Skip to main content
eScholarship
Open Access Publications from the University of California

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

  • Author(s): Flower, Thomas G;
  • Buffalo, Cosmo Z;
  • Hooy, Richard M;
  • Allaire, Marc;
  • Ren, Xuefeng;
  • Hurley, James H
  • et al.
Abstract

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-Å resolution by X-ray crystallography. The structure reveals a ∼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.

Main Content
For improved accessibility of PDF content, download the file to your device.
Current View