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Gene Review

PVgp1  -  genome polyprotein

Enterovirus C

 
 
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Disease relevance of PVgp1

  • Identification of the initiation site of poliovirus polyprotein synthesis [1].
  • Mammalian (+)-strand RNA viruses and retroviruses have responded by reducing the number of cis-acting regulatory elements, a constraint that has led to the emergence of the polyprotein [2].
  • The amino termini of capsid polypeptides VP1 and VP3 were determined by direct sequencing, and the other proteolytic cleavage sites in the polyprotein were predicted by comparison with other picornavirus proteins [3].
  • This genome includes a 5' untranslated region, relatively well-conserved when compared with aphtho- and cardioviruses, followed by an open reading frame coding for a 2180-amino acid-long polyprotein [3].
  • We have engineered a segment of the poliovirus genome (nucleotides 5438-6061) that encodes the 183 amino acid residues of the 3C region and 25 residues of the 3D region of the viral polyprotein into an Escherichia coli expression vector [4].
 

High impact information on PVgp1

 

Chemical compound and disease context of PVgp1

 

Biological context of PVgp1

 

Anatomical context of PVgp1

  • Because all proteins that map at the amino terminus of the polyprotein (P1-1a, VP0, and VP4) are blocked at their amino termini and previous studies of ribosome binding have been inconclusive, direct identification of the initiation site of protein synthesis was difficult [1].
  • A portion of the poliovirus polyprotein containing the 2Apro cleavage site at the P1/P2 junction was produced by translation of cDNA transcripts in rabbit reticulocyte lysates and then tested as a substrate for 2Apro-mediated cleavage [17].
  • Since these defects are observed under conditions where no abnormalities in the rate of synthesis and processing of the mutant polyprotein occur, the inability to induce the cytopathic effect in infected Vero cells denotes the existence of a defect in the activity of 3A, but not the level of expression of the viral genome [18].
 

Associations of PVgp1 with chemical compounds

  • This defect appeared to be due to the impaired initiation of viral polyprotein synthesis as evidenced by a relatively low level of accumulation of polypeptide 1a (which corresponds to an NH2-terminal region of the polyprotein) in samples programmed with RNAs from attenuated strains [19].
 

Analytical, diagnostic and therapeutic context of PVgp1

  • Sequence analysis of trypsin-digested VP4, which has a blocked amino terminus, demonstrates that VP4 is encoded at or very near to the amino terminus of the polyprotein [20].
  • A group of proteins derived from the P3 region of the polyprotein was identified by immunoprecipitation, time course, and N-formyl-[35S]methionine labeling studies to be the product of the initiation of protein synthesis at an internal site(s) located within the 3'-proximal RNA sequences [21].
  • Oligonucleotide-directed site-specific mutagenesis of an infectious poliovirus type 1 (Mahoney strain) cDNA was used to change the Gln-Gly site at the 3C/3D junction of the polyprotein into Gln-Val, Gln-Ala, Gln-Ser or Gln-Pro [22].

References

  1. Identification of the initiation site of poliovirus polyprotein synthesis. Dorner, A.J., Dorner, L.F., Larsen, G.R., Wimmer, E., Anderson, C.W. J. Virol. (1982) [Pubmed]
  2. Cardioviral internal ribosomal entry site is functional in a genetically engineered dicistronic poliovirus. Molla, A., Jang, S.K., Paul, A.V., Reuer, Q., Wimmer, E. Nature (1992) [Pubmed]
  3. A distinct picornavirus group identified by sequence analysis. Hyypiä, T., Horsnell, C., Maaronen, M., Khan, M., Kalkkinen, N., Auvinen, P., Kinnunen, L., Stanway, G. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  4. Expression and site-specific mutagenesis of the poliovirus 3C protease in Escherichia coli. Ivanoff, L.A., Towatari, T., Ray, J., Korant, B.D., Petteway, S.R. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  5. Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Allaire, M., Chernaia, M.M., Malcolm, B.A., James, M.N. Nature (1994) [Pubmed]
  6. Primary structure, gene organization and polypeptide expression of poliovirus RNA. 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., Anderson, C.W., Wimmer, E. Nature (1981) [Pubmed]
  7. Cell-free, de novo synthesis of poliovirus. Molla, A., Paul, A.V., Wimmer, E. Science (1991) [Pubmed]
  8. Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity. Kräusslich, H.G., Hölscher, C., Reuer, Q., Harber, J., Wimmer, E. J. Virol. (1990) [Pubmed]
  9. Determinants of substrate recognition by poliovirus 2A proteinase. Hellen, C.U., Lee, C.K., Wimmer, E. J. Virol. (1992) [Pubmed]
  10. Poliovirus capsid proteins derived from P1 precursors with glutamine-valine cleavage sites have defects in assembly and RNA encapsidation. Ansardi, D.C., Morrow, C.D. J. Virol. (1993) [Pubmed]
  11. Separation of native and truncated forms of poliovirus protease 3C produced in Escherichia coli. Polgár, L., Erdélyi, F., Hajnal, E., Löw, M., Gráf, L., Korant, B.D. Biochem. J. (1993) [Pubmed]
  12. PDTC inhibits picornavirus polyprotein processing and RNA replication by transporting zinc ions into cells. Lanke, K., Krenn, B.M., Melchers, W.J., Seipelt, J., van Kuppeveld, F.J. J. Gen. Virol. (2007) [Pubmed]
  13. Translational enhancement of the poliovirus 5' noncoding region mediated by virus-encoded polypeptide 2A. Hambidge, S.J., Sarnow, P. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  14. Nucleotide sequence and genome organization of foot-and-mouth disease virus. Forss, S., Strebel, K., Beck, E., Schaller, H. Nucleic Acids Res. (1984) [Pubmed]
  15. Degradation of cellular proteins during poliovirus infection: studies by two-dimensional gel electrophoresis. Urzainqui, A., Carrasco, L. J. Virol. (1989) [Pubmed]
  16. Genetic variation occurring on the genome of an in vitro insertion mutant of poliovirus type 1. Kuge, S., Kawamura, N., Nomoto, A. J. Virol. (1989) [Pubmed]
  17. cis- and trans-cleavage activities of poliovirus 2A protease expressed in Escherichia coli. Alvey, J.C., Wyckoff, E.E., Yu, S.F., Lloyd, R., Ehrenfeld, E. J. Virol. (1991) [Pubmed]
  18. Genetic analysis of poliovirus protein 3A: characterization of a non-cytopathic mutant virus defective in killing Vero cells. Lama, J., Sanz, M.A., Carrasco, L. J. Gen. Virol. (1998) [Pubmed]
  19. The genomes of attenuated and virulent poliovirus strains differ in their in vitro translation efficiencies. Svitkin, Y.V., Maslova, S.V., Agol, V.I. Virology (1985) [Pubmed]
  20. Cleavage sites within the poliovirus capsid protein precursors. Larsen, G.R., Anderson, C.W., Dorner, A.J., Semler, B.L., Wimmer, E. J. Virol. (1982) [Pubmed]
  21. In vitro translation of poliovirus RNA: utilization of internal initiation sites in reticulocyte lysate. Dorner, A.J., Semler, B.L., Jackson, R.J., Hanecak, R., Duprey, E., Wimmer, E. J. Virol. (1984) [Pubmed]
  22. Cleavage specificity of the poliovirus 3C protease is not restricted to Gln-Gly at the 3C/3D junction. Kean, K.M., Teterina, N., Girard, M. J. Gen. Virol. (1990) [Pubmed]
 
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