A I131V Substitution in the Fusion Glycoprotein of Human Parainfluenza Virus Type 1 Enhances Syncytium Formation and Virus Growth

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  • Fukushima Keijo
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Takahashi Tadanobu
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Takaguchi Masahiro
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Ito Seigo
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Suzuki Chihiro
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Agarikuchi Takashi
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Kurebayashi Yuuki
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Minami Akira
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
  • Suzuki Takashi
    Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka

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<p>Human parainfluenza virus type 1 (hPIV1) has two spike glycoproteins, the hemagglutinin-neuraminidase (HN) glycoprotein as a receptor-binding protein and the fusion (F) glycoprotein as a membrane-fusion protein. The F glycoprotein mediates both membrane fusion between the virus and cell and membrane fusion between cells, called syncytium formation. Wild-type C35 strain (WT) of hPIV1 shows little syncytium formation of infected cells during virus growth. In the present study, we isolated a variant virus (Vr) from the WT that showed enhanced syncytium formation of infected cells by using our previously established hPIV1 plaque formation assay. Vr formed a larger focus and showed increased virus growth compared with WT. Sequence analysis of the spike glycoprotein genes showed that the Vr had a single amino acid substitution of Ile to Val at position 131 in the fusion peptide region of the F glycoprotein without any substitutions of the HN glycoprotein. The Vr F glycoprotein showed enhanced syncytium formation in F and HN glycoprotein-expressing cells. Additionally, expression of the Vr F glycoprotein increased the focus area of the WT-infected cells. The single amino acid substitution at position 131 in the F glycoprotein of hPIV1 gives hPIV1 abilities to enhance syncytium formation and increase cell-to-cell spread. The present study supports the possibility that hPIV1 acquires increased virus growth in vitro from promotion of direct cell-to-cell transmission by syncytium formation.</p>

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