Skip Navigation

This Article
Right arrow Print PDF (932K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (32)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Urakawa, T.
Right arrow Articles by Roy, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Urakawa, T.
Right arrow Articles by Roy, P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1989, Vol. 17, No. 18 7395-7401
© 1989

MOLECULAR BIOLOGY

Expression of targest RNA segment and synthesis of VP1 protein of bluetongue virus in insect cells by recombinant baculovirus: association of VP1 protein with RNA polymerase activity

T. Urakawa1, D. G. Ritter2 and P. Roy1,2,*

1NERC Institute of Virology Mansfield Road, Oxford OX1 3SR, UK 2Department of Environmental Health Sciences, School of Public Health, University of Alabama Birmingham, AL 35294, USA

*To whom correspondence should be addressed

Received July 21, 1989. Revised August 22, 1989. Accepted August 22, 1989.

The bluetongue virus core particles have been shown to contain an RNA- directed RNA polymerase (1). To identify the protein responsible for the virion RNA polymerase activity, the complete 3.9 Kb DNA clone representing the largest RNA segment 1 (L1) of bluetongue virus (BTV-10) was placed under control of the polyhedrin promoter of Autographa californica nuclear polyhedrosis virus (AcNPV). The derived recombinant virus was used to infect Spodoptera frugiperda cells. As demonstrated by stained polyacrylamide gel electrophoresis and by the use of bluetongue virus antibody, infected insect cells synthesized the largest protein of BTV-10 (vP1, 150 k Da). Antibody raised in rabbit to recombinant VP1 protein recognized bluetongue virus VP1 protein. The recombinant virus infected cell lysate had significantly inducible levels of RNA polymerase enzymatic activity as determined by a poly (U)-oligo (A) polymerase assay. The availability of enzymatically active bluetongue virus RNA polymerase provides a system in which we can precisely delineate the role this protein plays in the regulation of bluetongue replication


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Virol.Home page
M. Boyce, J. Wehrfritz, R. Noad, and P. Roy
Purified Recombinant Bluetongue Virus VP1 Exhibits RNA Replicase Activity
J. Virol., April 15, 2004; 78(8): 3994 - 4002.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
A. K. Kar and P. Roy
Defining the Structure-Function Relationships of Bluetongue Virus Helicase Protein VP6
J. Virol., November 1, 2003; 77(21): 11347 - 11356.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. Ramadevi, N. J. Burroughs, P. P. C. Mertens, I. M. Jones, and P. Roy
Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus
PNAS, November 10, 1998; 95(23): 13537 - 13542.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.