and the shut-off of host cell protein synthesis by picornaviruses, Nature 264:807.PubMedCrossRefGoogle Scholar
  16. Celma, M. L., and Ehrenfeld, E., 1974, Effect of poliovirus double-stranded RNA on viral and host-cell protein synthesis, Proc. Natl. Acad. Sci. USA 71:2440.PubMedCrossRefGoogle Scholar
  17. Choppin, P. W., and Holmes, R. V., 1967, Replication of SV5 RNA and the effects of superinfection with poliovirus, Virology 33:442.PubMedCrossRefGoogle Scholar
  18. Cole, C., and Baltimore, D., 1973, Defective interfering particles of poliovirus II. Nature of the defect, J. Mol. Biol. 76:325.PubMedCrossRefGoogle Scholar
  19. Cords, C. E., and Holland, J. J., 1964, Interference between enteroviruses and conditions effecting its reversal, Virology 22:226.PubMedCrossRefGoogle Scholar
  20. Detjen, B. M., Jen, G., and Thach, R. E., 1981, Encephalomyocarditis viral RNA can be translated under conditions of polio-induced translation shut-off in vivo, J. Virol. 38:777.Google Scholar
  21. Detjen, B. M., Waiden, W. E., and Thach, R. E., 1982, Translational specificity in reovirus-infected mouse fibroblasts, J. Biol. Chem. 257:9855.PubMedGoogle Scholar
  22. Doyle, S., and Holland, J., 1972, Virus-induced interference in heterologously infected HeLa cells, J. Virol. 9:22.PubMedGoogle Scholar
  23. Duncan, R., Etchison, D., and Hershey, J. W. B., 1983, Protein synthesis eukaryotic initiation factors 4A and 4B are not altered by poliovirus infection of HeLa cells, J. Biol. Chem. 258:7236.PubMedGoogle Scholar
  24. Edery, I., Humbelin, M., Darveau, A., Lee, K., Milburn, S., Hershey, J., Trachsel, H., and Sonenberg, N., 1983, Involvement of eukaryotic initiation factor 4A in the cap recognition process, J. Biol. Chem. 258:11398.PubMedGoogle Scholar
  25. Egberts, E., Hackett, P., and Traub, P., 1977, Alteration of the intracellular energetic and ionic conditions by mengovirus infection of Ehrlich ascites tumor cells and its influence on protein synthesis in the midphase of infection, J. Virol. 22:591.PubMedGoogle Scholar
  26. Ehrenfeld, E., 1982, Poliovirus-induced inhibition of host cell protein synthesis, Cell 28:435.PubMedCrossRefGoogle Scholar
  27. Ehrenfeld, E., and Hunt, T., 1971, Double-stranded poliovirus RNA inhibits initiation of protein synthesis by reticulocyte lysates, Proc. Natl. Acad. Sci. USA 68:1075.PubMedCrossRefGoogle Scholar
  28. Ehrenfeld, E., and Lund, H., 1977, Untranslated vesicular stomatitis virus messenger RNA after poliovirus infection, Virology 80:297.PubMedCrossRefGoogle Scholar
  29. Ehrenfeld, E., and Manis, S., 1979, Inhibition of 80S initiation complex formation by infection with poliovirus, J. Gen. Virol. 43:441.PubMedCrossRefGoogle Scholar
  30. Etchison, D., Milburn, S. C., Edery, I., Sonenberg, N., and Hershey, J. W. B., 1982, Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000 dalton polypeptide associated with eukaryotic initiation factor 3 and a cap binding protein complex, J. Biol. Chem. 257:14806.PubMedGoogle Scholar
  31. Etchison, D., Edery, I., Sonenberg, N., Hansen, J., Ehrenfeld, E., Milburn, S., and Hershey, J. W. B., Poliovirus infection of HeLa cells inhibits the activity of a cap binding protein complex in the translation of globin messenger RNA, submitted.Google Scholar
  32. Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., and Trachsel, H., 1977, Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis, Cell 11:187.PubMedCrossRefGoogle Scholar
