Structure of SARS-CoV-2 ORF8, a rapidly evolving immune evasion protein

被引：168

作者：

Flower, Thomas G. ^{[1
,2
]}

Buffalo, Cosmo Z. ^{[1
,2
]}

Hooy, Richard M. ^{[1
,2
]}

Allaire, Marc ^{[3
]}

Ren, Xuefeng ^{[1
,2
]}

Hurley, James H. ^{[1
,2
,3
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Calif Inst Quantitat Biosci, Berkeley, CA 94720 USA

[3] Lawrence Berkeley Natl Lab, Mol Biophys & Integrated Bioimaging Div, Berkeley, CA 94720 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2021年 / 118卷 / 02期

关键词：

X-ray crystallography; SARS-CoV-2; COVID-19; CORONAVIRUS;

D O I：

10.1073/pnas.2021785118

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The molecular basis for the severity and rapid spread of the COVID-19 disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is largely unknown. ORF8 is a rapidly evolving accessory protein that has been proposed to interfere with immune responses. The crystal structure of SARS-CoV-2 ORF8 was determined at 2.04-angstrom resolution by X-ray crystallography. The structure reveals a similar to 60-residue core similar to SARS-CoV-2 ORF7a, with the addition of two dimerization interfaces unique to SARS-CoV-2 ORF8. A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, 73YIDI76. Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities.

引用

页数：6

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