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. 1979 Dec;32(3):770–778. doi: 10.1128/jvi.32.3.770-778.1979

Protease required for processing picornaviral coat protein resides in the viral replicase gene.

A C Palmenberg, M A Pallansch, R R Rueckert
PMCID: PMC525924  PMID: 229266

Abstract

Partial purification of the encephalomyocarditis protease synthesized in extracts from rabbit reticulocytes shows that the activity responsible for cleaving coat precursor protein cosediments with a previously unmapped virus-coded protein with an apparent molecular weight of 20,000. Tryptic analysis shows that this protein is derived from protein D, a virus-coded component of the encephalomyocarditis RNA polymerase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  2. Bowles S. A., Tershak D. R. Proteolysis of noncapsid protein 2 of type 3 poliovirus at the restrictive temperature: breakdown of noncapsid protein 2 correlates with loss of RNA synthesis. J Virol. 1978 Aug;27(2):443–448. doi: 10.1128/jvi.27.2.443-448.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Butterworth B. E., Hall L., Stoltzfus C. M., Rueckert R. R. Virus-specific proteins synthesized in encephalomyocarditis virus-infected HeLa cells. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3083–3087. doi: 10.1073/pnas.68.12.3083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Butterworth B. E., Korant B. D. Characterization of the large picornaviral polypeptides produced in the presence of zinc ion. J Virol. 1974 Aug;14(2):282–291. doi: 10.1128/jvi.14.2.282-291.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Butterworth B. E., Rueckert R. R. Kinetics of synthesis and cleavage of encephalomyocarditis virus-specific proteins. Virology. 1972 Nov;50(2):535–549. doi: 10.1016/0042-6822(72)90405-9. [DOI] [PubMed] [Google Scholar]
  6. Dasgupta A., Baron M. H., Baltimore D. Poliovirus replicase: a soluble enzyme able to initiate copying of poliovirus RNA. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2679–2683. doi: 10.1073/pnas.76.6.2679. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dunker A. K., Rueckert R. R. Observations on molecular weight determinations on polyacrylamide gel. J Biol Chem. 1969 Sep 25;244(18):5074–5080. [PubMed] [Google Scholar]
  8. Flanegan J. B., Baltimore D. Poliovirus polyuridylic acid polymerase and RNA replicase have the same viral polypeptide. J Virol. 1979 Jan;29(1):352–360. doi: 10.1128/jvi.29.1.352-360.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Golini F., Nomoto A., Wimmer E. The genome-linked protein of picornaviruses. IV. Difference in the VPg's of encephalomyocarditis virus and poliovirus as evidence that the genome-linked proteins are virus-coded. Virology. 1978 Aug;89(1):112–118. doi: 10.1016/0042-6822(78)90045-4. [DOI] [PubMed] [Google Scholar]
  10. Holland J. J., Doyle M., Perrault J., Kingsbury D. T., Etchison J. Proteinase activity in purified animal viruses. Biochem Biophys Res Commun. 1972 Jan 31;46(2):634–639. doi: 10.1016/s0006-291x(72)80187-6. [DOI] [PubMed] [Google Scholar]
  11. Hruby D. E., Roberts W. K. Encephalomyocarditis virus RNA. III. Presence of a genome-associated protein. J Virol. 1978 Jan;25(1):413–415. doi: 10.1128/jvi.25.1.413-415.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kessler S. W. Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J Immunol. 1975 Dec;115(6):1617–1624. [PubMed] [Google Scholar]
