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

Autor: Flower, Thomas G., Buffalo, Cosmo Z., Hooy, Richard M., Allaire, Marc, Ren, Xuefeng, Hurley, James H.
Rok vydání: 2021
Předmět:
Zdroj: Proceedings of the National Academy of Sciences of the United States of America, vol 118, iss 2
Proceedings of the National Academy of Sciences
bioRxiv
article-version (status) pre
article-version (number) 1
Popis: 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.
Databáze: OpenAIRE