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Journal of Virology, July 2006, p. 6612-6620, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.00157-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

X-Ray Structures of the N- and C-Terminal Domains of a Coronavirus Nucleocapsid Protein: Implications for Nucleocapsid Formation

Hariharan Jayaram,1,{dagger} Hui Fan,2 Brian R. Bowman,1,{ddagger} Amy Ooi,2 Jyothi Jayaram,3 Ellen W. Collisson,3 Julien Lescar,2* and B. V. Venkataram Prasad1*

Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030,1 School of Biological Sciences, Nanyang Technological University, Singapore 637551,2 Department of Veterinary Pathobiology, Texas A&M University, College Station, Texas 778433

Received 23 January 2006/ Accepted 10 April 2006

Coronaviruses cause a variety of respiratory and enteric diseases in animals and humans including severe acute respiratory syndrome. In these enveloped viruses, the filamentous nucleocapsid is formed by the association of nucleocapsid (N) protein with single-stranded viral RNA. The N protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. We describe the structure of the two proteolytically resistant domains of the N protein from infectious bronchitis virus (IBV), a prototype coronavirus. These domains are located at its N- and C-terminal ends (NTD and CTD, respectively). The NTD of the IBV Gray strain at 1.3-Å resolution exhibits a U-shaped structure, with two arms rich in basic residues, providing a module for specific interaction with RNA. The CTD forms a tightly intertwined dimer with an intermolecular four-stranded central ß-sheet platform flanked by {alpha} helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein. The variety of quaternary arrangements of the NTD and CTD revealed by the analysis of the different crystal forms delineates possible interfaces that could be used for the formation of a flexible filamentous ribonucleocapsid. The striking similarity between the dimeric structure of CTD and the nucleocapsid-forming domain of a distantly related arterivirus indicates a conserved mechanism of nucleocapsid formation for these two viral families.

* Corresponding author. Mailing address for B. V. V. Prasad: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030-3498. Phone: (713) 798-5686. Fax: (713) 798-1625. E-mail: vprasad{at}bcm.tmc.edu. Mailing address for J. Lescar: School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551. Phone: 65-6316-2859. Fax: 65-6791-3856. E-mail: julien{at}ntu.edu.sg.

{dagger} Present address: Howard Hughes Medical Institute and the Department of Biochemistry, Brandeis University, Waltham, MA 02454.

{ddagger} Present address: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

Journal of Virology, July 2006, p. 6612-6620, Vol. 80, No. 13
0022-538X/06/$08.00+0     doi:10.1128/JVI.00157-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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