title: Comparison of L proteins of vaccine and wild-type measles viruses.
abstract: The nucleotide sequences of the large (L) genes of ten measles virus (MV) strains were determined. These strains included the Moraten and Rubeovax vaccine strains and their Edmonston wild-type (wt) progenitor, two additional vaccine strains and five genotypically divergent wt isolates. The nucleotide and predicted amino acid sequences were compared with six previously sequenced L genes and the number and location of variable amino acid positions were characterized. The recent wt isolates demonstrated the greatest amount of variability found to date in the highly conserved L protein. Three full-length wt L proteins were expressed in mammalian cells and their ability to form a complex with the MV phosphoprotein was demonstrated. While no set of amino acid substitutions associated consistently with wt or vaccine strains was identified, these data will provide a basis for the analysis of the activity of L proteins from vaccine and wt viruses in a functional assay.
authors.forename: B
authors.initials: B
authors.lastname: Bankamp
authors.forename: W J
authors.initials: WJ
authors.lastname: Bellini
authors.forename: P A
authors.initials: PA
authors.lastname: Rota
mesh_terms: D000595:Amino Acid Sequence; D008458:Measles Vaccine / Q000235:genetics*; D008459:Measles virus / Q000235:genetics*; D008969:Molecular Sequence Data; D017421:Sequence Analysis; D014764:Viral Proteins / Q000235:genetics*
chemical_list: D008458:Measles Vaccine; D014764:Viral Proteins