Key result
Cryo-electron microscopy determined the 3.1 Å resolution structure of the SARS-CoV NSP12 polymerase bound to its essential co-factors NSP7 and NSP8.
Why the study?
Coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins to replicate and transcribe the viral genome following the emergence of highly pathogenic strains.
The structure of the SARS-CoV NSP12 polymerase complex provides insights into coronavirus RNA-synthesis machinery and a template for antiviral drug design.
Provides 3.1 Å structure of SARS-CoV polymerase holoenzyme; leaves open utility for designing targeted antivirals.
Recent history is punctuated by the emergence of highly pathogenic coronaviruses such as SARS- and MERS-CoV into human circulation. Upon infecting host cells, coronaviruses assemble a multi-subunit RNA-synthesis complex of viral non-structural proteins (NSP) responsible for the replication and transcription of the viral genome. Here, we present the 3.1 Å resolution structure of the SARS-CoV NSP12 polymerase bound to its essential co-factors, NSP7 and NSP8, using single particle cryo-electron microscopy. NSP12 possesses an architecture common to all viral polymerases as well as a large N-terminal extension containing a kinase-like fold and is unexpectedly bound by two NSP8 co-factors. This structure illuminates the assembly of the coronavirus core RNA-synthesis machinery, provides key insights into NSP12 polymerase catalysis and fidelity and acts as a template for the design of novel antiviral therapeutics.
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Kirchdoerfer et al. (2019) studied SARS-CoV. Cryo-electron microscopy was evaluated on Structure determination of the SARS-CoV NSP12 polymerase bound to NSP7 and NSP8. Cryo-electron microscopy determined the 3.1 Å resolution structure of the SARS-CoV NSP12 polymerase bound to its essential co-factors NSP7 and NSP8.
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