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

The molecular basis for the severity and rapid spread of the COVID-19 disease caused by 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 reso...

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Bibliographic Details
Published in:bioRxiv 2020-08
Main Authors: Flower, Thomas G, Buffalo, Cosmo Z, Hooy, Richard M, Allaire, Marc, Ren, Xuefeng, Hurley, James H
Format: Article
Language:English
Subjects:
Coronaviruses
COVID-19
Crystal structure
Crystallography
Crystals
Dimerization
Immune evasion
Immune response
Interfaces
Severe acute respiratory syndrome coronavirus 2
X-ray crystallography
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Summary:The molecular basis for the severity and rapid spread of the COVID-19 disease caused by 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 ~60 residue core similar to SARS-CoV 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 non-covalent 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. Competing Interest Statement The authors have declared no competing interest.
DOI:10.1101/2020.08.27.270637