Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins

Sugiyama, Aoi; Nomai, Tomo; Jiang, Xinxin; Minami, Miku; Yao, Min; Maenaka, Katsumi; Ito, Naoto; Gooley, Paul R.; Moseley, Gregory W.; Ose, Toyoyuki

Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins

Sugiyama, Aoi; Nomai, Tomo; Jiang, Xinxin et al.

Biochemical and biophysical research communications, 2020, 529(2), 507-512

Permalink : https://hdl.handle.net/2115/82124

このアイテムのアクセス数:634件（2026-08-14 01:16 集計）

閲覧可能ファイル

ファイル	フォーマット	サイズ	閲覧回数	説明
Biochem. Biophys. Res. Commun.529-2_507-512	pdf	6.82 MB	515
Supplementary_methods	pdf	79.7 KB	189

論文情報

ファイル出力 EndNote Basic出力 Mendeley出力

アクセス権	open access
URI	https://hdl.handle.net/2115/82124
タイトル	Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins
著者	Sugiyama, Aoi ; Nomai, Tomo ; Jiang, Xinxin ; Minami, Miku ; Yao, Min ; Maenaka, Katsumi ; Ito, Naoto ; Gooley, Paul R. ; Moseley, Gregory W. ; Ose, Toyoyuki
著者名 Sugiyama, Aoi
著者名 Nomai, Tomo
著者名 Jiang, Xinxin
著者名 Minami, Miku
著者名 Yao, Min
著者名 Maenaka, Katsumi
著者名 Ito, Naoto
著者名 Gooley, Paul R.
著者名 Moseley, Gregory W.
e-Rad_Researcher 80380525 著者名 Ose, Toyoyuki
言語	英語
キーワード	Lyssavirus
	P protein
	Immune evasion
	JAK-STAT pathway
	Hydrophobic interaction
発行日	2020-08-20
出版者	Elsevier
収録物名	Biochemical and biophysical research communications
巻(号)	529(2)
ページ	507-512
抄録	Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species. (C) 2020 Elsevier Inc. All rights reserved.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
権利情報	©2020. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
PISSN	0006-291X
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.bbrc.2020.05.195