Abstract
The amino acid sequences deduced from the nucleic acid sequences of several animal picornaviruses and cowpea mosaic virus (CPMV), a plant virus, were compared. Good homology was found between CPMV and the picornaviruses in the region of the picornavirus 2C (P2-X protein), VPg, 3C pro (proteinase) and 3D pol (RNA polymerase) regions. The CPMV B genome was found to have a similar gene organization to the picornaviruses. A comparison of the 3C pro (proteinase) regions of all of the available picornavirus sequences and CPMV allowed us to identify residues that are completely conserved; of these only two residues, Cys-147 and His-161 (poliovirus proteinase) could be the reactive residues of the active site of a proteinase with analogous mechanism to a known proteinase. We conclude that the proteinases encoded by these viruses are probably cysteine proteinases, mechanistically related, but not homologous to papain.
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Selected References
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- Argos P., Hanei M., Wilson J. M., Kelley W. N. A possible nucleotide-binding domain in the tertiary fold of phosphoribosyltransferases. J Biol Chem. 1983 May 25;258(10):6450–6457. [PubMed] [Google Scholar]
- Argos P., Palau J. Amino acid distribution in protein secondary structures. Int J Pept Protein Res. 1982 Apr;19(4):380–393. doi: 10.1111/j.1399-3011.1982.tb02619.x. [DOI] [PubMed] [Google Scholar]
- Carroll A. R., Rowlands D. J., Clarke B. E. The complete nucleotide sequence of the RNA coding for the primary translation product of foot and mouth disease virus. Nucleic Acids Res. 1984 Mar 12;12(5):2461–2472. doi: 10.1093/nar/12.5.2461. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 1974 Jan 15;13(2):211–222. doi: 10.1021/bi00699a001. [DOI] [PubMed] [Google Scholar]
- Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
- Creighton T. E. Experimental studies of protein folding and unfolding. Prog Biophys Mol Biol. 1978;33(3):231–297. doi: 10.1016/0079-6107(79)90030-0. [DOI] [PubMed] [Google Scholar]
- Dorner A. J., Dorner L. F., Larsen G. R., Wimmer E., Anderson C. W. Identification of the initiation site of poliovirus polyprotein synthesis. J Virol. 1982 Jun;42(3):1017–1028. doi: 10.1128/jvi.42.3.1017-1028.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Emini E. A., Elzinga M., Wimmer E. Carboxy-terminal analysis of poliovirus proteins: termination of poliovirus RNA translation and location of unique poliovirus polyprotein cleavage sites. J Virol. 1982 Apr;42(1):194–199. doi: 10.1128/jvi.42.1.194-199.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Flanegan J. B., Baltimore D. Poliovirus-specific primer-dependent RNA polymerase able to copy poly(A). Proc Natl Acad Sci U S A. 1977 Sep;74(9):3677–3680. doi: 10.1073/pnas.74.9.3677. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Forss S., Schaller H. A tandem repeat gene in a picornavirus. Nucleic Acids Res. 1982 Oct 25;10(20):6441–6450. doi: 10.1093/nar/10.20.6441. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Franssen H., Moerman M., Rezelman G., Goldbach R. Evidence That the 32,000-Dalton Protein Encoded by Bottom-Component RNA of Cowpea Mosaic Virus is a Proteolytic Processing Enzyme. J Virol. 1984 Apr;50(1):183–190. doi: 10.1128/jvi.50.1.183-190.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Goldbach R., Rezelman G. Orientation of the cleavage map of the 200-kilodalton polypeptide encoded by the bottom-component RNA of cowpea mosaic virus. J Virol. 1983 May;46(2):614–619. doi: 10.1128/jvi.46.2.614-619.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HARTLEY B. S. Proteolytic enzymes. Annu Rev Biochem. 1960;29:45–72. doi: 10.1146/annurev.bi.29.070160.000401. [DOI] [PubMed] [Google Scholar]
