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Journal of Virology, February 2001, p. 1978-1983, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1978-1983.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Rubella Virus E2 Signal Peptide Is Required for Perinuclear Localization of Capsid Protein and Virus Assembly

Lok Man J. Law,1 Robert Duncan,2 Ali Esmaili,2 Hira L. Nakhasi,2 and Tom C. Hobman*,1

Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada,1 and Laboratory of Bacterial, Parasitic, and Unconventional Agents, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 208922

Received 5 September 2000/Accepted 9 November 2000

The rubella virus (RV) structural proteins capsid, E2, and E1 are synthesized as a polyprotein precursor. The signal peptide that initiates translocation of E2 into the lumen of the endoplasmic reticulum remains attached to the carboxy terminus of the capsid protein after cleavage by signal peptidase. Among togaviruses, this feature is unique to RV. The E2 signal peptide has previously been shown to function as a membrane anchor for the capsid protein. In the present study, we demonstrate that this domain is required for RV glycoprotein-dependent localization of the capsid protein to the juxtanuclear region and subsequent virus assembly at the Golgi complex.

* Corresponding author. Mailing address: Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Phone: (780) 492-6485. Fax: (780) 492-0450. E-mail: tom.hobman{at}ualberta.ca.

Journal of Virology, February 2001, p. 1978-1983, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1978-1983.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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