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Gene Review

P  -  P

Bovine respiratory syncytial virus

 
 
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Disease relevance of P

 

High impact information on P

  • A double mutant containing both G172S and E176G changes in the P gene, substitution of the three charged residues at positions 174 to 176 by alanine, and a deletion of residues from positions 161 to 180 completely abolished the P protein function in the minigenome assay [6].
  • Both P mutants exhibited greatly reduced activity in supporting the replication and transcription of an RSV minigenome replicon at 37 and 39 degrees C. The G172S and E176G mutations were introduced individually into the RSV A2 (rA2) antigenomic cDNA, and recombinant viruses, rA2-P172 and rA2-P176, were obtained [6].
  • By screening a randomly mutagenized P gene cDNA library, two independent mutations, one with a substitution of glycine at position 172 by serine (G172S) and the other with a substitution of glutamic acid at position 176 by glycine (E176G), were identified to result in the loss of N-P interaction at 37 degrees C in the yeast two-hybrid assay [6].
  • Identification of temperature-sensitive mutations in the phosphoprotein of respiratory syncytial virus that are likely involved in its interaction with the nucleoprotein [6].
  • The data suggest that N and L protein binding domains on the P protein do not overlap [1].
 

Chemical compound and disease context of P

 

Biological context of P

  • The P mRNA is 860 nucleotides long with a single large open reading frame and the encoded polypeptide is 241 amino acids long [8].
  • Of the five proteins analyzed in U.S. viruses, P was the most variable (81% amino acid sequence identity) and N was the most conserved (95% amino acid sequence identity) [9].
  • In addition, the phosphorylation-defective P mutants exhibited a trans-dominant negative phenotype, consistent with the finding that the mutant proteins bound to the N-RNA template as efficiently as the wild type [10].
  • Transfection of plasmids encoding the BRSV minigenome, nucleocapsid protein (N), phosphoprotein (P) and L protein, each under the control of T7 promoter, into cells infected with a vaccinia virus recombinant expressing the T7 RNA polymerase gave rise to CAT activity and progeny with the minigenome [11].
  • The P gene of APV/US showed only 53% nucleotide sequence identity with the ortholog from APV subgroup A [12].
 

Anatomical context of P

 

Other interactions of P

  • Further, inclusion of small amounts of the M2 protein along with the N, P and L proteins greatly augmented minigenome transcription [11].
 

Analytical, diagnostic and therapeutic context of P

  • Moreover, sequence analysis of the N and P genes from two laboratory adapted isolates of APV/US (APV/MN-1a and APV/MN-1b) and from ten clinical samples from APV-infected turkeys suggests only modest level of amino acid divergence in the N (0-0.3%) and P (0-1.4%) proteins [12].
  • The nine isolates of BRSV showed different patterns of reactivity in enzyme immunoassays with panels of MAbs to HRSV subgroups A and B. Major variations in the molecular weights of the P (phosphoprotein) and F (fusion protein) proteins were demonstrated among the BRSV isolates tested [14].

References

  1. Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N-P and P-L interactions using a minigenome system. Khattar, S.K., Yunus, A.S., Samal, S.K. J. Gen. Virol. (2001) [Pubmed]
  2. Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N-P interaction using a two-hybrid system. Mallipeddi, S.K., Lupiani, B., Samal, S.K. J. Gen. Virol. (1996) [Pubmed]
  3. Biochemical characterization of the respiratory syncytial virus P-P and P-N protein complexes and localization of the P protein oligomerization domain. Castagné, N., Barbier, A., Bernard, J., Rezaei, H., Huet, J.C., Henry, C., Da Costa, B., Eléouët, J.F. J. Gen. Virol. (2004) [Pubmed]
  4. Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II. Mazumder, B., Adhikary, G., Barik, S. Virology (1994) [Pubmed]
  5. Sequence and in vitro expression of the phosphoprotein gene of avian pneumovirus. Ling, R., Davis, P.J., Yu, Q., Wood, C.M., Pringle, C.R., Cavanagh, D., Easton, A.J. Virus Res. (1995) [Pubmed]
  6. Identification of temperature-sensitive mutations in the phosphoprotein of respiratory syncytial virus that are likely involved in its interaction with the nucleoprotein. Lu, B., Brazas, R., Ma, C.H., Kristoff, T., Cheng, X., Jin, H. J. Virol. (2002) [Pubmed]
  7. Molecular cloning and sequence analysis of the phosphoprotein, nucleocapsid protein, matrix protein and 22K (M2) protein of the ovine respiratory syncytial virus. Alansari, H., Potgieter, L.N. J. Gen. Virol. (1994) [Pubmed]
  8. Sequence comparison between the phosphoprotein mRNAs of human and bovine respiratory syncytial viruses identifies a divergent domain in the predicted protein. Mallipeddi, S.K., Samal, S.K. J. Gen. Virol. (1992) [Pubmed]
  9. Molecular epidemiology of subgroup C avian pneumoviruses isolated in the United States and comparison with subgroup a and B viruses. Shin, H.J., Cameron, K.T., Jacobs, J.A., Turpin, E.A., Halvorson, D.A., Goyal, S.M., Nagaraja, K.V., Kumar, M.C., Lauer, D.C., Seal, B.S., Njenga, M.K. J. Clin. Microbiol. (2002) [Pubmed]
  10. Requirement of casein kinase II-mediated phosphorylation for the transcriptional activity of human respiratory syncytial viral phosphoprotein P: transdominant negative phenotype of phosphorylation-defective P mutants. Mazumder, B., Barik, S. Virology (1994) [Pubmed]
  11. Sequence analysis of a functional polymerase (L) gene of bovine respiratory syncytial virus: determination of minimal trans-acting requirements for RNA replication. Yunus, A.S., Collins, P.L., Samal, S.K. J. Gen. Virol. (1998) [Pubmed]
  12. Sequence analysis of the nucleocapsid and phosphoprotein genes of avian pneumoviruses circulating in the US. Dar, A.M., Munir, S., Goyal, S.M., Abrahamsen, M.S., Kapur, V. Virus Res. (2001) [Pubmed]
  13. Profilin is required for viral morphogenesis, syncytium formation, and cell-specific stress fiber induction by respiratory syncytial virus. Bitko, V., Oldenburg, A., Garmon, N.E., Barik, S. BMC Microbiol. (2003) [Pubmed]
  14. Identification of subgroups of bovine respiratory syncytial virus. Baker, J.C., Wilson, E.G., McKay, G.L., Stanek, R.J., Underwood, W.J., Velicer, L.F., Mufson, M.A. J. Clin. Microbiol. (1992) [Pubmed]
 
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