- Hanecak R., Semler B. L., Anderson C. W., Wimmer E. Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc Natl Acad Sci U S A. 1982 Jul;79(13):3973–3977. doi: 10.1073/pnas.79.13.3973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hanecak R., Semler B. L., Ariga H., Anderson C. W., Wimmer E. Expression of a cloned gene segment of poliovirus in E. coli: evidence for autocatalytic production of the viral proteinase. Cell. 1984 Jul;37(3):1063–1073. doi: 10.1016/0092-8674(84)90441-0. [DOI] [PubMed] [Google Scholar]
- Jones D. D. Amino acid properties and side-chain orientation in proteins: a cross correlation appraoch. J Theor Biol. 1975 Mar;50(1):167–183. doi: 10.1016/0022-5193(75)90031-4. [DOI] [PubMed] [Google Scholar]
- Keim P., Heinrikson R. L., Fitch W. M. An examination of the expected degree of sequence similarity that might arise in proteins that have converged to similar conformational states. The impact of such expectations on the search for homology between the structurally similar domains of rhodanese. J Mol Biol. 1981 Sep 5;151(1):179–197. doi: 10.1016/0022-2836(81)90227-8. [DOI] [PubMed] [Google Scholar]
- King A. M., Sangar D. V., Harris T. J., Brown F. Heterogeneity of the genome-linked protein of foot-and-mouth disease virus. J Virol. 1980 Jun;34(3):627–634. doi: 10.1128/jvi.34.3.627-634.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kitamura N., Adler C. J., Rothberg P. G., Martinko J., Nathenson S. G., Wimmer E. The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies. Cell. 1980 Aug;21(1):295–302. doi: 10.1016/0092-8674(80)90137-3. [DOI] [PubMed] [Google Scholar]
- Kitamura N., Semler B. L., Rothberg P. G., Larsen G. R., Adler C. J., Dorner A. J., Emini E. A., Hanecak R., Lee J. J., van der Werf S. Primary structure, gene organization and polypeptide expression of poliovirus RNA. Nature. 1981 Jun 18;291(5816):547–553. doi: 10.1038/291547a0. [DOI] [PubMed] [Google Scholar]
- Lomonossoff G. P., Shanks M. The nucleotide sequence of cowpea mosaic virus B RNA. EMBO J. 1983;2(12):2253–2258. doi: 10.1002/j.1460-2075.1983.tb01731.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lomonossoff G. P., Shanks M. The nucleotide sequence of cowpea mosaic virus B RNA. EMBO J. 1983;2(12):2253–2258. doi: 10.1002/j.1460-2075.1983.tb01731.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Manavalan P., Ponnuswamy P. K. Hydrophobic character of amino acid residues in globular proteins. Nature. 1978 Oct 19;275(5681):673–674. doi: 10.1038/275673a0. [DOI] [PubMed] [Google Scholar]
- Nomoto A., Omata T., Toyoda H., Kuge S., Horie H., Kataoka Y., Genba Y., Nakano Y., Imura N. Complete nucleotide sequence of the attenuated poliovirus Sabin 1 strain genome. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5793–5797. doi: 10.1073/pnas.79.19.5793. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palau J., Argos P., Puigdomenech P. Protein secondary structure. Studies on the limits of prediction accuracy. Int J Pept Protein Res. 1982 Apr;19(4):394–401. [PubMed] [Google Scholar]
- Pallansch M. A., Kew O. M., Semler B. L., Omilianowski D. R., Anderson C. W., Wimmer E., Rueckert R. R. Protein processing map of poliovirus. J Virol. 1984 Mar;49(3):873–880. doi: 10.1128/jvi.49.3.873-880.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palmenberg A. C., Kirby E. M., Janda M. R., Drake N. L., Duke G. M., Potratz K. F., Collett M. S. The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region. Nucleic Acids Res. 1984 Mar 26;12(6):2969–2985. doi: 10.1093/nar/12.6.2969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Palmenberg A. C., Rueckert R. R. Evidence for intramolecular self-cleavage of picornaviral replicase precursors. J Virol. 1982 Jan;41(1):244–249. doi: 10.1128/jvi.41.1.244-249.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Peng X. X., Shih D. S. Proteolytic processing of the proteins translated from the bottom component RNA of cowpea mosaic virus. The primary and secondary cleavage reactions. J Biol Chem. 1984 Mar 10;259(5):3197–3201. [PubMed] [Google Scholar]
