Phosphoprotein and nucleocapsid protein evolution of vesicular stomatitis virus New Jersey

Abstract

The entire phosphoprotein (P) and nucleocapsid (N) protein gene sequences and deduced amino acid sequences for 18 selected vesicular stomatitis virus isolates representative of the natural genetic diversity within the New Jersey serotype are reported. Phylogenetic analysis of the data using maximum parsimony allowed construction of evolutionary trees for the individual genes and the combined N, P, and glycoprotein (G) genes of these viruses. Virtually identical rates of nucleotide substitutions were found for each gene, indicating that evolution of these genes occurs at essentially the same rate. Although up to 19 and 17% sequence differences were evident in the P and N genes, respectively, no variation in gene length or evidence of recombinational rearrangements was found. However, striking evolutionary differences were observed among the amino acid sequences of vesicular stomatitis virus New Jersey N, P, and G proteins. The N protein amino acid sequence was the most highly conserved among the different isolates, indicating strong functional and structural constraints. Conversely, the P protein amino acid sequences were highly variable, indicating considerably fewer constraints or greater evolutionary pressure on the P protein. Much of the remarkable amino acid variability of the P protein resided in a hypervariable domain located between amino acids 153 and 205. The variability within this region would be consistent with it playing a structural role as a spacer to maintain correct conformational presentation of the separate active domains of this multifunctional protein. In marked contrast, the adjacent domain I of the P protein (previously thought to be under little evolutionary constraint) contained a highly conserved region. The colocalization of a short, potentially functional overlapping open reading frame to this region may explain this apparent anomaly.

Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II.

“…A protein possessing two closely located sites that are phosphorylated independently with identical functional effect has not, to our knowledge, been found previously. Both sites seem to be advantageous, since they are rigorously conserved through extensive evolutionary change (Bilsel et al, 1990;Nichol et al, 1993), raising the question of what function this apparent duplication might serve. Two separate answers may be suggested.…”

Lyssavirus P Gene Characterisation Provides Insights into the Phylogeny of the Genus and Identifies Structural Similarities and Diversity within the Encoded Phosphoprotein

“…Evidence for the selective retention of VSV C protein ORFs included a demonstration that mutation rates of the third base position of the P ORF, corresponding to the second base position of the C ORF, were lower than expected over the region of ORF overlap (Bilsel et al, 1990). Since the alternate ORF identified in the lyssavirus P gene was in the same relative position as that of the VSV C ORF, analyses of base substitution patterns were performed to investigate whether this ORF was being selectively retained by RABVs.…”

Characterization of the Sendai virus V protein with an anti-peptide antiserum

“…By analogy to the rhabdovirus VSV, whose L gene and that of the paramyxoviruses are thought to share a common ancestor (Poch et at, 1989), L is the actual polymerase, and capping and poly(A) formation of mRNAs are thought to map to this protein as well (Banerjee, 1987) . The VSV counterpart to the paramyxovirus P protein is NS, which has recently been referred to as P (Herman, 1986 ;Bilsel et at, 1990), as NS (nonstructural) is a misnomer . The paramyxovirus and rhabdovirus P proteins are not related by sequence homology or size, but are organized similarly .…”