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Structure of SARS-CoV-2 ORF8 accessory proteinStructure of SARS-CoV-2 ORF8 accessory protein
Structural highlights
Function[NS8_SARS2] May play a role in host-virus interaction. Publication Abstract from PubMedThe 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 A 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, 73 YIDI 76 . 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. Structure of SARS-CoV-2 ORF8, a rapidly evolving coronavirus protein implicated in immune evasion.,Flower TG, Buffalo CZ, Hooy RM, Allaire M, Ren X, Hurley JH bioRxiv. 2020 Aug 27. doi: 10.1101/2020.08.27.270637. PMID:32869027[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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