2000年9月
Involvement of the zinc-binding capacity of Sendai virus V protein in viral pathogenesis
JOURNAL OF VIROLOGY
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- 巻
- 74
- 号
- 17
- 開始ページ
- 7834
- 終了ページ
- 7841
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1128/JVI.74.17.7834-7841.2000
- 出版者・発行元
- AMER SOC MICROBIOLOGY
The V protein of Sendai virus (SeV) is nonessential to virus replication in cell culture but indispensable to viral pathogenicity in mice. The highly conserved cysteine-rich zinc finger-like domain in its carboxyl terminus is believed to be responsible for this viral pathogenicity. in the present study, we showed that the cysteine-rich domain of the SeV V protein could actually bind zinc by using glutathione-S-transferase fusion proteins. When the seven conserved cysteine residues at positions 337, 341, 353, 355, 358, 362, and 365 were replaced individually, the zinc-binding capacities of the mutant proteins were greatly impaired, ranging from 22 to 68% of that of the wild type. We then recovered two mutant SeVs from cDNA, which have V-C341S and V-C365R mutations and represent maximal and minimal zinc-binding capacities among the corresponding mutant Fusion proteins, respectively. The mutant viruses showed viral protein synthesis and growth patterns similar to those of wild-type SeV in cultured cells. However, the mutant viruses were strongly attenuated in mice in a way similar to that of SeV V-Delta C, which has a truncated V protein lacking the cysteine-rich domain, by exhibiting earlier viral clearance from the mouse lung and less virulence to mice. We therefore conclude that the zinc-binding capacity of the V protein is involved in viral pathogenesis.
- リンク情報
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- DOI
- https://doi.org/10.1128/JVI.74.17.7834-7841.2000
- CiNii Articles
- http://ci.nii.ac.jp/naid/80011977311
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/10933690
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000088866500016&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1128/JVI.74.17.7834-7841.2000
- ISSN : 0022-538X
- CiNii Articles ID : 80011977311
- PubMed ID : 10933690
- Web of Science ID : WOS:000088866500016