  33. Fernandez-Munoz, R., and Darnell, J. E., 1976, Structural difference between the 5′ termini of viral and cellular mRNA in poliovirus-infected cells: Possible basis for the inhibition of host protein synthesis, J. Virol. 18:719.PubMedGoogle Scholar
  34. Golini, F., Thach, S. S., Birge, C. H., Safer, B., Merrick, W. C., and Thach, R. E., 1976, Competition between cellular and viral mRNAs in vitro is regulated by a messenger discriminatory initiation factor, Proc. Natl. Acad. Sci. USA 73:3040.PubMedCrossRefGoogle Scholar
  35. Grifo, J. A., Tahara, S. M., Leis, J. P., Morgan, M. A., Shatkin, A. J., and Merrick, W., 1982, Characterization of eukaryotic initiation factor 4A, a protein involved in ATP-dependent binding of globin mRNA, J. Biol. Chem. 257:5246.PubMedGoogle Scholar
  36. Grifo, J. A., Tahara, S. M., Morgan, M. A., Shatkin, A. J., and Merrick, W. C., 1983, New initiation factor activity required for globin mRNA translation, J. Biol. Chem. 258:5804.PubMedGoogle Scholar
  37. Hackett, P. B., Egberts, E., and Traub, P., 1978a, Translation of ascites and mengovirus RNA in fractionated cell-free systems from uninfected and mengovirusinfected Ehrlich ascites tumor cells, Eur. J. Biochem. 83:341.PubMedCrossRefGoogle Scholar
  38. Hackett, P. B., Egberts, E., and Traub, P., 1978b, Selective translation of mengovirus RNA over host mRNA in homologous, fractionated, cell-free translational systems from Ehrlich ascites tumor cells, Eur. J. Biochem. 83:353.PubMedCrossRefGoogle Scholar
  39. Hansen, J. L., and Ehrenfeld, E., 1981, Presence of the cap-binding protein in initiation factor preparations from poliovirus-infected HeLa cells, J. Virol. 38:438.PubMedGoogle Scholar
  40. Hansen, J. L., Etchison, D., Hershey, J. W. B., and Ehrenfeld, E., 1982a, Association of cap-binding protein with eIF-3 in initiation factor preparations from uninfected and poliovirus-infected cells, J. Virol. 42:200.PubMedGoogle Scholar
  41. Hansen, J. L., Etchison, D. O., Hershey, J. W. B., and Ehrenfeld, E., 1982b, Localization of cap-binding protein in subcellular fractions of HeLa cells, Mol. Cell. Biol. 2:1639.PubMedGoogle Scholar
  42. Helentjaris, T., and Ehrenfeld, E., 1977, Inhibition of host cell protein synthesis by UV-inactivated poliovirus, J. Virol. 21:259.PubMedGoogle Scholar
  43. Helentjaris, T., and Ehrenfeld, E., 1978, Control of protein synthesis in extracts from poliovirus-infected cells I. mRNA discrimination by crude initiation factors, J. Virol. 26:510.PubMedGoogle Scholar
  44. Helentjaris, T., Ehrenfeld, E., Brown-Luedi, M. L., and Hershey, J. W. B., 1979, Alterations in initiation factor activity from poliovirus-infected HeLa cells, J. Biol. Chem. 254:10973.PubMedGoogle Scholar
  45. Hellman, G. M., Chu, L-Y., and Rhoades, R. E., 1982, A polypeptide which reverses cap analogue inhibition of cell-free protein synthesis, J. Biol. Chem. 257:4056.Google Scholar
  46. Hewlett, M. J., Rose, J. K., and Baltimore, D., 1976, 5′ Terminal structure of poliovirus polyribosomal RNA is pUp, Proc. Natl. Acad. Sci. USA 73:327.PubMedCrossRefGoogle Scholar
  47. Hewlett, M. J., Axelrod, J. H., Antorino, N., and Field, R., 1982, Isolation and preliminary characterization of temperature-sensitive mutants of poliovirus type 1, J. Virol. 41:1089.PubMedGoogle Scholar
  48. Holland, J. J., 1964, Inhibition of host cell macromolecular synthesis by high multiplicities of poliovirus under conditions preventing virus synthesis, J. Mol. Biol. 8:574.PubMedCrossRefGoogle Scholar
  49. Holland, J. J., and Peterson, J. A., 1964, Nucleic acid and protein synthesis during poliovirus infection of human cells, J. Mol. Biol. 8:556.PubMedCrossRefGoogle Scholar
