Alterations and diversity in the cytoplasmic tail of the fusion protein of subacute sclerosing panencephalitis virus strains isolated in Osaka, Japan

• Published in: Virus research Vol. 86; no. 1; pp. 123 - 131
• Main Authors: Ning, Xiaojun, Ayata, Minoru, Kimura, Masatsugu, Komase, Katsuhiro, Furukawa, Kyoko, Seto, Toshiyuki, Ito, Nobuhisa, Shingai, Masashi, Matsunaga, Isamu, Yamano, Tsunekazu, Ogura, Hisashi
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2002
• Subjects: Amino Acid Sequence; Fusion gene; Genetic Variation - genetics; Japan; Measles virus; Measles virus - genetics; Measles virus - isolation & purification; Measles virus - pathogenicity; Molecular Sequence Data; Mutation; Phylogeny; Sequence Alignment; Subacute Sclerosing Panencephalitis - virology; Subacute sclerosing panencephalitis virus; Viral Fusion Proteins - genetics; Japan; Mutation; Subacute sclerosing panencephalitis virus; Measles virus; Fusion gene
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/S0168-1702(02)00042-4

We determined the nucleotide sequence of the fusion (F) gene of three strains (Osaka-1, -2, and -3) of nonproductive variants of measles virus (MV). These viral strains were isolated in Osaka, Japan, from brain tissues of patients with subacute sclerosing panencephalitis (SSPE). Phylogenetic analysis revealed a close relationship among the three strains of SSPE virus. The cytoplasmic tail of the F protein, predicted from sequence analysis of the gene, is altered in all three SSPE strains when compared to the MV field strains. However, the extent and mode of alteration are different in each strain. The F protein of the Osaka-1 strain has six nonconservative amino acid substitutions and a 29-residue elongation of its cytoplasmic tail. The F protein of the Osaka-3 strain has two nonconservative substitutions and a 5-residue truncation of its C-terminus. Although the termination codon is not altered in the F protein of the Osaka-2 strain, five or six amino acids are changed in the cytoplasmic tail of the F protein of the two sibling viruses of this strain. The significance of the altered cytoplasmic domain of the SSPE viruses in the SSPE pathogenesis is discussed.