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J Virol, April 1998, p. 3362-3369, Vol. 72, No. 4
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Membrane Organization of Bluetongue Virus Nonstructural Glycoprotein NS3

Om B. Bansal,1 Ann Stokes,1,2 Anju Bansal,1 David Bishop,3 and Polly Roy1,2,*

Department of International Health, University of Alabama at Birmingham, Birmingham, Alabama,1 and Department of Biochemistry and NERC Institute of Virology and Environmental Microbiology2 and St. Cross College,3 University of Oxford, Oxford, United Kingdom

Received 20 June 1997/Accepted 24 December 1997

The smallest RNA segment (S10) of bluetongue virus (an orbivirus, family Reoviridae) encodes two closely related nonstructural proteins, the 229-amino-acid (aa) NS3 and the 216-aa NS3A. The proteins are found in glycosylated and nonglycosylated forms in infected cells (X. Wu, H. Iwata, S.-Y. Chen, R. W. Compans and P. Roy J. Virol. 66:7104-7112, 1992). The NS3/NS3A proteins have two hydrophobic domains (aa 118 to 141 and 162 to 182) and two potential asparagine-linked glycosylation sites (aa 63 and 150), one of which is located between the hydrophobic domains. To determine whether these features were used in the mature protein forms, we generated a series of mutants of the S10 gene and expressed them by using the vaccinia virus T7 polymerase transient-expression system. Our data indicate that both hydrophobic domains of NS3 span the cell membrane and that only the site at aa 150 is responsible for N-linked glycosylation of the NS3 proteins.

* Corresponding author. Mailing address: 308 TH, Department of International Health, School of Public Health, University of Alabama at Birmingham, Birmingham, AL 35294. Phone: (205) 934-6098. Fax: (205) 934-0639. E-mail: por{at}mail.nox.ac.uk.




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