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
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- Takahashi Tadanobu
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Takaguchi Masahiro
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Ito Seigo
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Suzuki Chihiro
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Agarikuchi Takashi
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Kurebayashi Yuuki
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Minami Akira
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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- Suzuki Takashi
- Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka
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Abstract
<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>
Journal
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- Biological and Pharmaceutical Bulletin
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Biological and Pharmaceutical Bulletin 42 (5), 827-832, 2019-05-01
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390001288134959488
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- NII Article ID
- 130007641461
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- NII Book ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL BIB ID
- 029657872
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- PubMed
- 31061326
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed