Membrane organization of bluetongue virus nonstructural glycoprotein NS3

被引:46
作者
Bansal, OB
Stokes, A
Bisal, A
Bishop, D
Roy, P
机构
[1] Univ Alabama Birmingham, Sch Publ Hlth, Dept Int Hlth, Birmingham, AL 35294 USA
[2] Univ Oxford, Dept Chem, Oxford, England
[3] Univ Oxford, NERC, Inst Virol & Environm Microbiol, Oxford, England
[4] Univ Oxford St Cross Coll, Oxford OX1 3LZ, England
关键词
D O I
10.1128/JVI.72.4.3362-3369.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The smallest RNA segment (S10) of bluetongue virus (an orboivirus, 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.
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页码:3362 / 3369
页数:8
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