Disease relevance of P

• RNA interference with measles virus N, P, and L mRNAs efficiently prevents and with matrix protein mRNA enhances viral transcription [1].
• The P gene was shown to have the capacity to encode three distinct proteins, P, V and C, in analogy to other morbilliviruses [2].
• When the nucleotide and deduced amino acid sequences of the N, P, V and C genes were aligned with corresponding sequences of other established members of the morbillivirus genus, compelling homology was found between PDV and canine distemper virus (CDV), whereas there was markedly less similarity between PDV and measles virus or rinderpest virus [2].
• CONCLUSIONS: This study shows that discrimination between SSPE and MS can be achieved in doubtful cases by IEF using MV-N, P and F proteins [3].
• The replication assay was also used to show that the N, P and L proteins of NiV recognize cis-acting sequences in the genomic termini of Hendra virus (HeV) but not measles virus [4].

High impact information on P

• The measles virus (MV) phosphoprotein (P) gene encodes two known proteins, P (Mr approximately 70,000), involved in viral transcription, and, in a different reading frame, C (Mr approximately 20,000) [5].
• By a combination of cDNA cloning, cDNA and RNA sequencing, and in vitro translation, we demonstrate here that the MV P gene also expresses a third product (Mr approximately 46,000) containing the amino-terminal region of P but a different, cysteine-rich carboxy-terminal motif [5].
• The viral polymerase associates with the nucleocapsid through a small, trihelical binding domain at the carboxyl terminus of the phosphoprotein (P) [6].
• Molecular mimicry in virus infection: crossreaction of measles virus phosphoprotein or of herpes simplex virus protein with human intermediate filaments [7].
• Using monoclonal antibodies, we demonstrate that the phosphoprotein of measles virus and a protein of herpes simplex virus type 1 crossreact with an intermediate filament protein of human cells [7].

Chemical compound and disease context of P

• Overall, the NP and in particular the F proteins of the morbilliviruses showed a high degree of epitopic homology; the P and M proteins showed a partial epitopic homology, with the greatest variation between the M proteins of CDV and MV; the H proteins showed a low degree of epitopic homology and then only between MV and RPV [8].
• Target sequences of measles virus nucleocapsid (N) and phosphoprotein genes were detected within measles virus infected Vero cells, both in suspension and in formalin-fixed sections, that had been treated by in situ reverse transcription and 30 cycles of direct in situ PCR [9].
• 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 [10].
• An edited mRNA transcribed from the phosphoprotein (P) gene of measles virus (MV) has been predicted to encode a cysteine-rich protein designated V [11].
• Measles virus (MV) inserts one guanosine (G) residue at a specific site in a subpopulation of the mRNA transcribed from the phosphoprotein (P) gene to produce V mRNA [12].

Biological context of P

• On the basis of the alignments presented, the estimated amino acid sequence similarity between the N and P genes of PDV and CDV was 84% and 76%, respectively [2].
• In contrast, all of the mutants retained the ability to form the L-L complex, so different amino acids are involved in the L and P binding sites on L [13].
• Identification of three lineages of wild measles virus by nucleotide sequence analysis of N, P, M, F, and L genes in Japan [14].
• These results imply that MV P is a substrate for tyrosine phosphorylation by cellular tyrosine kinase(s) [15].
• The clinical, virological, and histopathological signs in rabbits infected with the two new recombinant viruses did not differ significantly; therefore, the RPV P gene was considered to be a key determinant of cross-species pathogenicity [16].

Anatomical context of P

• Groups of monoclonal antibodies against measles virus nucleoprotein (NP), phosphoprotein (P), matrix (M), hemagglutinin (H) and fusion (F) components were used for characterization of 5 persistently infected cell lines [17].
• Our results indicate that a specific signal to an epitope on the plasma membrane (monoclonal antibody measles virus hemagglutinin) can alter the expression of measles virus phosphoprotein and membrane protein, both polypeptides present in the cytoplasm of infected cells [18].
• MV glycoproteins, the fusion protein (F) and hemagglutinin (H), the matrix protein (M), and the phosphoprotein (P), which is part of the viral ribonucleoprotein complex, were all sorted to the dendrites [19].
• Hemagglutinin (H) and phosphoprotein expressed in persistently infected IC-21 cells had retarded migration in SDS-PAGE gels when compared to these proteins expressed in Vero cells [20].
• Infection of cells with the virus recombinant resulted in the formation of cytoplasmic inclusions in which the nucleoprotein and the phosphoprotein colocalized [21].

Associations of P with chemical compounds

• These cross-reactivities and type-specific reactions were obtained with the internal viral proteins (M, P and NP) [8].
• To investigate whether cellular tyrosine kinases can bind and phosphorylate P, a solid phase kinase assay was employed [15].
• We show that N(TAIL2) has lost the ability to bind to P, thus supporting the hypothesis that the alpha-MoRE may play a role in binding to P. We have further analyzed the alpha-helical propensities of N(TAIL2) and N(TAIL) using circular dichroism in the presence of 2,2,2-trifluoroethanol [22].
• We speculate that the glutamic acid at position 192 of the measles phosphoprotein is a critical immunogenicity factor and may influence the antigenicity of the naturally processed HLA class II MV-P1 epitope [23].

Analytical, diagnostic and therapeutic context of P

• To identify amino acids important for binding P and L, site-directed mutagenesis of the L-408 protein was performed [13].
• Immunofluorescence analysis of measles virus- and RS virus-infected cells with this monoclonal antibody showed qualitatively different staining patterns which indicated that the antigen involved in cross-reaction was the RS virus nucleoprotein or phosphoprotein [24].
• Monoclonal antibodies to the hemagglutinin protein, fusion protein, phosphoprotein, matrix protein, and nucleoprotein of measles virus were evaluated as detector antibodies in capture enzyme immunoassays (EIAs) for the detection of specific serum immunoglobulin G (IgG), IgA, and IgM antibodies to measles virus [25].
• The humoral immune response in sera and cerebrospinal fluids (CSFs) of dogs with various forms of canine distemper virus (CDV)-induced encephalitis was assessed by immunoprecipitation of radiolabelled nucleocapsid, phosphoprotein, membrane (M), haemagglutinin and fusion proteins [26].
• Sequence analysis and editing of the phosphoprotein (P) gene of rinderpest virus [27].

References