  50. Hunt, T., and Ehrenfeld, E., 1971, Cytoplasmic from poliovirus-infected HeLa cells inhibits cell-free haemoglobin synthesis, Nature New Biol. 230:91.PubMedCrossRefGoogle Scholar
  51. Ito, Y., Okazaki, H., and Ishida, N., 1968, Growth inhibition of Newcastle Disease virus upon superinfection of poliovirus in the presence of guanidine, J. Virol. 2:645.PubMedGoogle Scholar
  52. Jackson, R. J., 1982, The Control of initiation of protein synthesis in reticulocyte lysates, in: Protein Biosynthesis in Eukaryotes (R. Perez-Bercoff, ed.), pp. 362–418, Plenum Press, New York.Google Scholar
  53. Jagus, R., Anderson, W. F., and Safer, B., 1981, The regulation of initiation of mammalian protein synthesis, in: Progress in Nucleic Acid Research and Molecular Biology, Vol. 25, (W. E. Cohn, and E. Volkin, eds.), pp. 127–185, Academic Press, New York.Google Scholar
  54. James, L. A., and Tershak, D. R., 1981, Protein phosphorylations in poliovirusinfected cells, Can. J. Microbiol. 27:28.PubMedCrossRefGoogle Scholar
  55. Jen, G., and Thach, R. E., 1982, Inhibition of host translation in encephalomyocarditis virus-infected L cells: A novel mechanism, J. Virol. 43:250.PubMedGoogle Scholar
  56. Jen, G., Birge, C. H., and Thach, R. E., 1978, Comparison of initiation rates of encephalomyocarditis virus and host protein synthesis in infected cells, J. Virol. 27:640.PubMedGoogle Scholar
  57. Jen, G., Detjen, B. M., and Thach, R. E., 1980, Shut-off of HeLa cell protein synthesis by encephalomyocarditis virus and poliovirus: A comparative study, J. Virol. 35:150.PubMedGoogle Scholar
  58. Jones, C., and Ehrenfeld, E., 1983, The effect of poliovirus infection on the translation in vitro of VSV messenger ribonucleoprotein particles, Virology 129:415.PubMedCrossRefGoogle Scholar
  59. Kaempfer, R., 1984, Regulation of eukaryotic translation, in: Comprehensive Virology, Vol. 19, (H. Fraenkel-Conrat and R. E. Wagner, eds.), Plenum Press, New York.Google Scholar
  60. Kaufmann, Y., Goldstein, E., and Penman, S., 1976, Poliovirus-induced inhibition of polypeptide initiation in vitro on native polyribosomes, Proc. Natl. Acad. Sci. USA 73:1834.PubMedCrossRefGoogle Scholar
  61. Koschel, K., 1974, Poliovirus infection and poly (A) sequences of cytoplasmic cellular RNA, J. Virol. 13:1061.PubMedGoogle Scholar
  62. Kozak, M., 1980b, Influence of mRNA secondary structure on binding and migration of 40S ribosomal subunits, Cell 19:79.PubMedCrossRefGoogle Scholar
  63. Kozak, M., 1980b, Role of ATP in binding and migration of 40S ribosomal subunits, Cell 22:459.PubMedCrossRefGoogle Scholar
  64. Lacal, J. C., and Carrasco, L., 1982, Relationship between membrane integrity and the inhibition of host translation in virus-infected mammalian cells, Eur. J. Biochem. 127:359.PubMedCrossRefGoogle Scholar
  65. Lacal, J. C., and Carrasco, L., 1983, Modification of membrane permeability in poliovirus-infected HeLa cells: Effect of guanidine, J. Gen. Virol. 64:787.PubMedCrossRefGoogle Scholar
  66. LaColla, P., Marcialis, M. A., Mereu, G. P., and Loddo, B., 1972, Specific inhibition of poliovirus-induced blockade of cell protein synthesis by a thiopyrimidine derivative, J. Gen. Virol. 17:13.CrossRefGoogle Scholar
  67. Lawrence, C., and Thach, R. E., 1974, Encephalomyocarditis virus infection of mouse plasmacytoma cells. I. Inhibition of cellular protein synthesis, J. Virol. 14:598.PubMedGoogle Scholar
  68. Lee, K. A. W., and Sonenberg, N., 1982, Inactivation of cap-binding protein accompanies the shut-off of host protein synthesis by poliovirus, Proc. Natl. Acad. Sci. USA 79:3447.PubMedCrossRefGoogle Scholar
