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


     

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 Cottone, R.
Right arrow Articles by Rziha, H.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cottone, R.
Right arrow Articles by Rziha, H.-J.
Agricola
Right arrow Articles by Cottone, R.
Right arrow Articles by Rziha, H.-J.
Journal of General Virology (2002), 83, 1043-1048.
© 2002 Society for General Microbiology

Animal: DNA Viruses

Orf virus encodes a functional dUTPase gene

R. Cottone1, M. Büttner1, C. J. McInnes2, A. R. Wood2 and H.-J. Rziha1

Federal Research Centre for Virus Diseases of Animals, Institute for Immunology, Paul-Ehrlich-Straße 28, D-72076 Tübingen, Federal Republic of Germany1
Moredun Research Institute, International Research Centre, Pentlands Science Park, Penicuik, Midlothian EH26 OPZ, UK2

Author for correspondence: Hanns-Joachim Rziha. Fax +49 7071 967 303. e-mail achim.rziha{at}tue.bfav.de

The present study is the first report on the functional activity of a parapoxvirus-encoded dUTPase. The dUTPase gene of the attenuated orf virus (ORFV), strain D1701, was expressed as a bacterial thioredoxin fusion protein. In vitro assays showed that ORFV dUTPase was highly specific for dUTP as substrate. The enzyme was active over a broad pH range (pH 6·0–9·0), with maximal enzymatic activity at pH 7·0 in the presence of Mg2+ cations. Kinetic studies of the recombinant ORFV dUTPase revealed an apparent Km of 4·0 µM, which is more similar to that of the mammalian or African swine fever virus enzyme than to the Km of vaccinia virus dUTPase. Enzyme activity was also found with purified ORFV particles, indicating its virion association.




This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
A. R. Wood and C. J. McInnes
Transcript mapping of the 'early' genes of Orf virus
J. Gen. Virol., November 1, 2003; 84(11): 2993 - 2998.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
H.-J. Rziha, B. Bauer, K.-H. Adam, M. Rottgen, R. Cottone, M. Henkel, C. Dehio, and M. Buttner
Relatedness and heterogeneity at the near-terminal end of the genome of a parapoxvirus bovis 1 strain (B177) compared with parapoxvirus ovis (Orf virus)
J. Gen. Virol., May 1, 2003; 84(5): 1111 - 1116.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
R. Chen, H. Wang, and L. M. Mansky
Roles of uracil-DNA glycosylase and dUTPase in virus replication
J. Gen. Virol., October 1, 2002; 83(10): 2339 - 2345.
[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 © 2002 by the Society for General Microbiology.