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


     

J Gen Virol 78 (1997), 2153-2157
© 1997 Society for General Microbiology
This Article
Right arrow Full Text (PDF)
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 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 McMillan, D. J.
Right arrow Articles by Mills, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McMillan, D. J.
Right arrow Articles by Mills, J. S.
Agricola
Right arrow Articles by McMillan, D. J.
Right arrow Articles by Mills, J. S.

Journal of General Virology, Vol 78, 2153-2157, Copyright © 1997 by Society for General Microbiology

ARTICLES

Characterization of the proteinase specified by varicella-zoster virus gene 33

DJ McMillan, J Kay and JS Mills
Department of Biology, Roche Discovery Welwyn, UK. David.Mc_millan@Roche.com

Varicella-zoster virus (VZV) genes 33 and 33.5 are predicted to encode the VZV proteinase and its substrate (the assembly protein) respectively. These genes were expressed in insect cells using recombinant baculovirus and it was confirmed that gene 33 encodes a proteinase capable of autoproteolytic processing at two positions. When VZV gene 33.5 was co-expressed with the VZV proteinase, processing of the VZV33.5 gene product was observed. A polyclonal antiserum to the VZV assembly protein domain highlighted a set of proteins in VZV infected HEL cells identical to those identified in insect cells expressing VZV genes 33 and 33.5. To facilitate further characterization of the VZV proteinase the enzyme was purified by affinity chromatography from an E. coli expression system and in vitro activity was observed.


This article has been cited by other articles:


Home page
 J. Gen. Virol.Home page
P. G. E. Kennedy, E. Grinfeld, M. Craigon, K. Vierlinger, D. Roy, T. Forster, and P. Ghazal
Transcriptomal analysis of varicella-zoster virus infection using long oligonucleotide-based microarrays
J. Gen. Virol., October 1, 2005; 86(10): 2673 - 2684.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
R. J. Cohrs, M. P. Hurley, and D. H. Gilden
Array Analysis of Viral Gene Transcription during Lytic Infection of Cells in Tissue Culture with Varicella-Zoster Virus
J. Virol., November 1, 2003; 77(21): 11718 - 11732.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. J. Tigue and J. Kay
Autoprocessing and Peptide Substrates for Human Herpesvirus 6 Proteinase
J. Biol. Chem., October 9, 1998; 273(41): 26441 - 26446.
[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 © 1997 by the Society for General Microbiology.