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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/82124

Title: Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins
Authors: Sugiyama, Aoi Browse this author
Nomai, Tomo Browse this author
Jiang, Xinxin Browse this author
Minami, Miku Browse this author
Yao, Min Browse this author
Maenaka, Katsumi Browse this author
Ito, Naoto Browse this author
Gooley, Paul R. Browse this author
Moseley, Gregory W. Browse this author
Ose, Toyoyuki Browse this author →KAKEN DB
Keywords: Lyssavirus
P protein
Immune evasion
JAK-STAT pathway
Hydrophobic interaction
Issue Date: 20-Aug-2020
Publisher: Elsevier
Journal Title: Biochemical and biophysical research communications
Volume: 529
Issue: 2
Start Page: 507
End Page: 512
Publisher DOI: 10.1016/j.bbrc.2020.05.195
Abstract: 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.
Rights: ©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/
http://creativecommons.org/licenses/by-nc-nd/4.0/
Type: article (author version)
URI: http://hdl.handle.net/2115/82124
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 尾瀬 農之

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