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-Structure paper
タイトル | Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus. |
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ジャーナル・号・ページ | PNAS Nexus, Vol. 2, Issue 4, Page pgad120, Year 2023 |
掲載日 | 2023年4月6日 |
著者 | Shangfan Hu / Yoko Fujita-Fujiharu / Yukihiko Sugita / Lisa Wendt / Yukiko Muramoto / Masahiro Nakano / Thomas Hoenen / Takeshi Noda / |
PubMed 要旨 | Lloviu virus (LLOV) is a novel filovirus detected in Schreiber's bats in Europe. The isolation of the infectious LLOV from bats has raised public health concerns. However, the virological and ...Lloviu virus (LLOV) is a novel filovirus detected in Schreiber's bats in Europe. The isolation of the infectious LLOV from bats has raised public health concerns. However, the virological and molecular characteristics of LLOV remain largely unknown. The nucleoprotein (NP) of LLOV encapsidates the viral genomic RNA to form a helical NP-RNA complex, which acts as a scaffold for nucleocapsid formation and de novo viral RNA synthesis. In this study, using single-particle cryoelectron microscopy, we determined two structures of the LLOV NP-RNA helical complex, comprising a full-length and a C-terminally truncated NP. The two helical structures were identical, demonstrating that the N-terminal region determines the helical arrangement of the NP. The LLOV NP-RNA protomers displayed a structure similar to that in the Ebola and Marburg virus, but the spatial arrangements in the helix differed. Structure-based mutational analysis identified amino acids involved in the helical assembly and viral RNA synthesis. These structures advance our understanding of the filovirus nucleocapsid formation and provide a structural basis for the development of antifiloviral therapeutics. |
リンク | PNAS Nexus / PubMed:37124400 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0356 - 3.2 Å |
構造データ | EMDB-34016, PDB-7ypw: EMDB-34049, PDB-7yr8: |
由来 |
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キーワード | VIRAL PROTEIN / nucleoprotein |