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Gene Review

MVEVgp1  -  polyprotein

Murray Valley encephalitis virus

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Disease relevance of MVEVgp1

  • Safety and immunogenicity of NYVAC-based recombinants expressing the rabies virus glycoprotein, a polyprotein from Japanese encephalitis virus, and seven antigens from Plasmodium falciparum have been demonstrated to be safe and immunogenic in early human vaccine studies [1].
  • Signal peptidase cleavage at the C-prM junction in the flavivirus structural polyprotein is inefficient in the absence of the cytoplasmic viral protease, which catalyzes cleavage at the COOH terminus of the C protein [2].
  • In this study, we used cDNA of Murray Valley encephalitis virus (MVE) to examine features of the structural polyprotein which allow this regulation of a luminal cleavage by a cytoplasmic protease [2].
  • The West Nile Virus (WNV) non-structural proteins 2B and 3 (NS2B-NS3) constitute the proteolytic complex that mediates the cleavage and processing of the viral polyprotein [3].
  • The cell-associated WN virus particles are constructed from the proteins C, pre-M, and E which contain the amino residues 1-105, 124-290, and 291-787 of the polyprotein, respectively [4].

High impact information on MVEVgp1

  • WNV has a positive strand RNA genome of about 11 kb that encodes a single polyprotein [5].
  • We show that control of signalase cleavage of the multimembrane-spanning flavivirus polyprotein by the catalytic function of the viral protease is critical for efficient virus morphogenesis [6].
  • We also examined the effect of proteolytic processing in the MVE nonstructural polyprotein segment mediated by the viral proteinase NS3 on antigen processing and presentation of the MVE H-2Kk-restricted T cell determinant [7].
  • The proteolytic processing of a non-structural polyprotein segment from the cytoplasmic domain of NS2A to the C terminus of NS5 of Murray Valley encephalitis (MVE) virus was examined, when expressed from cDNA via a vaccinia virus recombinant, in transiently transfected COS cells, or synthesized by cell-free translation [8].
  • Similarly, substitution of residue histidine 51 of the NS3 polyprotein segment, which is predicted to be part of the protease catalytic centre, with an alanine residue, blocks the processing of the polyprotein in vitro [9].

Chemical compound and disease context of MVEVgp1

  • A common genomic organization and molecular mechanisms of replication in hosts are shared by flaviviruses with a viral serine protease playing a pivotal role in processing the viral polyprotein into component polypeptides, an obligatory step in viral replication [10].

Biological context of MVEVgp1


Anatomical context of MVEVgp1

  • The amino-terminal part of the polyprotein containing the amino acid residues 1 to 123 is released as a molecule which migrates slightly slower than the mature viral core protein and which presumably is associated to the RER membranes via its carboxy-terminal sequence [4].

Associations of MVEVgp1 with chemical compounds


Analytical, diagnostic and therapeutic context of MVEVgp1

  • Termination codons were introduced by site-directed mutagenesis at the junctions of the NS3-4A, NS4A-4B and NS4B-5 genes to generate C-terminal truncations of the MVE virus polyprotein segment [8].


  1. Applications of pox virus vectors to vaccination: an update. Paoletti, E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM. Stocks, C.E., Lobigs, M. J. Virol. (1998) [Pubmed]
  3. Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway. Ramanathan, M.P., Chambers, J.A., Pankhong, P., Chattergoon, M., Attatippaholkun, W., Dang, K., Shah, N., Weiner, D.B. Virology (2006) [Pubmed]
  4. Analyses of the terminal sequences of West Nile virus structural proteins and of the in vitro translation of these proteins allow the proposal of a complete scheme of the proteolytic cleavages involved in their synthesis. Nowak, T., Färber, P.M., Wengler, G., Wengler, G. Virology (1989) [Pubmed]
  5. The molecular biology of West Nile Virus: a new invader of the western hemisphere. Brinton, M.A. Annu. Rev. Microbiol. (2002) [Pubmed]
  6. Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes. Lobigs, M., Lee, E. J. Virol. (2004) [Pubmed]
  7. The flavivirus nonstructural protein NS3 is a dominant source of cytotoxic T cell peptide determinants. Lobigs, M., Arthur, C.E., Müllbacher, A., Blanden, R.V. Virology (1994) [Pubmed]
  8. Proteolytic processing of a Murray Valley encephalitis virus non-structural polyprotein segment containing the viral proteinase: accumulation of a NS3-4A precursor which requires mature NS3 for efficient processing. Lobigs, M. J. Gen. Virol. (1992) [Pubmed]
  9. In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids. Wengler, G., Czaya, G., Färber, P.M., Hegemann, J.H. J. Gen. Virol. (1991) [Pubmed]
  10. Identification and characterization of nonsubstrate based inhibitors of the essential dengue and West Nile virus proteases. Ganesh, V.K., Muller, N., Judge, K., Luan, C.H., Padmanabhan, R., Murthy, K.H. Bioorg. Med. Chem. (2005) [Pubmed]
  11. Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins. Coia, G., Parker, M.D., Speight, G., Byrne, M.E., Westaway, E.G. J. Gen. Virol. (1988) [Pubmed]
  12. Identification and analysis of truncated and elongated species of the flavivirus NS1 protein. Blitvich, B.J., Scanlon, D., Shiell, B.J., Mackenzie, J.S., Hall, R.A. Virus Res. (1999) [Pubmed]
  13. Protection of mice against lethal Japanese encephalitis with a recombinant baculovirus vaccine. McCown, J., Cochran, M., Putnak, R., Feighny, R., Burrous, J., Henchal, E., Hoke, C. Am. J. Trop. Med. Hyg. (1990) [Pubmed]
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