Structure and assembly of double-headed Sendai virus nucleocapsids

Na Zhang; Hong Shan; Mingdong Liu; Tianhao Li; Rui Luo; Liuyan Yang; Lei Qi; Xiaofeng Chu; Xin Su; Rui Wang; Yunhui Liu; Wenzhi Sun; Qing-Tao Shen

doi:10.1038/s42003-021-02027-y

Communications Biology (Apr 2021)

Structure and assembly of double-headed Sendai virus nucleocapsids

Na Zhang,
Hong Shan,
Mingdong Liu,
Tianhao Li,
Rui Luo,
Liuyan Yang,
Lei Qi,
Xiaofeng Chu,
Xin Su,
Rui Wang,
Yunhui Liu,
Wenzhi Sun,
Qing-Tao Shen

Affiliations

Na Zhang: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Hong Shan: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Mingdong Liu: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Tianhao Li: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Rui Luo: State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University
Liuyan Yang: State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University
Lei Qi: Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology
Xiaofeng Chu: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Xin Su: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Rui Wang: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Yunhui Liu: iHuman Institute, School of Life Science and Technology, ShanghaiTech University
Wenzhi Sun: Chinese Institute for Brain Research
Qing-Tao Shen: iHuman Institute, School of Life Science and Technology, ShanghaiTech University

DOI: https://doi.org/10.1038/s42003-021-02027-y
Journal volume & issue: Vol. 4, no. 1
pp. 1 – 10

Abstract

Read online

The authors present the reconstruction of the Sendai Virus N-RNA complex at atomic resolution, including the helical part and a clam-shaped joint, resolved to 2.9 and 3.9 Å respectively, via cryo-EM. They also demonstrate the presence of an additional, ring like structural motif stabilising Nprotein interactions.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

About the journal