Structure of SARS-CoV-2 ORF8, a rapidly evolving coronavirus protein implicated in immune evasion
| Autor: | Flower, Thomas G, Buffalo, Cosmo Z, Hooy, Richard M, Allaire, Marc, Ren, Xuefeng, Hurley, James H |
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| Rok vydání: | 2020 |
| Předmět: |
Prevention
viruses fungi Pneumonia biochemical phenomena metabolism and nutrition Vaccine Related body regions Infectious Diseases Emerging Infectious Diseases Good Health and Well Being Biodefense Pneumonia & Influenza 2.1 Biological and endogenous factors Aetiology skin and connective tissue diseases Lung |
| Zdroj: | bioRxiv, vol 1, iss 08-31 |
| Popis: | The 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 Å 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. |
| Databáze: | OpenAIRE |
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