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

Thomas G Flower1,2, Cosmo Z Buffalo1,2, Richard M Hooy1,2

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.

Proceedings of the National Academy of Sciences of the United States of America
|December 28, 2020
PubMed

Insights

The SARS-CoV-2 ORF8 protein

Area of Science:

  • Structural biology
  • Virology
  • Immunology

Background:

  • The molecular mechanisms behind COVID-19 severity and spread remain unclear.
  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) accessory proteins, like ORF8, may influence viral pathogenesis.
  • ORF8 is implicated in modulating host immune responses.

Purpose of the Study:

  • To elucidate the structural basis of SARS-CoV-2 ORF8.
  • To understand how ORF8's unique structural features contribute to its function.

Main Methods:

  • X-ray crystallography was employed to determine the 3D structure of SARS-CoV-2 ORF8.
  • Structural analysis focused on identifying unique features and potential functional interfaces.

Main Results:

  • The crystal structure of SARS-CoV-2 ORF8 was resolved to 2.04-Å resolution.
  • ORF8 possesses a core structure homologous to ORF7a but includes two unique dimerization interfaces.
  • A covalent disulfide-linked dimer and a noncovalent dimer are formed via SARS-CoV-2-specific sequences.

Conclusions:

  • SARS-CoV-2 ORF8 can form unique large-scale assemblies distinct from SARS-CoV ORF8.
  • These structural assemblies may underlie ORF8's potential roles in immune suppression and evasion.
  • Understanding ORF8 structure provides insights into SARS-CoV-2 pathogenesis.
Keywords:
COVID-19SARS-CoV-2X-ray crystallography

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