J Gen Virol Faster Access
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 Klein, M.
Right arrow Articles by Nelsen-Salz, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klein, M.
Right arrow Articles by Nelsen-Salz, B.
Agricola
Right arrow Articles by Klein, M.
Right arrow Articles by Nelsen-Salz, B.
Journal of General Virology (2000), 81, 895-901.
© 2000 Society for General Microbiology

Animal: RNA Viruses

The picornavirus replication inhibitors HBB and guanidine in the echovirus-9 system: the significance of viral protein 2C

Marcus Klein1, Dirk Hadaschik1, Holger Zimmermannb,1, Hans J. Eggers1 and Birgit Nelsen-Salz1

Institut für Virologie der Universität zu Köln, Fürst-Pückler-Str. 56, 50935 Köln, Germany1

Author for correspondence: Birgit Nelsen-Salz. Fax +49 221 4783902. e-mail birgit.nelsen-salz{at}medizin.uni-koeln.de

HBB [2-({alpha}-hydroxybenzyl)-benzimidazole] and guanidine are potent inhibitors of picornavirus replication. Among other evidence, limited cross-resistance and a synergistic effect of both inhibitors suggest similar but not identical mechanisms of antiviral action. Echovirus-9 variants resistant to each of these drugs were characterized and sequenced. Complete resistance to HBB or guanidine was shown to be due to single but different point mutations in the non-structural protein 2C. Protein 2C was expressed as GST fusion and His-tagged proteins for the wild-type and various mutants. Although three mutations were located in or near conserved NTP binding motifs, NTPase activity was not altered in the presence of HBB or guanidine.




This article has been cited by other articles:


Home page
 J. Virol.Home page
A. M. De Palma, W. Heggermont, K. Lanke, B. Coutard, M. Bergmann, A.-M. Monforte, B. Canard, E. De Clercq, A. Chimirri, G. Purstinger, et al.
The Thiazolobenzimidazole TBZE-029 Inhibits Enterovirus Replication by Targeting a Short Region Immediately Downstream from Motif C in the Nonstructural Protein 2C
J. Virol., May 15, 2008; 82(10): 4720 - 4730.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
G. J. Belsham and P. Normann
Dynamics of picornavirus RNA replication within infected cells
J. Gen. Virol., February 1, 2008; 89(2): 485 - 493.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Microbiol. Rev.Home page
M. J. Grubman and B. Baxt
Foot-and-Mouth Disease
Clin. Microbiol. Rev., April 1, 2004; 17(2): 465 - 493.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
N. Pariente, A. Airaksinen, and E. Domingo
Mutagenesis versus Inhibition in the Efficiency of Extinction of Foot-and-Mouth Disease Virus
J. Virol., June 15, 2003; 77(12): 7131 - 7138.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
M. Klein, H. J. Eggers, and B. Nelsen-Salz
Echovirus-9 protein 2C binds single-stranded RNA unspecifically
J. Gen. Virol., October 1, 2000; 81(10): 2481 - 2484.
[Abstract] [Full Text]


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 © 2000 by the Society for General Microbiology.