  69. Lee, L. A. W., Guertin, D., and Sonenberg, N., 1983, mRNA secondary structure as a determinant in cap recognition and initiation complex formation, J. Biol. Chem. 258:707.PubMedGoogle Scholar
  70. Leibowitz, R., and Penman, S., 1971, Regulation of protein synthesis in HeLa cells. III. Inhibition during poliovirus infection, J. Virol. 8:661.PubMedGoogle Scholar
  71. Lodish, H. F., 1974, Model for the regulation of mRNA translation applied to haemoglobin synthesis, Nature 251:385.PubMedCrossRefGoogle Scholar
  72. McCormick, W., and Penman, S., 1968, Replication of mengovirus in HeLa cells preinfected with non-replicating poliovirus, J. Virol. 2:859.PubMedGoogle Scholar
  73. Merryman, P., Jaffe, I., and Ehrenfeld, E., 1974, Effect of D-penicillamine on poliovirus replication in HeLa cells, J. Virol. 13:881.PubMedGoogle Scholar
  74. Morgan, M. A., and Shatkin, A. J., 1980, Initiation of reovirus transcription by inosine 5′-triphosphate and properties of 7-methyl inosine-capped, inosine-substituted messenger RNA, Biochemistry 19:5960.PubMedCrossRefGoogle Scholar
  75. Nair, C., 1981, Monovalent cation metabolism and cytopathic effects of poliovirusinfected HeLa cells, J. Virol. 37:268.PubMedGoogle Scholar
  76. Nair, C. N., Stowers, J. W., and Singfield, B., 1979, Guanidine-sensitive Na+ accumulation by poliovirus-infected HeLa cells, J. Virol. 31:184.PubMedGoogle Scholar
  77. Noble, J., and Levintow, L., 1970, Dynamics of poliovirus-specific RNA synthesis and the effects of inhibitors of virus replication, Virology 40:634.PubMedCrossRefGoogle Scholar
  78. Nomoto, A., Lee, Y. F., and Wimmer, E., 1976, The 5′ end of poliovirus mRNA is not capped with m7G(5′)ppp(5′)Np, Proc. Natl. Acad. Sci. USA 73:375.PubMedCrossRefGoogle Scholar
  79. Nuss, D. L., Oppermann, H., and Koch, G., 1975, Selective blockage of initiation of host protein synthesis in RNA virus-infected cells, Proc. Natl. Acad. Sci. USA 72:1258.PubMedCrossRefGoogle Scholar
  80. Otto, M. J., and Lucas-Lenard, J., 1980, The influence of the host cell on the inhibition of viral protein synthesis in cells doubly-infected with vesicular stomatitis virus and mengovirus, J. Gen. Virol. 50:293.PubMedCrossRefGoogle Scholar
  81. Penman, S., and Summers, D., 1965, Effects on host cell metabolism following synchronous infection with poliovirus, Virology 27:614.PubMedCrossRefGoogle Scholar
  82. Penman, S., Scherrer, K., Becker, Y., and Darnell, J. E., 1963, Polyribosomes in normal and poliovirus-infected HeLa cells and their relationship to messenger RNA, Proc. Natl. Acad. Sci. USA 49:654.PubMedCrossRefGoogle Scholar
  83. Pettersson, R. F., Soderlund, H., and Kaariainen, L., 1980, The nucleotide sequences of the 5′-terminal T1 oligonucleotides of Semliki Forest Virus 42S and 26S RNAs are different, Ear. J. Biochem. 105:435.CrossRefGoogle Scholar
  84. Racevskis, J., Kerwar, S. S., and Koch, G., 1976, Inhibition of protein synthesis in reticulocyte lysates by poliovirus, J. Gen. Virol. 31:135.PubMedCrossRefGoogle Scholar
  85. Raghow, R., and Granoff, A., 1983, Cell-free translation of frog virus 3 messenger RNAs: Initiation factors from infected cells discriminate between early and late viral mRNAs. J. Biol. Chem. 258:571.PubMedGoogle Scholar
  86. Rose, J. K., Trachsel, M., Leong, K., and Baltimore, D., 1978, Inhibition of translation by poliovirus inactivation of a specific initiation factor, Proe. Natl. Aead. Sci. USA 75:2732.CrossRefGoogle Scholar
