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

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-

SUBMITTER: Flower TG 

PROVIDER: S-EPMC7812859 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature