J Gen Virol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 84 (2003), 2317-2322; DOI 10.1099/vir.0.19297-0

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tijms, M. A.
Right arrow Articles by Snijder, E. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tijms, M. A.
Right arrow Articles by Snijder, E. J.
Agricola
Right arrow Articles by Tijms, M. A.
Right arrow Articles by Snijder, E. J.
© 2003 Society for General Microbiology

Short Communication

Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100

Marieke A. Tijms and Eric J. Snijder

Molecular Virology Laboratory, Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, LUMC E4-P, PO Box 9600, 2300 RC Leiden, The Netherlands

Correspondence
Eric Snijder
E.J.Snijder{at}LUMC.NL

Non-structural protein 1 (nsp1), the N-terminal subunit of the replicase polyprotein of the arterivirus Equine arteritis virus (EAV), is essential for viral subgenomic mRNA synthesis, but fully dispensable for genome replication. However, at the molecular level, the role of nsp1 in EAV subgenomic mRNA synthesis is poorly understood. A yeast two-hybrid screen did not reveal interactions between EAV nsp1 and other viral non-structural proteins or the nucleocapsid protein, although both nsp1 and the nucleocapsid protein were found to form homomers. Subsequently, a yeast two-hybrid screen of a HeLa cell cDNA library was performed using nsp1 as bait. Remarkably, this analysis revealed (potential) interactions between EAV nsp1 and factors that are involved in host cell transcriptional regulation. The interaction of nsp1 with one of these proteins, p100, a transcription co-activator that also interacts with regulatory proteins of other viruses, was confirmed by mutual co-immunoprecipitation from lysates of EAV-susceptible mammalian cells.




This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
C. R. Johnson, W. Yu, and M. P. Murtaugh
Cross-reactive antibody responses to nsp1 and nsp2 of Porcine reproductive and respiratory syndrome virus
J. Gen. Virol., April 1, 2007; 88(4): 1184 - 1195.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
W. Peti, M. A. Johnson, T. Herrmann, B. W. Neuman, M. J. Buchmeier, M. Nelson, J. Joseph, R. Page, R. C. Stevens, P. Kuhn, et al.
Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7
J. Virol., October 15, 2005; 79(20): 12905 - 12913.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. M. Brockway, X. T. Lu, T. R. Peters, T. S. Dermody, and M. R. Denison
Intracellular Localization and Protein Interactions of the Gene 1 Protein p28 during Mouse Hepatitis Virus Replication
J. Virol., November 1, 2004; 78(21): 11551 - 11562.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2003 by the Society for General Microbiology.