Disease relevance of HPIV3gp2

• Interaction between the nucleocapsid protein and the phosphoprotein of human parainfluenza virus 3. Mapping of the interacting domains using a two-hybrid system [1].
• This situation is unlike that with Sendai virus, a paramyxovirus, which has a nonstructural C protein encoded by a second overlapping reading frame near the 5' end of the mRNA for phosphoprotein [2].
• There was no other potential reading frame within the phosphoprotein gene of respiratory syncytial virus [2].
• Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3 [3].
• RNA-dependent RNA polymerases of single-stranded, negative-sense RNA viruses comprise a phosphoprotein (P) and a large protein [4].

High impact information on HPIV3gp2

• Mapping of the domains in P (603 amino acids) involved in the association with NP revealed that NH2-terminal 40 and COOH-terminal 20 amino acids are important for such association [1].
• The phosphoprotein (P) binding site resides in the N terminus of the L polymerase subunit of sendai virus [5].
• These studies suggest that like the primary, the alternate phosphorylation of the P protein is also dispensable for virus replication in cell cultures [6].
• Interestingly, the ability of the multiple site mutant of P (combo mutant has eight serine residues changed to alanine residues) to support efficient virus RNA synthesis suggests that the P protein has a high flexibility at least in its sequence and perhaps also in structure [6].
• Editing at an alternate site (AAUUGGAAAGGAAAGG), mRNA nucleotides 1121-1136, for accession of a conserved V cistron, which is present in a number of paramyxovirus P genes, was not found to occur in HPIV3 [7].

Chemical compound and disease context of HPIV3gp2

• Human parainfluenza virus type 3 phosphoprotein: identification of serine 333 as the major site for PKC zeta phosphorylation [8].

Biological context of HPIV3gp2

• However, there is no obvious conserved phosphorylation site in HPIV-1 P protein [4].
• RNA editing in the phosphoprotein gene of the human parainfluenza virus type 3 [7].
• The phosphoprotein (P) of human parainfluenza virus type 3 (HPIV 3) plays a central role in the viral genome RNA transcription and replication [3].
• The five viruses display amino acid sequence identity ranging from 58.6% for the phosphoprotein to 89.7% for the matrix protein [9].
• An analysis of the amino acid differences in each open reading frame revealed that of all the genes, the coding region of the M gene was the most highly conserved (1.1% amino acid variability), while the phosphoprotein (P) gene was the most variable (5.8% amino acid variability) [10].

Associations of HPIV3gp2 with chemical compounds

• Labelling of virus with [32P]orthophosphate disclosed one band with an Mr of 52K, corresponding to the phosphoprotein [11].
• Significantly, the P proteins from both viruses are constitutively and primarily phosphorylated at one serine and the phosphorylation of that serine is dependent on the presence of a proline on its carboxyl side [4].

Analytical, diagnostic and therapeutic context of HPIV3gp2

• Site-directed mutagenesis of the N terminus of L has identified amino acids important for binding P [5].
• The sequence of the mRNA encoding the phosphoprotein (P protein) of the human parainfluenza virus 3 (PF3) was determined by molecular cloning [12].

References