SARS-CoV-2 structural coverage map reveals viral protein assembly, mimicry, and hijacking mechanisms

Seán I. O’Donoghue, Andrea Schafferhans, Neblina Sikta, Christian Stolte, Sandeep Kaur, Bosco K. Ho, Stuart Anderson, James B. Procter, Christian Dallago, Nicola Bordin, Matt Adcock, Burkhard Rost

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

20 Zitate (Scopus)

Abstract

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.

OriginalspracheEnglisch
Aufsatznummere10079
FachzeitschriftMolecular Systems Biology
Jahrgang17
Ausgabenummer9
DOIs
PublikationsstatusVeröffentlicht - Sept. 2021

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