PMID: 9525663Apr 3, 1998Paper

Membrane organization of bluetongue virus nonstructural glycoprotein NS3

Journal of Virology
O B BansalP Roy

Abstract

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.

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Citations

Aug 5, 2004·The Journal of Biological Chemistry·Ziying Han, Ronald N Harty
Aug 13, 2010·Journal of Virology·Cheng-Qiang HeHong-Shan Guo
Sep 10, 2014·Viruses·Bjorn-Patrick Mohl, Polly Roy
Nov 23, 2000·Proceedings of the National Academy of Sciences of the United States of America·B StrackH G Gottlinger
Apr 19, 2008·The Journal of General Virology·Melvyn QuanAlan J Guthrie
Sep 1, 2015·Virus Genes·Nirmal ChackoSathish Bhadravati Shivachandra
Apr 17, 2009·Journal of Virology·Cristina C P Celma, Polly Roy
Jun 8, 2012·Journal of Virology·Andrew E ShawFrederick Arnaud
Sep 18, 2002·Proceedings of the National Academy of Sciences of the United States of America·Andrew R BeatonPolly Roy
Jul 17, 2015·The Journal of Veterinary Medical Science·Maho UrataHiroyuki Iwata
Jun 26, 2021·Frontiers in Microbiology·José Manuel RojasNoemí Sevilla

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