HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Joubert, P. Articles by Rasschaert, D. Search for Related Content PubMed PubMed Citation Articles by Joubert, P. Articles by Rasschaert, D. Agricola Articles by Joubert, P. Articles by Rasschaert, D.

Identification of a new cleavage site of the 3C-like protease of rabbit haemorrhagic disease virus

Laboratoire de Virologie et Barrière d’Espèce, Unité de Pathologie Aviaire et de Parasitologie, INRA de Tours, 37380 Nouzilly, France¹
Unité de Virologie et d’Immunologie Moléculaires, INRA, 78350 Jouy-en-Josas, France²

Author for correspondence: Denis Rasschaert. Fax +33 2 47 42 77 74. e-mail rasschae{at}tours.inra.fr

The calicivirus rabbit haemorrhagic disease virus (RHDV) possesses a 3C-like protease which processes the RHDV polyprotein. In order to monitor the proteolytic activity of the RHDV 3C-like protease on its putative target sequences, i.e. the 10 EG dipeptide bonds distributed along the large polyprotein, a new approach was carried out. Preliminary experiments showed that the luciferase gene when fused in-frame with a long gene yielded a fusion protein almost devoid of luciferase activity. This reporter system was used to test which EG dipeptide bonds were cleaved by the RHDV protease when the coding sequences of the dipeptides and their flanking sequences were inserted at the junction between the protease and luciferase genes. The coding sequences of the fusion proteins were cloned downstream of the T7 promoter and the proteolytic activity was evaluated by measuring the luciferase activity in both in vitro and ‘in vivo’ systems. The EG dipeptide bonds at positions 718–719, 1108–1109 and 1767–1768 were confirmed as cleavage sites and a new cleavage site EG (143–144) was identified.

This article has been cited by other articles:

				L. Fragnet, E. Kut, and D. Rasschaert Comparative Functional Study of the Viral Telomerase RNA Based on Natural Mutations J. Biol. Chem., June 24, 2005; 280(25): 23502 - 23515. [Abstract] [Full Text] [PDF]

				L. Fragnet, M. A. Blasco, W. Klapper, and D. Rasschaert The RNA Subunit of Telomerase Is Encoded by Marek's Disease Virus J. Virol., May 15, 2003; 77(10): 5985 - 5996. [Abstract] [Full Text] [PDF]

				J. R. Smiley, K. O. Chang, J. Hayes, J. Vinje, and L. J. Saif Characterization of an Enteropathogenic Bovine Calicivirus Representing a Potentially New Calicivirus Genus J. Virol., October 15, 2002; 76(20): 10089 - 10098. [Abstract] [Full Text] [PDF]

				L. Wei, J. S. Huhn, A. Mory, H. B. Pathak, S. V. Sosnovtsev, K. Y. Green, and C. E. Cameron Proteinase-Polymerase Precursor as the Active Form of Feline Calicivirus RNA-Dependent RNA Polymerase J. Virol., February 1, 2001; 75(3): 1211 - 1219. [Abstract] [Full Text] [PDF]

				F. Dorange, S. El Mehdaoui, C. Pichon, P. Coursaget, and J.-F. Vautherot Marek's disease virus (MDV) homologues of herpes simplex virus type 1 UL49 (VP22) and UL48 (VP16) genes: high-level expression and characterization of MDV-1 VP22 and VP16 J. Gen. Virol., September 1, 2000; 81(9): 2219 - 2230. [Abstract] [Full Text]