|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine >
Peer-reviewed Journal Articles, etc >
Functional Importance of the Coiled-Coil of the Ebola Virus Glycoprotein
| Title: | Functional Importance of the Coiled-Coil of the Ebola Virus Glycoprotein |
| Authors: | Watanabe, Shinji Browse this author | | Takada, Ayato Browse this author →KAKEN DB | | Watanabe, Tokiko Browse this author | | Ito, Hiroshi Browse this author | | Kida, Hiroshi Browse this author →KAKEN DB | | Kawaoka, Yoshihiro Browse this author →KAKEN DB |
| Issue Date: | Nov-2000 |
| Publisher: | American Society for Microbiology |
| Journal Title: | Journal of Virology |
| Volume: | 74 |
| Issue: | 21 |
| Start Page: | 10194 |
| End Page: | 10201 |
| Publisher DOI: | 10.1128/JVI.74.21.10194-10201.2000 |
| PMID: | 11024148 |
| 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: | 獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 喜田 宏
|
