Journal article

Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9

Dene R Littler, Benjamin S Gully, Rhys N Colson, Jamie Rossjohn

iScience | CELL PRESS | Published : 2020


Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and viral genomic RNA reproduction. We sought to better characterize the SARS-CoV-2 Nsp9 and subsequently solved its X-ray crystal structure, in an apo form and, unexpectedly, in a peptide-bound form with a sequence originating from a rhinoviral 3C protease sequence (LEVL). The SARS-CoV-2 Nsp9 structure revealed the high level of structural conservation within the Nsp9 family. The exogenous peptide binding site is close to the dimer interface and impacted..

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University of Melbourne Researchers


Funding Acknowledgements

Funding for the work originated from the Australian Research Council Centre of Excellence for Advanced Molecular Imaging. This research was undertaken in part using the MX2 beamline at the Australian Synchrotron, part of ANSTO, and made use of the Australian Cancer Research Foundation (ACRF) detector. Additionally, we thank Dr. Geoffrey Kong of the Monash Molecular Crystallisation Facility for his assistance with crystallographic screening and optimization. We thank A. Riboldi-Tunnicliffe for assistance with data collection and J. Whisstock and G. Watson for advice on the manuscript.