- Polgár L., Halász P. Current problems in mechanistic studies of serine and cysteine proteinases. Biochem J. 1982 Oct 1;207(1):1–10. doi: 10.1042/bj2070001. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Racaniello V. R., Baltimore D. Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4887–4891. doi: 10.1073/pnas.78.8.4887. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robertus J. D., Alden R. A., Birktoft J. J., Kraut J., Powers J. C., Wilcox P. E. An x-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN'. Biochemistry. 1972 Jun 20;11(13):2439–2449. doi: 10.1021/bi00763a009. [DOI] [PubMed] [Google Scholar]
- Rothberg P. G., Harris T. J., Nomoto A., Wimmer E. O4-(5'-uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4868–4872. doi: 10.1073/pnas.75.10.4868. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rueckert R. R., Wimmer E. Systematic nomenclature of picornavirus proteins. J Virol. 1984 Jun;50(3):957–959. doi: 10.1128/jvi.50.3.957-959.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Semler B. L., Hanecak R., Anderson C. W., Wimmer E. Cleavage sites in the polypeptide precursors of poliovirus protein P2-X. Virology. 1981 Oct 30;114(2):589–594. doi: 10.1016/0042-6822(81)90242-7. [DOI] [PubMed] [Google Scholar]
- Stanway G., Cann A. J., Hauptmann R., Hughes P., Clarke L. D., Mountford R. C., Minor P. D., Schild G. C., Almond J. W. The nucleotide sequence of poliovirus type 3 leon 12 a1b: comparison with poliovirus type 1. Nucleic Acids Res. 1983 Aug 25;11(16):5629–5643. doi: 10.1093/nar/11.16.5629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sweet R. M., Eisenberg D. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J Mol Biol. 1983 Dec 25;171(4):479–488. doi: 10.1016/0022-2836(83)90041-4. [DOI] [PubMed] [Google Scholar]
- Takegami T., Kuhn R. J., Anderson C. W., Wimmer E. Membrane-dependent uridylylation of the genome-linked protein VPg of poliovirus. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7447–7451. doi: 10.1073/pnas.80.24.7447. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Takegami T., Semler B. L., Anderson C. W., Wimmer E. Membrane fractions active in poliovirus RNA replication contain VPg precursor polypeptides. Virology. 1983 Jul 15;128(1):33–47. doi: 10.1016/0042-6822(83)90316-1. [DOI] [PubMed] [Google Scholar]
- Takio K., Towatari T., Katunuma N., Teller D. C., Titani K. Homology of amino acid sequences of rat liver cathepsins B and H with that of papain. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3666–3670. doi: 10.1073/pnas.80.12.3666. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Toyoda H., Kohara M., Kataoka Y., Suganuma T., Omata T., Imura N., Nomoto A. Complete nucleotide sequences of all three poliovirus serotype genomes. Implication for genetic relationship, gene function and antigenic determinants. J Mol Biol. 1984 Apr 25;174(4):561–585. doi: 10.1016/0022-2836(84)90084-6. [DOI] [PubMed] [Google Scholar]
- Wolfenden R. V., Cullis P. M., Southgate C. C. Water, protein folding, and the genetic code. Science. 1979 Nov 2;206(4418):575–577. doi: 10.1126/science.493962. [DOI] [PubMed] [Google Scholar]
- van Wezenbeek P., Verver J., Harmsen J., Vos P., van Kammen A. Primary structure and gene organization of the middle-component RNA of cowpea mosaic virus. EMBO J. 1983;2(6):941–946. doi: 10.1002/j.1460-2075.1983.tb01525.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
