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单链骆驼科抗体存在下 Toscana 病毒核蛋白的结构柔韧性。

Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody.

机构信息

Université Aix-Marseille, Architecture et Fonction des Macromolécules Biologiques (AFMB)-UMR7257 CNRS, Case 925, 163 Avenue de Luminy, 13009 Marseille, France.

Unité des Virus Émergents (UVE: Aix-Marseille University-IRD 190-Inserm 1207), Marseille, France.

出版信息

Acta Crystallogr D Struct Biol. 2024 Feb 1;80(Pt 2):113-122. doi: 10.1107/S2059798324000196. Epub 2024 Jan 24.

DOI:10.1107/S2059798324000196
PMID:38265877
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10836398/
Abstract

Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and polymerizes through the N-terminus, which is presented as a highly flexible arm, as demonstrated in this article. The nucleoprotein exists in an open' or a closed' conformation. In the case of the closed conformation the flexible N-terminal arm folds over the RNA-binding cleft, preventing RNA adsorption. In the open conformation the arm is extended in such a way that both RNA adsorption and N polymerization are possible. In this article, single-crystal X-ray diffraction and small-angle X-ray scattering were used to study the N protein of Toscana virus complexed with a single-chain camelid antibody (VHH) and it is shown that in the presence of the antibody the nucleoprotein is unable to achieve a functional assembly to form a ribonucleoprotein complex.

摘要

细小病毒科核衣壳蛋白是病毒周期的主要结构和功能组成部分，可保护病毒 RNA 并介导必要的复制/转录过程。核蛋白（N）通过其球形核心与 RNA 结合，并通过呈现为高度灵活臂的 N 端聚合，如本文所示。核蛋白存在于“开放”或“闭合”构象中。在封闭构象中，灵活的 N 端臂折叠在 RNA 结合裂隙上，防止 RNA 吸附。在开放构象中，臂伸展，使得 RNA 吸附和 N 聚合都成为可能。在本文中，使用单晶 X 射线衍射和小角 X 射线散射研究了与单链骆驼科抗体（VHH）结合的托斯卡纳病毒的 N 蛋白，并表明在抗体存在的情况下，核蛋白无法实现功能性组装以形成核糖核蛋白复合物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/66f60ef83ba3/d-80-00113-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/ad9640543455/d-80-00113-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/a51d5dc8b129/d-80-00113-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/87f24bb79183/d-80-00113-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/66f60ef83ba3/d-80-00113-fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/ad9640543455/d-80-00113-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/a51d5dc8b129/d-80-00113-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/87f24bb79183/d-80-00113-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fe66/10836398/66f60ef83ba3/d-80-00113-fig4.jpg

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Brothers in Arms: Structure, Assembly and Function of Nucleoprotein.
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