HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Gretton, S. N. Articles by McLauchlan, J. Search for Related Content PubMed PubMed Citation Articles by Gretton, S. N. Articles by McLauchlan, J. Agricola Articles by Gretton, S. N. Articles by McLauchlan, J.

Mobility of the hepatitis C virus NS4B protein on the endoplasmic reticulum membrane and membrane-associated foci

Sarah N. Gretton

Annette I. Taylor^,

MRC Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, UK

Correspondence
John McLauchlan
j.mclauchlan{at}vir.gla.ac.uk

The hepatitis C virus (HCV) non-structural protein NS4B induces morphological changes in the endoplasmic reticulum (ER) membrane that may have a direct role in viral RNA replication. A chimeric GFP–NS4B fusion protein located to the ER membrane and to foci that were attached to the ER. These membrane-associated foci (MAFs) could be related to the membrane alterations observed in cells that replicate HCV RNA. The relationship of MAFs to pre-existing cellular structures is not known. Indirect immunofluorescence analysis demonstrated that they did not contain a cellular marker for vesicles, which have been implicated in the replication of other viruses. From photobleaching studies to examine diffusion of NS4B, the GFP-tagged protein had reduced mobility on MAFs compared with on the ER membrane. This slower mobility suggested that NS4B is likely to form different interactions on MAFs and the ER.

These authors contributed equally to this work.

Present address: Ingenza Ltd, King's Buildings, Edinburgh EH9 3JJ, UK.

This article has been cited by other articles:

				M. Tasaka, N. Sakamoto, Y. Itakura, M. Nakagawa, Y. Itsui, Y. Sekine-Osajima, Y. Nishimura-Sakurai, C.-H. Chen, M. Yoneyama, T. Fujita, et al. Hepatitis C virus non-structural proteins responsible for suppression of the RIG-I/Cardif-induced interferon response J. Gen. Virol., December 1, 2007; 88(12): 3323 - 3333. [Abstract] [Full Text] [PDF]

				D. M. Jones, S. N. Gretton, J. McLauchlan, and P. Targett-Adams Mobility analysis of an NS5A-GFP fusion protein in cells actively replicating hepatitis C virus subgenomic RNA J. Gen. Virol., February 1, 2007; 88(2): 470 - 475. [Abstract] [Full Text] [PDF]

				M. Lundin, H. Lindstrom, C. Gronwall, and M. A. A. Persson Dual topology of the processed hepatitis C virus protein NS4B is influenced by the NS5A protein. J. Gen. Virol., November 1, 2006; 87(Pt 11): 3263 - 3272. [Abstract] [Full Text] [PDF]

				I. Umareddy, A. Chao, A. Sampath, F. Gu, and S. G. Vasudevan Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA J. Gen. Virol., September 1, 2006; 87(9): 2605 - 2614. [Abstract] [Full Text] [PDF]

				J. Roosendaal, E. G. Westaway, A. Khromykh, and J. M. Mackenzie Regulated Cleavages at the West Nile Virus NS4A-2K-NS4B Junctions Play a Major Role in Rearranging Cytoplasmic Membranes and Golgi Trafficking of the NS4A Protein J. Virol., May 1, 2006; 80(9): 4623 - 4632. [Abstract] [Full Text] [PDF]