Abstract
The Jeryl Lynn (JL) vaccine against mumps virus (MuV) contains two components, MuVJL5 and MuVJL2, which differ by over 400 nt. Due to the occurrence of bias in the direction of mutation, these differences and those found in nucleotide sequences of different isolates of the minor component in the vaccine (MuVJL2) might be due to the effect of ADAR-like deaminases on MuV grown in tissue-cultured cells. A molecular clone of MuVJL2 (pMuVJL2) and MuVJL2-specific helper plasmids were constructed in order to investigate molecular interactions between MuVJL5 and MuVJL2, to augment the existing molecular clone of MuVJL5 (pMuVJL5) and MuVJL5-specific helper plasmids. Genome and mRNA termini of MuVJL2 were characterized, and an unusual oligo-G insertion transcriptional editing event was detected near the F mRNA polyadenylation site of MuVJL2, but not of MuVJL5. Genes encoding glycoproteins of rMuVJL2 and rMuVJL5 have been exchanged to characterize the oligo-G insertion, which associated with the specific sequence of the F gene of MuVJL2 and not with any other genes or the RNA-dependent RNA polymerase of strain MuVJL2. The results indicate that a single G-to-A sequence change obliterates the co-transcriptional editing of the F mRNA and that this oligo-G insertion does not affect the growth of the virus.
Highlights
The Jeryl Lynn (JL) mumps virus (MuV) vaccine contains two different component strains, MuVJL5 and MuVJL2, that differ considerably in their nucleotide sequences (Amexis et al, 2002)
A further potential biased mutation event that may have occurred during passage of MuVJL2 and MuVJL5 is located in the 39 non-coding region of the N gene where there are nine changes between MuVJL5 and both MuVJL2 sequences, of which eight are T in both of the MuVJL2 sequences, but C in MuVJL5
Fig. 6. 39-Terminal sequences of F genes and transcripts of rMuVJL2(FJL5) and rMuVJL5(FJL2). (a, b) Sequence from rMuVJL2(FJL5); (c, d) sequence from rMuVJL5(FJL2). (a) and (c) show sequence electrochromatograms of the virion sequence of the F polyadenylation region cut to the first nucleotide difference between MuVJL2 and MuVJL5 in the small hydrophobic (SH) gene; (b) and (d) show the 39-terminal region of the F mRNA 2. rMuVJL2(FJL5) has the F sequence characteristic of rMuVJL5 and the SH sequence characteristic of rMuVJL2, and rMuVJL5(FJL2) has the F sequence characteristic of rMuVJL2 and the SH sequence characteristic of rMuVJL5
Summary
The Jeryl Lynn (JL) mumps virus (MuV) vaccine contains two different component strains, MuVJL5 and MuVJL2, that differ considerably in their nucleotide sequences (Amexis et al, 2002). The inner core consists of the non-segmented negative-strand viral RNA (length, 15 384 nt) associated with the nucleocapsid (N) protein, lesser amounts of the polymerase associated phospho- (P) protein and small amounts of the large (L) RNA-dependent RNA polymerase (RdRp) protein. The ribonucleoprotein (RNP) is surrounded by a host-derived membrane, which is spanned by two glycoproteins: the haemagglutinin–neuraminidase (HN) and fusion (F) proteins. On the inner face of the membrane is a membrane or matrix (M) protein that interacts with the cytoplasmic tails of the HN and F proteins and with the RNP. Two are derived from the second transcription unit, which encodes the nonstructural V protein directly and, after co-transcriptional
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