SARS-CoV-2 structural coverage map reveals viral protein assembly, mimicry, and hijacking mechanisms
We modeled 3D structures of all SARS-CoV-2 proteins, generating 2,060 models that span 69% of the viral proteome and provide details not available elsewhere. We found that 6% of the proteome mimicked human proteins, while 7% was implicated in hijacking mechanisms that reverse post-translational modifications, block host translation, and disable host defenses; a further 29% self-assembled into heteromeric states that provided insight into how the viral replication and translation complex forms. To make these 3D models more accessible, we devised a structural coverage map, a novel visualization method to show what is-and is not-known about the 3D structure of the viral proteome. We integrated the coverage map into an accompanying online resource (https://aquaria.ws/covid) that can be used to find and explore models corresponding to the 79 structural states identified in this work. The resulting Aquaria-COVID resource helps scientists use emerging structural data to understand the mechanisms underlying coronavirus infection and draws attention to the 31% of the viral proteome that remains structurally unknown or dark.
|ISBN||1744-4292 (Electronic) 1744-4292 (Linking)|
|Authors||O'Donoghue, S. I.; Schafferhans, A.; Sikta, N.; Stolte, C.; Kaur, S.; Ho, B. K.; Anderson, S.; Procter, J. B.; Dallago, C.; Bordin, N.; Adcock, M.; Rost, B.|
|Responsible Garvan Author|
|Publisher Name||Molecular Systems Biology|
|URL link to publisher's version||https://www.ncbi.nlm.nih.gov/pubmed/34519429|