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 Roudet-Tavert, G. Articles by Le Gall, O. Search for Related Content PubMed PubMed Citation Articles by Roudet-Tavert, G. Articles by Le Gall, O. Agricola Articles by Roudet-Tavert, G. Articles by Le Gall, O.

Interaction between potyvirus helper component-proteinase and capsid protein in infected plants

Virologie Végétale, UMR GDPP, Institut de Biologie Végétale Moléculaire, INRA, BP 81, 33883 Villenave d’Ornon Cedex, France¹

Author for correspondence: Geneviève Roudet-Tavert. Fax +33 557 122 384. e-mail groudet{at}bordeaux.inra.fr

Monoclonal antibodies were raised against helper component-proteinase (HcPro) purified from plants infected with the potyvirus Lettuce mosaic virus (LMV). These antibodies were used in a two-site triple antibody sandwich ELISA assay together with polyclonal antibodies directed against purified virions. An interaction between HcPro and the viral coat protein (CP) was demonstrated in extracts of LMV-infected leaves, as well as for two other potyviruses, Plum pox virus and Potato virus Y. The CP–HcPro interaction was not abolished in LMV derivatives with an HcPro GFP N-terminal fusion, or with a deletion from the CP of the amino acids involved in aphid transmission. Electron microscopy indicated that HcPro probably does not interact with the CP in the form of assembled virions or virus-like particles. Together, these results suggest that the interaction detected between CP and HcPro might be involved in a process of the potyvirus cycle different from aphid transmission.

This article has been cited by other articles:

				G. Roudet-Tavert, T. Michon, J. Walter, T. Delaunay, E. Redondo, and O. Le Gall Central domain of a potyvirus VPg is involved in the interaction with the host translation initiation factor eIF4E and the viral protein HcPro J. Gen. Virol., March 1, 2007; 88(3): 1029 - 1033. [Abstract] [Full Text] [PDF]

				F. Aparicio, J. A. Sanchez-Navarro, and V. Pallas In vitro and in vivo mapping of the Prunus necrotic ringspot virus coat protein C-terminal dimerization domain by bimolecular fluorescence complementation J. Gen. Virol., June 1, 2006; 87(6): 1745 - 1750. [Abstract] [Full Text] [PDF]

				L. Ballut, M. Drucker, M. Pugniere, F. Cambon, S. Blanc, F. Roquet, T. Candresse, H.-P. Schmid, P. Nicolas, O. L. Gall, et al. HcPro, a multifunctional protein encoded by a plant RNA virus, targets the 20S proteasome and affects its enzymic activities J. Gen. Virol., September 1, 2005; 86(9): 2595 - 2603. [Abstract] [Full Text] [PDF]

				V. Ruiz-Ferrer, J. Boskovic, C. Alfonso, G. Rivas, O. Llorca, D. Lopez-Abella, and J. J. Lopez-Moya Structural Analysis of Tobacco Etch Potyvirus HC-Pro Oligomers Involved in Aphid Transmission J. Virol., March 15, 2005; 79(6): 3758 - 3765. [Abstract] [Full Text] [PDF]

				V. Paalme, E. Gammelgard, L. Jarvekulg, and J. P. T. Valkonen In vitro recombinants of two nearly identical potyviral isolates express novel virulence and symptom phenotypes in plants J. Gen. Virol., March 1, 2004; 85(3): 739 - 747. [Abstract] [Full Text] [PDF]

				C. Plisson, M. Drucker, S. Blanc, S. German-Retana, O. Le Gall, D. Thomas, and P. Bron Structural Characterization of HC-Pro, a Plant Virus Multifunctional Protein J. Biol. Chem., June 20, 2003; 278(26): 23753 - 23761. [Abstract] [Full Text] [PDF]