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Gene Review

RPVgp2  -  P protein

Rinderpest virus (strain Kabete O)

 
 
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Disease relevance of RPVgp2

  • In an in vivo replication/transcription system using a synthetic minigenome of RPV, we show that multimerization is essential for P protein function(s), and the multimerization domain is highly conserved between two morbilliviruses namely RPV and peste de petits ruminants virus [1].
  • We report here the characterization of oligomeric P protein of rinderpest virus (RPV) and provide a structural basis for its multimerization [1].
  • These results are discussed in the context of biological functions of P protein among various negative-stranded RNA viruses [1].
  • The P gene of measles virus (MV) encodes the P protein and three accessory proteins (C, V, and R) [2].
  • Of the antibodies specific for the P protein, the antibody against one site was cross-reactive with all the strains of RPV, measles virus (MV) and canine distemper virus (CDV), the antibody against another site was reactive with RPV and MV but not with CDV, and the antibodies against the other two sites were specific for RPV [3].
 

High impact information on RPVgp2

 

Biological context of RPVgp2

  • Plasmid DNA containing a virus-specific insert, representing greater than 98% of the gene derived from the P-protein mRNA of canine distemper virus, showed significant cross-hybridisation with all the other members of the morbillivirus group [8].
 

Associations of RPVgp2 with chemical compounds

  • The N and P protein were demonstrated in nucleus, cytoplasm and cell processes, whereas M, H and F protein were observed in the cytoplasm only and rarely in cell processes [9].
 

Regulatory relationships of RPVgp2

 

Other interactions of RPVgp2

  • Furthermore, when the Sendai P-L polymerase complex was provided separately, measles N protein alone synthesized DI genome RNA in the absence of Sendai P protein [11].
  • When these proteins were coexpressed from plasmids in a mammalian expression system, a complex was formed as detected by the coimmunoprecipitation of the L protein with the P protein by anti-P antibodies [7].
  • However, limited proteolysis has shown that this protein is not a phosphorylated form of the M protein, but appears related to the P protein of measles virus [12].
  • In acute and subacute lesions without associated inflammation, expression of the M, H and F protein was only slightly diminished compared to the N and P protein [9].
 

Analytical, diagnostic and therapeutic context of RPVgp2

  • Using the same two-hybrid assay, we discovered that the P protein interacts strongly with itself [13].
  • The SDS-PAGE migration pattern of the P protein varied from case to case, but was similar when isolates from different tissues of the same case were compared [14].
  • Contrasting with the reported colocalization of intracellular measles virus C proteins with nucleocapsid inclusions, immunofluorescence studies revealed that Sendai virus C proteins were uniformly distributed in the cytoplasm whereas the viral P protein was present in inclusions that were mainly perinuclear [15].

References

  1. Phosphoprotein of the rinderpest virus forms a tetramer through a coiled coil region important for biological function. A structural insight. Rahaman, A., Srinivasan, N., Shamala, N., Shaila, M.S. J. Biol. Chem. (2004) [Pubmed]
  2. Stringent requirement for the C protein of wild-type measles virus for growth both in vitro and in macaques. Takeuchi, K., Takeda, M., Miyajima, N., Ami, Y., Nagata, N., Suzaki, Y., Shahnewaz, J., Kadota, S., Nagata, K. J. Virol. (2005) [Pubmed]
  3. Characterization of monoclonal antibodies against four structural proteins of rinderpest virus. Sugiyama, M., Minamoto, N., Kinjo, T., Hirayama, N., Sasaki, H., Yoshikawa, Y., Yamanouchi, K. J. Gen. Virol. (1989) [Pubmed]
  4. Ribosomal frameshifting during translation of measles virus P protein mRNA is capable of directing synthesis of a unique protein. Liston, P., Briedis, D.J. J. Virol. (1995) [Pubmed]
  5. Conformational maturation of measles virus nucleocapsid protein. Gombart, A.F., Hirano, A., Wong, T.C. J. Virol. (1993) [Pubmed]
  6. Cellular casein kinase II-mediated phosphorylation of rinderpest virus P protein is a prerequisite for its role in replication/transcription of the genome. Kaushik, R., Shaila, M.S. J. Gen. Virol. (2004) [Pubmed]
  7. An amino-proximal domain of the L protein binds to the P protein in the measles virus RNA polymerase complex. Horikami, S.M., Smallwood, S., Bankamp, B., Moyer, S.A. Virology (1994) [Pubmed]
  8. Comparison of messenger RNAs induced in cells infected with each member of the morbillivirus group. Barrett, T., Underwood, B. Virology (1985) [Pubmed]
  9. Restricted expression of viral surface proteins in canine distemper encephalitis. Alldinger, S., Baumgärtner, W., Orvell, C. Acta Neuropathol. (1993) [Pubmed]
  10. Domains of the measles virus N protein required for binding to P protein and self-assembly. Bankamp, B., Horikami, S.M., Thompson, P.D., Huber, M., Billeter, M., Moyer, S.A. Virology (1996) [Pubmed]
  11. Measles virus nucleocapsid protein can function in Sendai virus defective interfering particle genome synthesis in vitro. Chandrika, R., Myers, T., Moyer, S.A. Virology (1995) [Pubmed]
  12. A study of phosphorylation of the measles membrane protein. Rima, B.K., Lappin, S.A., Roberts, M.W., Martin, S.J. J. Gen. Virol. (1981) [Pubmed]
  13. Measles virus phosphoprotein (P) requires the NH2- and COOH-terminal domains for interactions with the nucleoprotein (N) but only the COOH terminus for interactions with itself. Harty, R.N., Palese, P. J. Gen. Virol. (1995) [Pubmed]
  14. In vitro and in vivo properties of the virus causing natural canine distemper encephalitis. Kimoto, T. J. Gen. Virol. (1986) [Pubmed]
  15. Localization and characterization of Sendai virus nonstructural C and C' proteins by antibodies against synthetic peptides. Portner, A., Gupta, K.C., Seyer, J.M., Beachey, E.H., Kingsbury, D.W. Virus Res. (1986) [Pubmed]
 
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