  87. Saborio, J. L., Pong, S. S., and Koch, G., 1974, Selective and reversible inhibition of initiation of protein synthesis in mammalian cells, J. Mol. Biol. 85:195.PubMedCrossRefGoogle Scholar
  88. Saxton, R. E., and Stevens, J. C., 1972, Restriction of herpes simplex virus replication by poliovirus: A selective inhibition of viral translation, Virology 48:207.PubMedCrossRefGoogle Scholar
  89. Seal, S. N., Schmidt, A., and Marcus, A., 1983, Eukaryotic initiation factor 4A is the component that interacts with ATP in protein chain initiation, Proc. Natl. Acad. Sci. USA 80:6562.PubMedCrossRefGoogle Scholar
  90. Sharpe, A. H., and Fields, B. N., 1982, Reovirus inhibition of cellular RNA and protein synthesis: Role of the S4 gene, Virology 122:381.PubMedCrossRefGoogle Scholar
  91. Shih, D. S., Shih, C. T., Kew, O., Pallansch, M., Rueckert, R., and Kaesberg, P., 1978, Cell-free synthesis and processing of the proteins of poliovirus, Proe. Natl. Acad. Sci. USA 75:5807.CrossRefGoogle Scholar
  92. Skup, D., and Millward, S., 1980a, Reovirus-induced modification of cap-dependent translation in infected L cells, Proc. Natl. Acad. Sci. USA 77:152.PubMedCrossRefGoogle Scholar
  93. Skup, D., and Millward, S., 1980b, mRNA capping enzymes are masked in reovirus progeny subviral particles, J. Virol. 34:490.PubMedGoogle Scholar
  94. Skup, D., Zarbl, H., and Millward, S., 1981, Regulation of translation in L-cells infected with reovirus, J. Mol. Biol. 151:35.PubMedCrossRefGoogle Scholar
  95. Sonenberg, N., 1981, ATP/Mg++-dependent crosslinking of cap binding proteins to the 5′ end of eukaryotic mRNA, Nucl. Acids Res. 9:1643.CrossRefGoogle Scholar
  96. Sonenberg, N., and Shatkin, A. J., 1977, Reovirus mRNA can be covalently crosslinked via the 5′ cap to protein in initiation complexes, Proc. Natl. Acad. Sci. USA 74:4288.PubMedCrossRefGoogle Scholar
  97. Sonenberg, N., Morgan, M., Merrick, W., and Shatkin, A. J., 1978, A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA, Proc. Natl. Acad. Sci. USA 75:4843.PubMedCrossRefGoogle Scholar
  98. Sonenberg, N., Morgan, M. A., Testa, D., Collonno, R. J., and Shatkin, A. J., 1979a, Interaction of a limited set of proteins with different mRNAs and protection of 5′-caps against pyrophosphatase digestion in initiation complexes, Nucl. Acids Res. 7:15.CrossRefGoogle Scholar
  99. Sonenberg, N., Ruprecht, K., Hecht, S., and Shatkin, A., 1979b, Eukaryotic mRNA cap binding protein: Purification by affinity chromatography on sepharose-coupled m7 GDP, Proc. Natl. Acad. Sci. USA 76:4345.PubMedCrossRefGoogle Scholar
  100. Sonenberg, N., Trachsel, H., Hecht, S., and Shatkin, A., 1980, Differential stimulation of capped mRNA translation in vitro by cap binding protein, Nature 285:331.PubMedCrossRefGoogle Scholar
  101. Sonenberg, N., Guertin, D., Cleveland, D., and Trachsel, H., 1981, Probing the structure of the eukaryotic 5′ cap structure using a monoclonal antibody directed against cap binding proteins, Cell 27:563.PubMedCrossRefGoogle Scholar
  102. Sonenberg, N., Guertin, D., and Lee, K., 1982, Capped mRNAs with reduced secondary structure can function in extracts from poliovirus-infected cells, Mol. Cell. Biol. 2:1633.PubMedGoogle Scholar
  103. Steiner-Pryor, A., and Cooper, P. D., 1973, Temperature-sensitive poliovirus mutants defective in repression of host protein synthesis are also defective in structural protein, J. Gen. Virol. 21:215.PubMedCrossRefGoogle Scholar
  104. Summers, D. F., and Maizel, J. V., 1967, Disaggregation of HeLa cell polysomes after infection with poliovirus, Virology 31:550.PubMedCrossRefGoogle Scholar
