IUCr journals

Structural genomics of the SARS coronavirus: preliminary crystallographic study of the Nsp9 protein

Acta Cryst. (2003). D59, 1628–1631

[Figure 5] Optimized crystals of the SARS-CoV Nsp9 protein. An electron microscopy view of a coronavirus is displayed in the background (courtesy of Prof. McNulty, Queen’s U., Belfast, UK)

The recent epidemics of Severe Acute Respiratory Syndrome (SARS) represent a real paradigm for emerging viral pathogens. The etiologic agent of SARS (SARS-CoV), a positive-stranded RNA virus within the Coronaviridae family, is mainly transmitted by the respiratory route. In the absence of any efficient treatment, a wide effort is being made to design drugs against this agent. In this context, we have developed a SARS-CoV whole genome approach aimed at determining the crystal structure of all the 28 SARS-CoV proteins. We anticipate that this will greatly facilitate drug design and contribute to fundamental knowledge. The SARS-CoV genome encodes two large replicase polyproteins, which are processed into a set of mature non-structural proteins by internal viral proteases [E. J. Snijder, P. J. Bredenbeek, J. C. Dobbe, V. Thiel, J. Ziebuhr, L. L. M. Poon, Y. Guan, M. Rozanov, W. J. M. Spaan and A. E. Gorbalenya (2003). J. Mol. Biol. 331: 991–1004]. We have crystallized one of the replicase proteins (Nsp9, 113 residues), which diffracts to 2.8 Å resolution.

Valérie Campanacci, Marie-Pierre Egloff, Sonia Longhi, François Ferron, Corinne Rancurel, Aurelia Salomoni, Cécile Durousseau, Fabienne Tocque, Nicolas Brémond, Jessika C. Dobbe, Eric J. Snijder, Bruno Canard and Christian Cambillau