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Functional Importance of the Coiled-Coil of the Ebola Virus Glycoprotein

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/28145

Title: Functional Importance of the Coiled-Coil of the Ebola Virus Glycoprotein
Authors: Watanabe, Shinji Browse this author
Takada, Ayato Browse this author
Watanabe, Tokiko Browse this author
Ito, Hiroshi Browse this author
Kida, Hiroshi Browse this author
Kawaoka, Yoshihiro Browse this author
Issue Date: Nov-2000
Publisher: American Society for Microbiology
Journal Title: Journal of Virology
Volume: 74
Issue: 21
Start Page: 10194
End Page: 10201
Abstract: Ebola virus contains a single glycoprotein (GP) that is responsible for receptor binding and membrane fusion and is proteolytically cleaved into disulfide-linked GP1 and GP2 subunits. The GP2 subunit possesses a coiled-coil motif, which plays an important role in the oligomerization and fusion activity of other viral GPs. To determine the functional significance of the coiled-coil motif of GP2, we examined the effects of peptides corresponding to the coiled-coil motif of GP2 on the infectivity of a mutant vesicular stomatitis virus (lacking the receptor-binding/fusion protein) pseudotyped with the Ebola virus GP. A peptide corresponding to the C-terminal helix reduced the infectivity of the pseudotyped virus. We next introduced alanine substitutions into hydrophobic residues in the coiled-coil motif to identify residues important for GP function. None of the substitutions affected GP oligomerization, but some mutations, two in the N-terminal helix and all in the C-terminal helix, reduced the ability of GP to confer infectivity to the mutant vesicular stomatitis virus without affecting the transport of GP to the cell surface, its incorporation into virions, and the production of virus particles. These results indicate that the coiled-coil motif of GP2 plays an important role in facilitating the entry of Ebola virus into host cells and that peptides corresponding to this region could act as efficient antiviral agents.
Rights: Copyright © 2000 American Society for Microbiology
Type: article
URI: http://hdl.handle.net/2115/28145
Appears in Collections:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 喜田 宏

 

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