  105. Summers, D. F., Maizel, J. V., and Darnell, J. E., 1965, Evidence for virus-specific noncapsid proteins in poliovirus-infected cells, Proc. Natl. Acad. Sci. USA 54:505.PubMedCrossRefGoogle Scholar
  106. Svitkin, Y. V., Agarova, T. Y., Ginevskaya, V. A., Kalinina, N. O., Scarlat, I. V., and Agol, V. I., 1974, Efficiency of translation of viral and cellular mRNAs in extracts from cells infected with encephalomyocarditis virus, Intervirology 4:214.PubMedGoogle Scholar
  107. Svitkin, Y. V., Ginevskaya, V. A., Ugarova, T. Y., and Agol, V. I., 1978, A cellfree model of the encephalomyocarditis virus-induced inhibition of host cell protein synthesis, Virology 87:199.PubMedCrossRefGoogle Scholar
  108. Tahara, S. M., Morgan, M. A., and Shatkin, A. J., 1981, Two forms of purified m7Gcap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells, J. Biol. Chem. 256:7691.PubMedGoogle Scholar
  109. Tahara, S. M., Morgan, M. A., and Shatkin, A. J., 1983, Binding of inosine-substituted mRNA to reticulocyte ribosomes and eukaryotic initiation factors 4A and 4B requires ATP, J. Biol. Chem. 258:11350.PubMedGoogle Scholar
  110. Tershak, D. A., 1978, Protein kinase activity of polysome-ribosome preparations from poliovirus-infected cells, Biochem. Biophys. Res. Commun. 80:283.PubMedCrossRefGoogle Scholar
  111. Trachsel, H., Sonenberg, N., Shatkin, A. J., Rose, J. K., Leong, K., Bergman, J. E., Gordon, J., and Baltimore, D., 1980, Purification of a factor that restores translation of VSV mRNA in extracts from poliovirus-infected HeLa cells, Proc. Natl. Sci. Acad. Sci. USA 77:770.CrossRefGoogle Scholar
  112. Van Steeg, H., Thomas, A., Verbeck, S., Kasperaitis, M., Voorma, H. O., and Benne, R., 1981a, Shut-off of neuroblastoma cell protein synthesis by Semliki Forest Virus: Loss of ability of crude initiation factors to recognize early Semliki Forest Virus and host mRNAs, J. Virol. 38:728.PubMedGoogle Scholar
  113. Van Steeg, H., Van Grinsven, M., Van Mansfield, F., Voorma, H. O., and Benne, R., 1981b, Initiation of protein synthesis in neuroblastoma cells infected by Semliki Forest Virus: A decreased requirement of late viral mRNA for eIF-4B and cap binding protein, FEBS Lett. 129:62.CrossRefGoogle Scholar
  114. Waiden, W., Godfrey-Colburn, T., and Thach, R. E., 1981, The role of mRNA competition in regulating translation. I. Demonstration of competition in vivo, J. Biol. Chem. 256:11739.Google Scholar
  115. Weber, L. A., Hickey, E. D., Nuss, D. L., and Baglioni, C., 1977, 5′-Terminal 7-methylguanosine and mRNA function: Influence of potassium concentration on translation in vitro, Proc. Natl. Acad. Sci. USA 72:318.Google Scholar
  116. Willems, M., and Penman, S., 1966, The mechanism of host cell protein synthesis inhibition by poliovirus, Virology 30:355.PubMedCrossRefGoogle Scholar
  117. Wright, P. J., and Cooper, P. D., 1974, Poliovirus proteins associated with ribosomal structures in infected cells, Virology 59:1.PubMedCrossRefGoogle Scholar
  118. Zarbl, H., Skup, D., and Millward, S., 1980, Reovirus progeny subviral particles synthesize uncapped mRNA, J. Virol. 34:497.PubMedGoogle Scholar
  119. Zimmerman, E. F., Heeter, M., and Darnell, J. E., 1963, RNA synthesis in poliovirus-infected cells, Virology 19:400.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Ellie Ehrenfeld
    • 1
  1. 1.Departments of Biochemistry and Cellular, Viral, and Molecular BiologyUniversity of Utah School of MedicineSalt Lake CityUSA

Personalised recommendations