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Journal of Virology, April 2007, p. 4298-4304, Vol. 81, No. 8
0022-538X/07/$08.00+0 doi:10.1128/JVI.02239-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom,1 Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom2
Received 12 October 2006/ Accepted 27 December 2006
The nucleocapsid (N) protein of infectious bronchitis virus (IBV) localizes to the cytoplasm and nucleolus and contains an eight-amino-acid nucleolar retention motif. In this study, a leucine-rich nuclear export signal (NES) (291-LQLDGLHL-298) present in the C-terminal region of the IBV N protein was analyzed by using alanine substitution and deletion mutagenesis to investigate the relative contributions that leucine residues make to nuclear export and where these residues are located on the structure of the IBV N protein. The analysis indicated that Leu296 and Leu298 are required for efficient nuclear export of the protein. Structural information indicated that both of these amino acids are available for interaction with protein complexes involved in this process. However, export of N protein from the nucleus/nucleolus was not inhibited by leptomycin B treatment, indicating that N protein nuclear export is independent of the CRM1-mediated export pathway.
Published ahead of print on 3 January 2007.
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