  13. Korant B., Chow N., Lively M., Powers J. Virus-specified protease in poliovirus-infected HeLa cells. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2992–2995. doi: 10.1073/pnas.76.6.2992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lawrence C., Thach R. E. Identification of a viral protein involved in post-translational maturation of the encephalomyocarditis virus capsid precursor. J Virol. 1975 Apr;15(4):918–928. doi: 10.1128/jvi.15.4.918-928.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Loesch W. T., Jr, Arlinghaus A. Stable polypeptides associated with the 250S mengovirus-induced RNA polymerase structure. Arch Virol. 1975;47(3):201–215. doi: 10.1007/BF01317808. [DOI] [PubMed] [Google Scholar]
  16. Lundquist R. E., Ehrenfeld E., Maizel J. V., Jr Isolation of a viral polypeptide associated with poliovirus RNA polymerase. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4773–4777. doi: 10.1073/pnas.71.12.4773. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. McGregor S. Evidence for the existence of protomers in the assembly of encephalomyocarditis virus. J Virol. 1975 May;15(5):1107–1120. doi: 10.1128/jvi.15.5.1107-1120.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Medappa K. C., McLean C., Rueckert R. R. On the structure of rhinovirus 1A. Virology. 1971 May;44(2):259–270. doi: 10.1016/0042-6822(71)90258-3. [DOI] [PubMed] [Google Scholar]
  19. Medvedkina O. A., Scarlat I. V., Kalinina N. O., Agol V. I. Virus-specific proteins associated with ribosomes of Krebs-II cells infected with encephalomyocarditis virus. FEBS Lett. 1974 Feb 1;39(1):4–8. doi: 10.1016/0014-5793(74)80003-7. [DOI] [PubMed] [Google Scholar]
  20. Pelham H. R. Translation of encephalomyocarditis virus RNA in vitro yields an active proteolytic processing enzyme. Eur J Biochem. 1978 Apr 17;85(2):457–462. doi: 10.1111/j.1432-1033.1978.tb12260.x. [DOI] [PubMed] [Google Scholar]
  21. Pettersson R. F., Ambros V., Baltimore D. Identification of a protein linked to nascent poliovirus RNA and to the polyuridylic acid of negative-strand RNA. J Virol. 1978 Aug;27(2):357–365. doi: 10.1128/jvi.27.2.357-365.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pettersson R. F., Flanegan J. B., Rose J. K., Baltimore D. 5'-Terminal nucleotide sequences of polio virus polyribosomal RNA and virion RNA are identical. Nature. 1977 Jul 21;268(5617):270–272. doi: 10.1038/268270a0. [DOI] [PubMed] [Google Scholar]
  23. Polatnick J., Arlinghaus R. B., Graves J. H., Cowan K. M. Inhibition of cell-free foot-and-mouth disease virus-ribonucleic acid synthesis by antibody. Virology. 1967 Apr;31(4):609–615. doi: 10.1016/0042-6822(67)90189-4. [DOI] [PubMed] [Google Scholar]
  24. Röder A., Koschel K. Virus-specific proteins associated with the replication complex of poliovirus RNA. J Gen Virol. 1975 Jul;28(1):85–98. doi: 10.1099/0022-1317-28-1-85. [DOI] [PubMed] [Google Scholar]
  25. Shih D. S., Shih C. T., Kew O., Pallansch M., Rueckert R., Kaesberg P. Cell-free synthesis and processing of the proteins of poliovirus. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5807–5811. doi: 10.1073/pnas.75.12.5807. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Shih D. S., Shih C. T., Zimmern D., Rueckert R. R., Kaesberg P. Translation of encephalomyocarditis virus RNA in reticulocyte lysates: kinetic analysis of the formation of virion proteins and a protein required for processing. J Virol. 1979 May;30(2):472–480. doi: 10.1128/jvi.30.2.472-480.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Svitkin Y. V., Agol V. I. Complete translation of encephalomyocarditis virus RNA and faithful cleavage of virus-specific proteins in a cell-free system from Krebs-2 cells. FEBS Lett. 1978 Mar 1;87(1):7–11. doi: 10.1016/0014-5793(78)80121-5. [DOI] [PubMed] [Google Scholar]
  28. Traub A., Duskin B., Rosenberg H., Kalmar E. Isolation and properties of the replicase of encephalomyocarditis virus. J Virol. 1976 May;18(2):375–382. doi: 10.1128/jvi.18.2.375-382.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]

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