Cryo-EM structure of a herpesvirus capsid at 3.1 Å-Reference-Cited by-全球学者库

Cryo-EM structure of a herpesvirus capsid at 3.1 Å

Published:2018-04-06 Issue:6384 Volume:360 Page:
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Yuan Shuai¹²^ORCID,Wang Jialing¹²^ORCID,Zhu Dongjie¹³^ORCID,Wang Nan¹²^ORCID,Gao Qiang¹⁴,Chen Wenyuan⁵^ORCID,Tang Hao⁵,Wang Junzhi⁶,Zhang Xinzheng¹²^ORCID,Liu Hongrong⁵^ORCID,Rao Zihe¹²⁷⁸⁹^ORCID,Wang Xiangxi¹²^ORCID

Affiliation:

1. National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.

2. University of Chinese Academy of Sciences, Beijing, 100049, China.

3. School of Life Science, University of Science and Technology of China, Hefei, 230026, China.

4. Sinovac Biotech Co., Ltd., Beijing, 100085, China.

5. College of Physics and Information Science, Synergetic Innovation Center for Quantum Effects and Applications, Hunan Normal University, Changsha, 410081, Hunan, China.

6. National Institutes for Food and Drug Control, No. 2, Tiantanxili, Beijing, 100050, China.

7. Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, 201210, China.

8. State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300353, China.

9. Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China.

Abstract

Focusing in on herpesvirus The herpesvirus family includes herpes simplex virus type 1 (HSV-1), which causes cold sores, and type 2 (HSV-2), which causes genital herpes. Herpesviruses comprise a large DNA genome enclosed in a large and complex protein cage called a capsid (see the Perspective by Heldwein). Dai and Zhou used electron microscopy to determine a high-resolution structure of the HSV-1 capsid bound to the tegument proteins that occupy the space between the capsid and the nuclear envelope. The structure suggests how these components may play a role in viral transport. Yuan et al. describe a higher-resolution structure of an HSV-2 capsid, providing insight into how the shell assembles and is stabilized. Science , this issue p. eaao7298 , p. eaao7283 ; see also p. 34

Funder

National Science Foundation of China

the Strategic Priority Research Program

the 973 Projects

the National Key Research and Development Program of MOST

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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